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Published in: Drugs 3/2000

01-03-2000 | Review Article

Kinase Inhibitors in Cancer Therapy

A Look Ahead

Author: Dr H. H. Sedlacek

Published in: Drugs | Issue 3/2000

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Abstract

The most essential kinases involved in cell membrane receptor activation, signal transduction and cell cycle control or programmed cell death and their interconections are reviewed. In tumours, the genes of many of those kinases are mutated or amplified or the proteins are overexpressed.
The use of key kinases offers the possibility to screen in vitro for synthetic small molecule kinase inhibitors. In view of the many interconnections of cellular kinases, their role in preventing or inducing programmed cell death and the possibility that a considerable number of signal transducing proteins are still unknown, cellular test systems are recommended in which the respective key kinase or one of its main partner molecules are overexpressed.
Literature
1.
go back to reference Denn WA, Smaill JB, Fry DW, et al. Structure-activity relationships for 4-anilinoquinazoline and related pyridopyrimidine acrylamides as specific, irreversible inhibitors of the ATP site of the epidermal growth factor receptor [abstract]. Proc Am Assoc Cancer Res 1998; 39: 559 Denn WA, Smaill JB, Fry DW, et al. Structure-activity relationships for 4-anilinoquinazoline and related pyridopyrimidine acrylamides as specific, irreversible inhibitors of the ATP site of the epidermal growth factor receptor [abstract]. Proc Am Assoc Cancer Res 1998; 39: 559
2.
go back to reference Hanks SK, Hunter T. The eukaryotic protein kinase superfamily. In: Hardie G, Hanks S, editors. The protein kinase facts book. New York: Academic Press, 1995; 7: 7–47CrossRef Hanks SK, Hunter T. The eukaryotic protein kinase superfamily. In: Hardie G, Hanks S, editors. The protein kinase facts book. New York: Academic Press, 1995; 7: 7–47CrossRef
3.
go back to reference Sedlacek HH, Hoffmann D, Schulz G, et al. The chemotherapy of malignant diseases: research perspectives. In: Sedlacek HH, Hoffmann D, Schulz G, et al., editors. Contributions to Oncology No. 34. München: Karger Verlag, 1989 Sedlacek HH, Hoffmann D, Schulz G, et al. The chemotherapy of malignant diseases: research perspectives. In: Sedlacek HH, Hoffmann D, Schulz G, et al., editors. Contributions to Oncology No. 34. München: Karger Verlag, 1989
4.
go back to reference Plowman GD, Green JM, Culouscou JM, et al. Heregulin induces tyrosine phosphorylation of HER4/P180 (erbB4). Nature 1993; 366: 473–5PubMedCrossRef Plowman GD, Green JM, Culouscou JM, et al. Heregulin induces tyrosine phosphorylation of HER4/P180 (erbB4). Nature 1993; 366: 473–5PubMedCrossRef
5.
go back to reference Pusztal L, Lewis CE, Lorenzen J, et al. Growth factors: regulation of normal and neoplastic growth. J Pathol 1993; 169: 191–201CrossRef Pusztal L, Lewis CE, Lorenzen J, et al. Growth factors: regulation of normal and neoplastic growth. J Pathol 1993; 169: 191–201CrossRef
6.
go back to reference Boyle WJ. Growth factors and tyrosine kinase receptors during development and cancer. Curr Opin Oncol 1992; 4: 156–62PubMedCrossRef Boyle WJ. Growth factors and tyrosine kinase receptors during development and cancer. Curr Opin Oncol 1992; 4: 156–62PubMedCrossRef
7.
go back to reference Boulikas T. The phosphorylation connection to cancer (review). Int J Oncol 1995; 6: 271–8PubMed Boulikas T. The phosphorylation connection to cancer (review). Int J Oncol 1995; 6: 271–8PubMed
8.
go back to reference Cohen S, Ushiro H, Stoscheck C, et al. A native 170 000 epidermal growth factor receptor-kinase complex from shed plasma membrane vesicles. J Biol Chem 1982; 257: 1523–31PubMed Cohen S, Ushiro H, Stoscheck C, et al. A native 170 000 epidermal growth factor receptor-kinase complex from shed plasma membrane vesicles. J Biol Chem 1982; 257: 1523–31PubMed
9.
go back to reference Gale NW, Kaplan S, Lowenstein EJ, et al. Grb2 mediates the EGF-dependent activation of guanine nucleotide exchange on Ras. Nature 1993; 363: 88–90PubMedCrossRef Gale NW, Kaplan S, Lowenstein EJ, et al. Grb2 mediates the EGF-dependent activation of guanine nucleotide exchange on Ras. Nature 1993; 363: 88–90PubMedCrossRef
10.
go back to reference Li X, Liu J, Park JK, et al. T cells from renal cell carcinoma patients exhibit an abnormal pattern of kappa B-specific DNA-binding activity: a preliminary report. Cancer Res 1994; 54: 5424–9PubMed Li X, Liu J, Park JK, et al. T cells from renal cell carcinoma patients exhibit an abnormal pattern of kappa B-specific DNA-binding activity: a preliminary report. Cancer Res 1994; 54: 5424–9PubMed
11.
go back to reference Medema RH, De Vries-Smits AMM, Van Der Zon GCM, et al. Ras activation by insulin and epidermal growth factor through enhanced exchange of guanine nucleotides on p21ras. Mol Cell Biol 1993; 13: 155–62PubMed Medema RH, De Vries-Smits AMM, Van Der Zon GCM, et al. Ras activation by insulin and epidermal growth factor through enhanced exchange of guanine nucleotides on p21ras. Mol Cell Biol 1993; 13: 155–62PubMed
12.
go back to reference Ellis C, Moran M, McCormick F, et al. Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases. Nature 1990; 343: 377–81PubMedCrossRef Ellis C, Moran M, McCormick F, et al. Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases. Nature 1990; 343: 377–81PubMedCrossRef
13.
go back to reference Fisher DA, Lakshmanan J. Metabolism and the effects of epidermal growth factor and related growth factors in mammals. Endocr Rev 1990 11: 418–45PubMedCrossRef Fisher DA, Lakshmanan J. Metabolism and the effects of epidermal growth factor and related growth factors in mammals. Endocr Rev 1990 11: 418–45PubMedCrossRef
14.
go back to reference Velu TJ, Beguinot L, Vass WC, et al. Epidermal growth factor dependent transformation by a human EGF receptor protooncogene. Science 1987; 238: 1408–10PubMedCrossRef Velu TJ, Beguinot L, Vass WC, et al. Epidermal growth factor dependent transformation by a human EGF receptor protooncogene. Science 1987; 238: 1408–10PubMedCrossRef
15.
go back to reference Downward J, Yarden Y, Mayes E, et al. Close similarity of epidermal growth factor receptor and v-erbB oncogene protein sequence. Nature 1984; 307: 521–7PubMedCrossRef Downward J, Yarden Y, Mayes E, et al. Close similarity of epidermal growth factor receptor and v-erbB oncogene protein sequence. Nature 1984; 307: 521–7PubMedCrossRef
16.
go back to reference Fitzpatrick SL, Brightwell J, Wittliff J, et al. Epidermal growth factor binding by breast tumor biopsies and relationship to estrogen and progestin receptor levels. Cancer Res 1984; 44: 3448–53PubMed Fitzpatrick SL, Brightwell J, Wittliff J, et al. Epidermal growth factor binding by breast tumor biopsies and relationship to estrogen and progestin receptor levels. Cancer Res 1984; 44: 3448–53PubMed
17.
go back to reference Klijn JGM, Berns PMJJ, Schmitz PIM, et al. The clinical significance of epidermal growth factor receptor (EGF-R) in human breast cancer: a review on 5232 patients. Endocr Rev 1992; 13: 3–15PubMed Klijn JGM, Berns PMJJ, Schmitz PIM, et al. The clinical significance of epidermal growth factor receptor (EGF-R) in human breast cancer: a review on 5232 patients. Endocr Rev 1992; 13: 3–15PubMed
18.
go back to reference Salomon DS, Brandt R, Ciardiello F, et al. Epidermal growth factor-related peptides and their receptors in human malignancies. Crit Rev Oncol 1995; 19: 183–232CrossRef Salomon DS, Brandt R, Ciardiello F, et al. Epidermal growth factor-related peptides and their receptors in human malignancies. Crit Rev Oncol 1995; 19: 183–232CrossRef
19.
go back to reference Khazaie K, Schirrmacher V, Lichtner R. EGF receptor in neoplasia and metastasis. Cancer Metast Rev 1993; 12: 255–74CrossRef Khazaie K, Schirrmacher V, Lichtner R. EGF receptor in neoplasia and metastasis. Cancer Metast Rev 1993; 12: 255–74CrossRef
20.
21.
go back to reference Fekete M, Wittliff JL, Schally AV Characteristics and distribution of receptors for [D-Trp6]-luteinizing hormone-releasing hormone, somatostatin, epidermal growth factor and sex steroids in 500 biopsy samples of human breast cancer. J Clin Lab Anal 1989; 3: 137–47PubMedCrossRef Fekete M, Wittliff JL, Schally AV Characteristics and distribution of receptors for [D-Trp6]-luteinizing hormone-releasing hormone, somatostatin, epidermal growth factor and sex steroids in 500 biopsy samples of human breast cancer. J Clin Lab Anal 1989; 3: 137–47PubMedCrossRef
22.
go back to reference Srkalovic G, Wittliff JL, Schally AV. Detection and partial characterization of receptors for [D-Trp6]-luteinizing hormone-releasing hormone and epidermal growth factor in human endometrial carcinoma. Cancer Res 1990; 50: 1841–6PubMed Srkalovic G, Wittliff JL, Schally AV. Detection and partial characterization of receptors for [D-Trp6]-luteinizing hormone-releasing hormone and epidermal growth factor in human endometrial carcinoma. Cancer Res 1990; 50: 1841–6PubMed
23.
go back to reference Korc M, Meltzer P, Trent J. Enhanced expression of epidermal growth factor receptor correlates with alterations of chromosome 7 in human pancreatic cancer. Proc Natl Acad Sci U S A 1986; 83: 5141–4PubMedCrossRef Korc M, Meltzer P, Trent J. Enhanced expression of epidermal growth factor receptor correlates with alterations of chromosome 7 in human pancreatic cancer. Proc Natl Acad Sci U S A 1986; 83: 5141–4PubMedCrossRef
24.
go back to reference Yamazaki H, Ohba Y, Tamaoki N, et al. A deletion mutation within the ligand binding domain is responsible for activation of epidermal growth factor gene in human brain tumors. Jpn J Cancer Res 1990; 81: 773–9PubMedCrossRef Yamazaki H, Ohba Y, Tamaoki N, et al. A deletion mutation within the ligand binding domain is responsible for activation of epidermal growth factor gene in human brain tumors. Jpn J Cancer Res 1990; 81: 773–9PubMedCrossRef
25.
go back to reference Moscatello DK, Holgado-Madruga M, Godwin AK, et al. Frequent expression of a mutant epidermal growth factor receptor in multiple human tumors. Cancer Res 1995; 55: 5536–9PubMed Moscatello DK, Holgado-Madruga M, Godwin AK, et al. Frequent expression of a mutant epidermal growth factor receptor in multiple human tumors. Cancer Res 1995; 55: 5536–9PubMed
26.
go back to reference Wickstrand CJ, Hale LP, Batra SK, et al. Monoclonal antibodies against EGFRvIII are tumor specific and react with breast and lung carcinomas and malignant gliomas. Cancer Res 1995; 55: 3140–8 Wickstrand CJ, Hale LP, Batra SK, et al. Monoclonal antibodies against EGFRvIII are tumor specific and react with breast and lung carcinomas and malignant gliomas. Cancer Res 1995; 55: 3140–8
27.
go back to reference Myers MG, Sun XJ, Cheatham B, et al. IRS-1 is a common element in insulin and insulin-like growth factor-I signalling to the phosphatidylinositol 3′-kinase. Endocrinol 1993; 132: 1421–30CrossRef Myers MG, Sun XJ, Cheatham B, et al. IRS-1 is a common element in insulin and insulin-like growth factor-I signalling to the phosphatidylinositol 3′-kinase. Endocrinol 1993; 132: 1421–30CrossRef
28.
go back to reference Kern JA, Schwartz DA, Nordberg JE, et al. p185neu expression in human lung adenocarcinomas predicts shortened survival. Cancer Res 1990; 50: 5184–8PubMed Kern JA, Schwartz DA, Nordberg JE, et al. p185neu expression in human lung adenocarcinomas predicts shortened survival. Cancer Res 1990; 50: 5184–8PubMed
29.
go back to reference Hall PA, Hughes CM, Staddon SL, et al. The c-erb B-2 protooncogene in human pancreatic cancer. J Pathol 1990; 161: 195–200PubMedCrossRef Hall PA, Hughes CM, Staddon SL, et al. The c-erb B-2 protooncogene in human pancreatic cancer. J Pathol 1990; 161: 195–200PubMedCrossRef
30.
go back to reference Berchuck A, Rodriguez G, Kinney RB, et al. Overexpression of HER-2/neu in endometrial cancer is associated with advanced stage disease. Am J Obstet Gynecol 1991; 164: 15–21PubMed Berchuck A, Rodriguez G, Kinney RB, et al. Overexpression of HER-2/neu in endometrial cancer is associated with advanced stage disease. Am J Obstet Gynecol 1991; 164: 15–21PubMed
31.
go back to reference Bergman CL, Hung MC, Weinberg RA. Multiple independent activation of the neu oncogene by point mutations altering the transmembrane domain of p 185. Cell 1984; 46: 649–57 Bergman CL, Hung MC, Weinberg RA. Multiple independent activation of the neu oncogene by point mutations altering the transmembrane domain of p 185. Cell 1984; 46: 649–57
32.
go back to reference Radinsky R. Paracrine growth regulation of human colon carcinoma organ-specific metastasis. Cancer Metast Rev 1993; 12: 345–61CrossRef Radinsky R. Paracrine growth regulation of human colon carcinoma organ-specific metastasis. Cancer Metast Rev 1993; 12: 345–61CrossRef
33.
go back to reference Kobrin MS, Yamanaka Y, Friess H, et al. Aberrant expression of the type I fibroblast growth factor receptor in human pancreatic adenocarcinomas. Cancer Res 1993; 53: 4741–4PubMed Kobrin MS, Yamanaka Y, Friess H, et al. Aberrant expression of the type I fibroblast growth factor receptor in human pancreatic adenocarcinomas. Cancer Res 1993; 53: 4741–4PubMed
34.
go back to reference Rudland PS, Fernig DG, Smith JA. Growth factors and their receptors in neoplastic mammary glands. Biomed Pharmacother 1995; 49: 389–99PubMedCrossRef Rudland PS, Fernig DG, Smith JA. Growth factors and their receptors in neoplastic mammary glands. Biomed Pharmacother 1995; 49: 389–99PubMedCrossRef
35.
go back to reference Kato J, Wanebo H, Calabresi P, et al. Basic fibroblast growth factor production and growth factor receptors as potential targets for melanoma therapy. Melanoma Res 1992; 2: 13–23PubMedCrossRef Kato J, Wanebo H, Calabresi P, et al. Basic fibroblast growth factor production and growth factor receptors as potential targets for melanoma therapy. Melanoma Res 1992; 2: 13–23PubMedCrossRef
36.
go back to reference Shih IM, Herlyn M. Autocrine and paracrine roles for growth factors in melanoma. In Vivo 1994; 8: 113–24PubMed Shih IM, Herlyn M. Autocrine and paracrine roles for growth factors in melanoma. In Vivo 1994; 8: 113–24PubMed
37.
go back to reference Helle SI, Lonning PE. Insulin-like growth factors in breast and prostatic cancer. Endocr Relat Cancer 1995; 2: 153–69CrossRef Helle SI, Lonning PE. Insulin-like growth factors in breast and prostatic cancer. Endocr Relat Cancer 1995; 2: 153–69CrossRef
39.
go back to reference Bergmann U, Funtomi H, Yokoyama M, et al. Insulin-like growth factor I overexpression in human pancreatic cancer: evidence for autocrine and paracrine roles. Cancer Res 1995; 55: 2007–11PubMed Bergmann U, Funtomi H, Yokoyama M, et al. Insulin-like growth factor I overexpression in human pancreatic cancer: evidence for autocrine and paracrine roles. Cancer Res 1995; 55: 2007–11PubMed
40.
go back to reference Baserga R. Controlling IGF-receptor function: a possible strategy for tumor therapy. Tibtech 1996; 14: 150CrossRef Baserga R. Controlling IGF-receptor function: a possible strategy for tumor therapy. Tibtech 1996; 14: 150CrossRef
41.
go back to reference Tanaka S, Wands JR. Insulin receptor substrate 1 overexpression in human hepatocellular carcinoma cells prevents transforming growth factor ß1-induced apoptosis. Cancer Res 1996; 56: 3391–4PubMed Tanaka S, Wands JR. Insulin receptor substrate 1 overexpression in human hepatocellular carcinoma cells prevents transforming growth factor ß1-induced apoptosis. Cancer Res 1996; 56: 3391–4PubMed
42.
go back to reference Ware JL. Growth factors and their receptors as determinants in the proliferation and metastasis of human prostate cancer. Cancer Metast Rev 1993; 12: 287–301CrossRef Ware JL. Growth factors and their receptors as determinants in the proliferation and metastasis of human prostate cancer. Cancer Metast Rev 1993; 12: 287–301CrossRef
43.
go back to reference Rodeck U, Herlyn M, Menssen HD, et al. Metastatic but not primary melanoma cells grow in vitro independently of exogenous growth factors. Int J Cancer 1987; 40: 687–90PubMedCrossRef Rodeck U, Herlyn M, Menssen HD, et al. Metastatic but not primary melanoma cells grow in vitro independently of exogenous growth factors. Int J Cancer 1987; 40: 687–90PubMedCrossRef
44.
go back to reference Lee AV, Yee D. Insulin-like growth factors and breast cancer. Biomed Pharmacother 1995; 49: 415–21PubMedCrossRef Lee AV, Yee D. Insulin-like growth factors and breast cancer. Biomed Pharmacother 1995; 49: 415–21PubMedCrossRef
45.
go back to reference Moody TW, Guttitta F. Growth factor and peptide receptors in small cell lung cancer. Life Sci 1993; 52: 1161–73PubMedCrossRef Moody TW, Guttitta F. Growth factor and peptide receptors in small cell lung cancer. Life Sci 1993; 52: 1161–73PubMedCrossRef
46.
go back to reference Rubin R, Baserga R. Insulin-like growth factor-I receptor: its role in cell proliferation, apoptosis, and tumorigenicity. Lab Invest 1995; 73: 311–31PubMed Rubin R, Baserga R. Insulin-like growth factor-I receptor: its role in cell proliferation, apoptosis, and tumorigenicity. Lab Invest 1995; 73: 311–31PubMed
47.
go back to reference Ponzetto C, Giordano S, Della Valle G, et al. c-met is amplified but not mutated in a cell line with an activated met tyrosine kinase. Oncogene 1991; 6: 553–9PubMed Ponzetto C, Giordano S, Della Valle G, et al. c-met is amplified but not mutated in a cell line with an activated met tyrosine kinase. Oncogene 1991; 6: 553–9PubMed
48.
go back to reference Halaban R, Rubin JS, Funasaka Y, et al. Met and hepatocyte growth factor/scatter factor signal transduction in normal melanocytes and melanoma cells. Oncogene 1992; 7: 2195–206PubMed Halaban R, Rubin JS, Funasaka Y, et al. Met and hepatocyte growth factor/scatter factor signal transduction in normal melanocytes and melanoma cells. Oncogene 1992; 7: 2195–206PubMed
49.
go back to reference DiRenzo MF, Poulsom R, Olivero M, et al. Expression of the met/hepatocyte growth factor receptor in human pancreatic cancer. Cancer Res 1995; 55: 1129–38 DiRenzo MF, Poulsom R, Olivero M, et al. Expression of the met/hepatocyte growth factor receptor in human pancreatic cancer. Cancer Res 1995; 55: 1129–38
50.
go back to reference DiRenzo MF, Olivero M, Ferro S, et al. Overexpression of the c-MET/HGF receptor gene in human thyroid carcinomas. Oncogene 1992; 7: 2549–53 DiRenzo MF, Olivero M, Ferro S, et al. Overexpression of the c-MET/HGF receptor gene in human thyroid carcinomas. Oncogene 1992; 7: 2549–53
51.
go back to reference Stracke ML, Engel JD, Wilson LW, et al. The type I insulin-like growth factor receptor is a motility receptor in human melanoma cells. J Biol Chem 1989; 264: 21544–9PubMed Stracke ML, Engel JD, Wilson LW, et al. The type I insulin-like growth factor receptor is a motility receptor in human melanoma cells. J Biol Chem 1989; 264: 21544–9PubMed
52.
go back to reference Nakagawara A, Azar CG, Scavarda NJ, et al. Expression and function of TRK-B and BDNF in human neuroblastomas. Mol Cell Biol 1994; 14: 759–67PubMed Nakagawara A, Azar CG, Scavarda NJ, et al. Expression and function of TRK-B and BDNF in human neuroblastomas. Mol Cell Biol 1994; 14: 759–67PubMed
53.
go back to reference Hermansson M, Funa K, Hartman M, et al. Platelet-derived growth factor and its receptors in human glioma tissue: expression of messenger RNA and protein suggests the presence of autocrine and paracrine loops. Cancer Res 1992; 52: 3213–9 Hermansson M, Funa K, Hartman M, et al. Platelet-derived growth factor and its receptors in human glioma tissue: expression of messenger RNA and protein suggests the presence of autocrine and paracrine loops. Cancer Res 1992; 52: 3213–9
54.
go back to reference Nister M, Heldin CH, Wasteson A, et al. A glioma-derived analog to platelet-derived growth factor: demonstration of receptor dompeting activity and immunological crossreactivity. Proc Natl Acad Sci U S A 1984; 81: 926–30PubMedCrossRef Nister M, Heldin CH, Wasteson A, et al. A glioma-derived analog to platelet-derived growth factor: demonstration of receptor dompeting activity and immunological crossreactivity. Proc Natl Acad Sci U S A 1984; 81: 926–30PubMedCrossRef
55.
go back to reference Nister M, Libermann TA, Betsholtz C, et al. Expression of messenger RNAs for platelet-derived growth factor and transforming growth factor-alpha and their receptors in human malignant glioma cell lines. Cancer Res 1988; 48: 3910–8PubMed Nister M, Libermann TA, Betsholtz C, et al. Expression of messenger RNAs for platelet-derived growth factor and transforming growth factor-alpha and their receptors in human malignant glioma cell lines. Cancer Res 1988; 48: 3910–8PubMed
56.
go back to reference Claesson-Welsh L, Eriksson A, Westermark B, et al. cDNA cloning and expression of the human A-type platelet-derived growth factor (PDGF) receptor establishes structural similarity of the B-type PDGF receptor. Proc Natl Acad Sci U S A 1989; 86: 4917–21PubMedCrossRef Claesson-Welsh L, Eriksson A, Westermark B, et al. cDNA cloning and expression of the human A-type platelet-derived growth factor (PDGF) receptor establishes structural similarity of the B-type PDGF receptor. Proc Natl Acad Sci U S A 1989; 86: 4917–21PubMedCrossRef
57.
go back to reference Heldin CH, Johnsson A, Wennergren S, et l.A human osteosarcoma cell line secretes a growth factor structurally related to a homodimer of PDGF A-chains. Nature 1986; 310: 511–4CrossRef Heldin CH, Johnsson A, Wennergren S, et l.A human osteosarcoma cell line secretes a growth factor structurally related to a homodimer of PDGF A-chains. Nature 1986; 310: 511–4CrossRef
58.
go back to reference Leveen P, Claesson-Welsh L, Heldin CH, et al. Expression of messenger RNAs for platelet-derived growth factor and its receptors in human sarcoma cell lines. Int J Cancer 1990; 46: 1066–70PubMedCrossRef Leveen P, Claesson-Welsh L, Heldin CH, et al. Expression of messenger RNAs for platelet-derived growth factor and its receptors in human sarcoma cell lines. Int J Cancer 1990; 46: 1066–70PubMedCrossRef
59.
go back to reference Werner S, Hofschneider PH, Heldin CH, et al. Cultured Kaposi’s sarcoma-derived cells express functional PDGF A-type and B-type receptors. Exp Cell Res 1990; 187: 98–103PubMedCrossRef Werner S, Hofschneider PH, Heldin CH, et al. Cultured Kaposi’s sarcoma-derived cells express functional PDGF A-type and B-type receptors. Exp Cell Res 1990; 187: 98–103PubMedCrossRef
60.
go back to reference Tsai TF, Yauk YK, Chou CK, et al. Evidence of autocrine regulation in human hepatoma cell lines. Biochem Biophys Res Commun 1988; 153: 39–45PubMedCrossRef Tsai TF, Yauk YK, Chou CK, et al. Evidence of autocrine regulation in human hepatoma cell lines. Biochem Biophys Res Commun 1988; 153: 39–45PubMedCrossRef
61.
go back to reference Herlyn M, Kath R, Williams N, et a1. Growth-regulatory factors for normal, premalignant, and malignant human cells in vitro. Adv Cancer Res 1990; 54: 213–34PubMedCrossRef Herlyn M, Kath R, Williams N, et a1. Growth-regulatory factors for normal, premalignant, and malignant human cells in vitro. Adv Cancer Res 1990; 54: 213–34PubMedCrossRef
62.
go back to reference Ito M, Yoshida K, Kyo E, et al. Expression of several growth factors and their receptor genes in human colon carcinomas. Virchows Archiv B Cell Pathol 1990; 59: 173–8CrossRef Ito M, Yoshida K, Kyo E, et al. Expression of several growth factors and their receptor genes in human colon carcinomas. Virchows Archiv B Cell Pathol 1990; 59: 173–8CrossRef
63.
go back to reference Pantazis P, Sariban E, Bohan CA, et al. Synthesis of PDGF by cultured human T cells transformed with HTLV-I and II. Oncogene 1987; 1: 285–9PubMed Pantazis P, Sariban E, Bohan CA, et al. Synthesis of PDGF by cultured human T cells transformed with HTLV-I and II. Oncogene 1987; 1: 285–9PubMed
64.
go back to reference Pantazis P, Kharbanda S, Goustin AS, et al. Coexpression of the genes for platelet-derived growth factor B-chain receptor and macrophage colony-stimulating factor 1 receptor during monocytic differentiation. Proc Natl Acad Sci U S A 1991; 88: 2481–5PubMedCrossRef Pantazis P, Kharbanda S, Goustin AS, et al. Coexpression of the genes for platelet-derived growth factor B-chain receptor and macrophage colony-stimulating factor 1 receptor during monocytic differentiation. Proc Natl Acad Sci U S A 1991; 88: 2481–5PubMedCrossRef
65.
go back to reference Mäkelä TP, Alitalo R, Paulsson Y, et al. Regulation of platelet-derived growth factor gene expression by transforming growth factor beta and phorbol ester in human leukemia cell lines. Mol Cell Biol 1987; 7: 3656–62PubMed Mäkelä TP, Alitalo R, Paulsson Y, et al. Regulation of platelet-derived growth factor gene expression by transforming growth factor beta and phorbol ester in human leukemia cell lines. Mol Cell Biol 1987; 7: 3656–62PubMed
66.
go back to reference Maxwell M, Galanopoulos T, Hedley-Whyte ET, et al. Human meningiomas co-express platelet-derived growth factor (PDGF) and PDGF-receptor genes and their protein products. Int J Cancer 1990; 46: 16–21PubMedCrossRef Maxwell M, Galanopoulos T, Hedley-Whyte ET, et al. Human meningiomas co-express platelet-derived growth factor (PDGF) and PDGF-receptor genes and their protein products. Int J Cancer 1990; 46: 16–21PubMedCrossRef
67.
go back to reference Peres R, Betsholtz C, Westermark B, et al. Frequent expression of growth factors for mesenchymal cells in human mammary carcinoma cell lines. Cancer Res 1987; 47: 3425–9PubMed Peres R, Betsholtz C, Westermark B, et al. Frequent expression of growth factors for mesenchymal cells in human mammary carcinoma cell lines. Cancer Res 1987; 47: 3425–9PubMed
68.
go back to reference Ginsburg E, Vonderhaar BK. Stimulation of growth of human breast cancer cells (T47D) by platelet derived growth factor. Cancer Lett 1991; 58: 137–44PubMedCrossRef Ginsburg E, Vonderhaar BK. Stimulation of growth of human breast cancer cells (T47D) by platelet derived growth factor. Cancer Lett 1991; 58: 137–44PubMedCrossRef
69.
70.
go back to reference Collins T, Pober JS, Gimbrone MA, et al. Cultured human endothelial cells express platelet-derived growth factor A chain. Am J Pathol 1987; 126:7–12PubMed Collins T, Pober JS, Gimbrone MA, et al. Cultured human endothelial cells express platelet-derived growth factor A chain. Am J Pathol 1987; 126:7–12PubMed
71.
go back to reference Roussel MF, Downing JR, Rettenmier CW, et al. A point mutation in the extracellular domain of the human CSF-1 receptor (Fms proto-oncogene product) activates its transforming potential. Cell 1988; 55: 979–88PubMedCrossRef Roussel MF, Downing JR, Rettenmier CW, et al. A point mutation in the extracellular domain of the human CSF-1 receptor (Fms proto-oncogene product) activates its transforming potential. Cell 1988; 55: 979–88PubMedCrossRef
72.
go back to reference Yokoyama Y, Morishita S, Takahashi Y, et al. Modulation of c-fms proto-oncogene in an ovarian carcinoma cell line by a hammerhead ribozyme. Br J Cancer 1997; 76: 977–82PubMedCrossRef Yokoyama Y, Morishita S, Takahashi Y, et al. Modulation of c-fms proto-oncogene in an ovarian carcinoma cell line by a hammerhead ribozyme. Br J Cancer 1997; 76: 977–82PubMedCrossRef
73.
go back to reference Suzuki M, Sekiguchi I, Ohwada M, et al. Expression of c-fms proto-oncogene product by ovarian cancer cell lines with effects of macrophage colony-stimulating factor on proliferation. Oncology 1996; 53: 99–103PubMedCrossRef Suzuki M, Sekiguchi I, Ohwada M, et al. Expression of c-fms proto-oncogene product by ovarian cancer cell lines with effects of macrophage colony-stimulating factor on proliferation. Oncology 1996; 53: 99–103PubMedCrossRef
74.
go back to reference Sapi E, Flick MB, Gilmore-Hebert M, et al. Transcriptional regulation of the c-fms (CSF-1R) proto-oncogene in human breast carcinoma cells by glucocorticoids. Oncogene 1995; 10: 529–42PubMed Sapi E, Flick MB, Gilmore-Hebert M, et al. Transcriptional regulation of the c-fms (CSF-1R) proto-oncogene in human breast carcinoma cells by glucocorticoids. Oncogene 1995; 10: 529–42PubMed
75.
go back to reference Chambers SK, Wang Y, Gilmore-Hebert M, et al. Post-transcriptional regulation of c-fms proto-oncogene expression by dexamethasone and of CSF-1 in human breast carcinomas in vitro. Steroids 1994; 59: 514–22PubMedCrossRef Chambers SK, Wang Y, Gilmore-Hebert M, et al. Post-transcriptional regulation of c-fms proto-oncogene expression by dexamethasone and of CSF-1 in human breast carcinomas in vitro. Steroids 1994; 59: 514–22PubMedCrossRef
76.
go back to reference Scholl SM, Mosseri V, Tang R, et al. Expression of colony-stimulating factor-1 and its receptor (the protein product of c-fms) in invasive breast tumor cells: induction of urokinase production via this pathway? Ann N Y Acad Sci 1993; 698: 131–5PubMedCrossRef Scholl SM, Mosseri V, Tang R, et al. Expression of colony-stimulating factor-1 and its receptor (the protein product of c-fms) in invasive breast tumor cells: induction of urokinase production via this pathway? Ann N Y Acad Sci 1993; 698: 131–5PubMedCrossRef
77.
go back to reference Kacinski BM, Scata KA, Carter D, et al. FMS (CSF-1 receptor) and CSF-1 transcripts and protein are expressed by human breast carcinomas in vivo and in vitro. Oncogene 1991; 6: 941–52PubMed Kacinski BM, Scata KA, Carter D, et al. FMS (CSF-1 receptor) and CSF-1 transcripts and protein are expressed by human breast carcinomas in vivo and in vitro. Oncogene 1991; 6: 941–52PubMed
78.
go back to reference Leiserowitz GS, Harris SA, Subramaniam M, et al. The protooncogene c-fms is overexpressed in endometrial cancer. Gynecol Oncol 1993; 49: 190–6PubMedCrossRef Leiserowitz GS, Harris SA, Subramaniam M, et al. The protooncogene c-fms is overexpressed in endometrial cancer. Gynecol Oncol 1993; 49: 190–6PubMedCrossRef
79.
go back to reference Storga D, Pecina-Slaus N, Pavelic J, et al. c-fms is present in primary tumours as well as in their metastases in bone marrow. Int J Exp Pathol 1992; 73: 527–33PubMed Storga D, Pecina-Slaus N, Pavelic J, et al. c-fms is present in primary tumours as well as in their metastases in bone marrow. Int J Exp Pathol 1992; 73: 527–33PubMed
80.
go back to reference Qui F, Ray R, Brown K, et al. Primary structure of cKit: relationship with the CSF-1/PDGF receptor kinase family. Oncogenic activation of vKit involves deletion of extracellular domain and C-terminus. EMBO J 1988; 7: 1003–11 Qui F, Ray R, Brown K, et al. Primary structure of cKit: relationship with the CSF-1/PDGF receptor kinase family. Oncogenic activation of vKit involves deletion of extracellular domain and C-terminus. EMBO J 1988; 7: 1003–11
81.
go back to reference Funasaka Y, Boulton T, Cobb M, et al. c-kit-kinase induces a cascade of protein tyrosine phosphorylation in normal human melanocytes in response to mast cell growth factor in stimulates mitogen-activated protein kinase but is down-regulated in melanomas. Mol Biol Cell 1992; 3: 197–209PubMed Funasaka Y, Boulton T, Cobb M, et al. c-kit-kinase induces a cascade of protein tyrosine phosphorylation in normal human melanocytes in response to mast cell growth factor in stimulates mitogen-activated protein kinase but is down-regulated in melanomas. Mol Biol Cell 1992; 3: 197–209PubMed
82.
go back to reference Natali PG, Nicotra MR, Winkler AB, et al. Progression of human cutaneous melanoma is associated with loss of expression of c-kit proto-oncogene receptor. Int J Cancer 1992; 52: 197–201PubMedCrossRef Natali PG, Nicotra MR, Winkler AB, et al. Progression of human cutaneous melanoma is associated with loss of expression of c-kit proto-oncogene receptor. Int J Cancer 1992; 52: 197–201PubMedCrossRef
83.
go back to reference Lassam N, Bickford S. Loss of c-kit expression in cultured melanoma cells. Oncogene 1992; 7: 51–6PubMed Lassam N, Bickford S. Loss of c-kit expression in cultured melanoma cells. Oncogene 1992; 7: 51–6PubMed
84.
go back to reference Charnock-Jones DS, Sharkey AM, Boocock AM, et al. Vascular endothelial growth factor receptor localization and activation in human trophoblast and choriocarcinoma cells. Biol Reproduct 1994; 51: 524–30CrossRef Charnock-Jones DS, Sharkey AM, Boocock AM, et al. Vascular endothelial growth factor receptor localization and activation in human trophoblast and choriocarcinoma cells. Biol Reproduct 1994; 51: 524–30CrossRef
85.
go back to reference Gitay-Goren H., Halaban R, Neufeld G, et al. Human melanoma cells but not nor normal melanocytes express vascular endothelial growth factor receptors. Biochem Biophys Res Commun 1993; 190: 702–9PubMedCrossRef Gitay-Goren H., Halaban R, Neufeld G, et al. Human melanoma cells but not nor normal melanocytes express vascular endothelial growth factor receptors. Biochem Biophys Res Commun 1993; 190: 702–9PubMedCrossRef
86.
go back to reference Boocock CA, Charnock-Jones DS, Sharkey AM, et al. Expression of vascular endothelial growth factor and its receptors flt and KDR in ovarian carcinoma. J Natl Cancer Inst 1995; 87: 506–16PubMedCrossRef Boocock CA, Charnock-Jones DS, Sharkey AM, et al. Expression of vascular endothelial growth factor and its receptors flt and KDR in ovarian carcinoma. J Natl Cancer Inst 1995; 87: 506–16PubMedCrossRef
87.
go back to reference Brown LF, Berse B, Jackman RW, et al. Increased expression of vascular permeability factor (vascular endothelial growth factor) and its receptors in kidney and bladder carcinomas. Am J Pathol 1993; 143: 1255–62PubMed Brown LF, Berse B, Jackman RW, et al. Increased expression of vascular permeability factor (vascular endothelial growth factor) and its receptors in kidney and bladder carcinomas. Am J Pathol 1993; 143: 1255–62PubMed
88.
go back to reference Enomoto T, Okamoto T, Sato JD. Vascular endothelial growth factor induces the disorganization of actin stress fibers accompanied by protein tyrosine phosphorylation and morphological change in Balb/C3T3 cells. Biochem Biophy Res Commun 1994; 202: 1716–23CrossRef Enomoto T, Okamoto T, Sato JD. Vascular endothelial growth factor induces the disorganization of actin stress fibers accompanied by protein tyrosine phosphorylation and morphological change in Balb/C3T3 cells. Biochem Biophy Res Commun 1994; 202: 1716–23CrossRef
89.
go back to reference Katoh O, Tauchi H, Kawaishi K, et al. Expression of the vascular endothelial growth factor (VEGF) receptor gene, KDR, in hematopoietic cells and inhibitory effect of VEGF on apoptotic cell death caused by ionizing radiation. Cancer Res 1995; 55: 5687–92PubMed Katoh O, Tauchi H, Kawaishi K, et al. Expression of the vascular endothelial growth factor (VEGF) receptor gene, KDR, in hematopoietic cells and inhibitory effect of VEGF on apoptotic cell death caused by ionizing radiation. Cancer Res 1995; 55: 5687–92PubMed
90.
go back to reference Soker S, Takahima S, Mia HQ, et al. Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor. Cell 1998; 735-45 Soker S, Takahima S, Mia HQ, et al. Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor. Cell 1998; 735-45
91.
go back to reference Koura AN, Liu W, Kitadai Y, et al. Regulation of vascular endothelial growth factor expression in human colon carcinoma cells by cell density. Cancer Res 1996; 56: 3891–4PubMed Koura AN, Liu W, Kitadai Y, et al. Regulation of vascular endothelial growth factor expression in human colon carcinoma cells by cell density. Cancer Res 1996; 56: 3891–4PubMed
92.
go back to reference Brown K, Gerstbergre S, Carlson L, et al. Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation. Science 1995; 267: 1485–8PubMedCrossRef Brown K, Gerstbergre S, Carlson L, et al. Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation. Science 1995; 267: 1485–8PubMedCrossRef
93.
go back to reference Takahashi T, Shibuya M. The 230 kDa mature form of KDR/Flk-1 (VEGF receptor-2) activates the PLCγ pathway and partially induces mitotic signals in NIH3T3 fibroblasts. Oncogene 1997; 14: 2079–89PubMedCrossRef Takahashi T, Shibuya M. The 230 kDa mature form of KDR/Flk-1 (VEGF receptor-2) activates the PLCγ pathway and partially induces mitotic signals in NIH3T3 fibroblasts. Oncogene 1997; 14: 2079–89PubMedCrossRef
94.
go back to reference Berse B, Brown LF, Van De Water L, et al. Vascular permeability factor (vascular endothelial growth factor) gene is expressed differentially in normal tissues, macrophages, and tumors. Mol Biol Cell 1992; 3: 211–20PubMed Berse B, Brown LF, Van De Water L, et al. Vascular permeability factor (vascular endothelial growth factor) gene is expressed differentially in normal tissues, macrophages, and tumors. Mol Biol Cell 1992; 3: 211–20PubMed
95.
go back to reference Dhingra K, Horn S, Sahin A, et al. Expression of TIE-2 receptor and ligand in human cell lines and tumor biopsy specimens [abstract]. Proc Annu Meet Am Assoc Cancer Res 1997; 38: A3260 Dhingra K, Horn S, Sahin A, et al. Expression of TIE-2 receptor and ligand in human cell lines and tumor biopsy specimens [abstract]. Proc Annu Meet Am Assoc Cancer Res 1997; 38: A3260
96.
go back to reference Chang J, Park K, Bang YJ, et al. Expression of transforming growth factor ß type II receptor reduces tumorigenicity in human gastric cancer cells. Cancer Res 1997; 57: 2856–9PubMed Chang J, Park K, Bang YJ, et al. Expression of transforming growth factor ß type II receptor reduces tumorigenicity in human gastric cancer cells. Cancer Res 1997; 57: 2856–9PubMed
97.
go back to reference Markowitz S, Wang J, Myeroff L, et al. Inactivation of the type II TGF-ß receptor in colon cancer cells with microsatellite instability. Science 1995; 268: 1336–8PubMedCrossRef Markowitz S, Wang J, Myeroff L, et al. Inactivation of the type II TGF-ß receptor in colon cancer cells with microsatellite instability. Science 1995; 268: 1336–8PubMedCrossRef
98.
go back to reference Kadin M, Cavaille-Coll MW, Gertz R, et al. Loss of receptors for transforming growth factor ß receptors: role in physiology and disease. J Biomed Sci 1996; 3: 143–58CrossRef Kadin M, Cavaille-Coll MW, Gertz R, et al. Loss of receptors for transforming growth factor ß receptors: role in physiology and disease. J Biomed Sci 1996; 3: 143–58CrossRef
99.
go back to reference Kim IY, Ahn HJ, Zelner DJ, et al. Genetic change in transforming growth factor ß (TGF-ß) receptor type I gene correlates with insensitivity to RGF-ß1 in human prostate cancer cells. Cancer Res 1996; 56: 44–8PubMed Kim IY, Ahn HJ, Zelner DJ, et al. Genetic change in transforming growth factor ß (TGF-ß) receptor type I gene correlates with insensitivity to RGF-ß1 in human prostate cancer cells. Cancer Res 1996; 56: 44–8PubMed
100.
go back to reference Parsons R, Myerhoff LL, Liu BL, et al. Microsatellite instability and mutations of the transforming growth factor ß type II receptor gene in colorectal cancer. Cancer Res 1995; 55: 5548–50PubMed Parsons R, Myerhoff LL, Liu BL, et al. Microsatellite instability and mutations of the transforming growth factor ß type II receptor gene in colorectal cancer. Cancer Res 1995; 55: 5548–50PubMed
101.
go back to reference Myeroff LL, Parsons R, Kim SJ, et al. A transforming growth factor ß receptor type II gene mutation common in colon and gastric but rare in endomietric cancers with microsatellite instability. Cancer Res 1995; 55: 5545–7PubMed Myeroff LL, Parsons R, Kim SJ, et al. A transforming growth factor ß receptor type II gene mutation common in colon and gastric but rare in endomietric cancers with microsatellite instability. Cancer Res 1995; 55: 5545–7PubMed
102.
go back to reference Easty DJ, Ganz SE, Farr CJ, et al. Novel and known protein tyrosine kinases and their abnormal expression in human melanoma. J Invest Dermatol 1993; 101: 679–84PubMedCrossRef Easty DJ, Ganz SE, Farr CJ, et al. Novel and known protein tyrosine kinases and their abnormal expression in human melanoma. J Invest Dermatol 1993; 101: 679–84PubMedCrossRef
103.
go back to reference Boyd AW, Ward LD, Wicks IP, et al. Isolation and characterization of a novel receptor-type protein tyrosine kinase (hek) from a human pre-B cell lines. J Biol Chem 1992; 267: 3262–7PubMed Boyd AW, Ward LD, Wicks IP, et al. Isolation and characterization of a novel receptor-type protein tyrosine kinase (hek) from a human pre-B cell lines. J Biol Chem 1992; 267: 3262–7PubMed
104.
go back to reference Wicks IP, Wilkinson D, Salvaris E, et al. Molecular cloning of HEK the gene encoding a receptor tyrosine kinase expressed by human lymphoid tumor cell lines. Proc Natl Acad Sci U S A 1992; 89: 1611–5PubMedCrossRef Wicks IP, Wilkinson D, Salvaris E, et al. Molecular cloning of HEK the gene encoding a receptor tyrosine kinase expressed by human lymphoid tumor cell lines. Proc Natl Acad Sci U S A 1992; 89: 1611–5PubMedCrossRef
105.
go back to reference Easty DJ, Guthrie BA, Maung K, et al. Protein B61 as a new growth factor: expression of B61 and up-regulation of its receptor epithelial cell kinase during melanoma progression. Cancer Res 1995; 55: 2528–32PubMed Easty DJ, Guthrie BA, Maung K, et al. Protein B61 as a new growth factor: expression of B61 and up-regulation of its receptor epithelial cell kinase during melanoma progression. Cancer Res 1995; 55: 2528–32PubMed
106.
go back to reference Maru Y, Hirai H, Yoshida MC, et al. Evolution, expression and chromosomal location of a novel receptor tyrosine kinase gene. Mol Cell Biol 1988; 8: 3770–6PubMed Maru Y, Hirai H, Yoshida MC, et al. Evolution, expression and chromosomal location of a novel receptor tyrosine kinase gene. Mol Cell Biol 1988; 8: 3770–6PubMed
107.
go back to reference Carlomagno F, Savatore D, Santoro M, et al. Point mutation of the RET proto-oncogene in the TT human medullary thyroid carcinoma cell line. Biochem Biophys Res Commun 1995; 207: 1022–8PubMedCrossRef Carlomagno F, Savatore D, Santoro M, et al. Point mutation of the RET proto-oncogene in the TT human medullary thyroid carcinoma cell line. Biochem Biophys Res Commun 1995; 207: 1022–8PubMedCrossRef
108.
go back to reference Sugg SL, Zheng L, Rosen IB, et al. ret/PTC-1, -2, and -3 oncogene rearrangements in human thyroid carcinomas: implications for metastatic potential? J Clin Endocrin Metab 1996; 81: 3360–5CrossRef Sugg SL, Zheng L, Rosen IB, et al. ret/PTC-1, -2, and -3 oncogene rearrangements in human thyroid carcinomas: implications for metastatic potential? J Clin Endocrin Metab 1996; 81: 3360–5CrossRef
109.
go back to reference Takaya K, Yoshimasa T, Arai H, et al. Expression of the RET proto-oncogene in normal human tissues, pheochromocytomas, and other tumors of neural crest origin. J Mol Med 1996; 74: 617–21PubMedCrossRef Takaya K, Yoshimasa T, Arai H, et al. Expression of the RET proto-oncogene in normal human tissues, pheochromocytomas, and other tumors of neural crest origin. J Mol Med 1996; 74: 617–21PubMedCrossRef
110.
go back to reference Nakamura T, Ishizaka Y, Nagao M, et al. Expression of the ret proto-oncogene product in human normal and neoplastic tissues of neural crest origin. J Pathol 1994; 172: 255–60PubMedCrossRef Nakamura T, Ishizaka Y, Nagao M, et al. Expression of the ret proto-oncogene product in human normal and neoplastic tissues of neural crest origin. J Pathol 1994; 172: 255–60PubMedCrossRef
111.
go back to reference Ivanchuk S, Eng C, Myers S, et al. Expression of alternatively spliced RET transcripts in the developing human kidney and Wilm’s tumor. Am J Hum Genet 1995; 57: A302 Ivanchuk S, Eng C, Myers S, et al. Expression of alternatively spliced RET transcripts in the developing human kidney and Wilm’s tumor. Am J Hum Genet 1995; 57: A302
112.
go back to reference Mapstone T, McMichael M, Goldthwait D. Expression of platelet-derived growth factors, transforming growth factors, and the ros gene in a variety of primary human brain tumors. Neurosurgery 1991; 28: 216–22PubMedCrossRef Mapstone T, McMichael M, Goldthwait D. Expression of platelet-derived growth factors, transforming growth factors, and the ros gene in a variety of primary human brain tumors. Neurosurgery 1991; 28: 216–22PubMedCrossRef
113.
go back to reference Watkins D, Dion F, Poisson M, et al. Analysis of oncogene expression in primary human gliomas: evidence for increased expression of the ros oncogene. Cancer Genet Cytogenet 1994; 72: 130–6PubMedCrossRef Watkins D, Dion F, Poisson M, et al. Analysis of oncogene expression in primary human gliomas: evidence for increased expression of the ros oncogene. Cancer Genet Cytogenet 1994; 72: 130–6PubMedCrossRef
114.
go back to reference Wu JK, Chikaraishi DM, Differential expression of ros oncogene in primary human astrocytomas and astrocytoma cell lines. Cancer Res 1990; 50: 3032–5PubMed Wu JK, Chikaraishi DM, Differential expression of ros oncogene in primary human astrocytomas and astrocytoma cell lines. Cancer Res 1990; 50: 3032–5PubMed
115.
go back to reference Dickson RB, Lippman ME. Growth factors in breast cancer. Endocrine Rev 1995; 16: 559 Dickson RB, Lippman ME. Growth factors in breast cancer. Endocrine Rev 1995; 16: 559
116.
go back to reference Nicholson RI, McClelland RA, Gee JMW, et al. Transforming growth factor-α and endocrine sensitivity in breast cancer. Cancer Res 1994; 54: 1684–9PubMed Nicholson RI, McClelland RA, Gee JMW, et al. Transforming growth factor-α and endocrine sensitivity in breast cancer. Cancer Res 1994; 54: 1684–9PubMed
117.
go back to reference Barrett-Lee P, Travers M, Luqmani Y, et al. Transcripts fortransforming growth factors in human breast cancer: clinical correlates. Br J Cancer 1990; 61: 612–7PubMedCrossRef Barrett-Lee P, Travers M, Luqmani Y, et al. Transcripts fortransforming growth factors in human breast cancer: clinical correlates. Br J Cancer 1990; 61: 612–7PubMedCrossRef
118.
go back to reference Murphy LC, Dotslaw H, Wong MSJ. Epidermal growth factor: receptor and ligand expression in human breast cancer. Semin Cancer Biol 1990; 1: 305–15PubMed Murphy LC, Dotslaw H, Wong MSJ. Epidermal growth factor: receptor and ligand expression in human breast cancer. Semin Cancer Biol 1990; 1: 305–15PubMed
119.
go back to reference Murray PA, Barrett-Lee P, Travers M, et al. The prognostic significance of transforming growth factors in human breast cancer. Br J Cancer 1993; 67: 1408–12PubMedCrossRef Murray PA, Barrett-Lee P, Travers M, et al. The prognostic significance of transforming growth factors in human breast cancer. Br J Cancer 1993; 67: 1408–12PubMedCrossRef
120.
go back to reference Semba K, Kamata N, Toyoshima K, et al. A v-erbB-related protooncogene, c-erbB-2, is distinct from the c-erbB-1/epidermal growth factor-receptor gene and is amplified in a human salivary gland adenocarcinoma. Proc Natl Acad Sci U S A 1985; 82: 6497–501PubMedCrossRef Semba K, Kamata N, Toyoshima K, et al. A v-erbB-related protooncogene, c-erbB-2, is distinct from the c-erbB-1/epidermal growth factor-receptor gene and is amplified in a human salivary gland adenocarcinoma. Proc Natl Acad Sci U S A 1985; 82: 6497–501PubMedCrossRef
121.
go back to reference Plowman GD, Culouscou JM, Whitney GS, et al. Ligand-specific activation of HER4/p180erbB4, a fourth member of the epidermal growth factor receptor family. Proc Natl Acad Sci US A 1993; 90: 1746–50CrossRef Plowman GD, Culouscou JM, Whitney GS, et al. Ligand-specific activation of HER4/p180erbB4, a fourth member of the epidermal growth factor receptor family. Proc Natl Acad Sci US A 1993; 90: 1746–50CrossRef
122.
go back to reference Carraway KL, Cantley LC. A new acquaintance for erbB3 and erbB4: a role for receptor heterodimerization in growth signalling. Cell 1994; 78: 5–8PubMedCrossRef Carraway KL, Cantley LC. A new acquaintance for erbB3 and erbB4: a role for receptor heterodimerization in growth signalling. Cell 1994; 78: 5–8PubMedCrossRef
123.
go back to reference Goldman R, Levy RB, Peles E, et al. Heterodimerization of the erbB-1 and erbB-2 receptors in human breast carcinoma cells: a mechanism for receptor transregulation. Biochemistry 1990; 29: 11024–8PubMedCrossRef Goldman R, Levy RB, Peles E, et al. Heterodimerization of the erbB-1 and erbB-2 receptors in human breast carcinoma cells: a mechanism for receptor transregulation. Biochemistry 1990; 29: 11024–8PubMedCrossRef
124.
go back to reference Qian X, Decker SJ, Greene MI. p185c-neu and epidermal growth factor receptor associate into a structure composed of activated kinases. Proc Natl Acad Sci U S A 1992; 89: 1330–4CrossRef Qian X, Decker SJ, Greene MI. p185c-neu and epidermal growth factor receptor associate into a structure composed of activated kinases. Proc Natl Acad Sci U S A 1992; 89: 1330–4CrossRef
125.
go back to reference Soltoff SP, Carraway KL, Prigent SA, et al. ErbB3 is involved in activating phosphatidylinositol 3-kinase by epidermal growth factor. Mol Cell Biol 1994; 14: 3550–8PubMed Soltoff SP, Carraway KL, Prigent SA, et al. ErbB3 is involved in activating phosphatidylinositol 3-kinase by epidermal growth factor. Mol Cell Biol 1994; 14: 3550–8PubMed
126.
go back to reference Lee PL, Johnson DE, Cousens LS, et al. Purification and cDNA cloning of a receptor for basic fibroblast growth factor. Science 1989; 245: 57–60PubMedCrossRef Lee PL, Johnson DE, Cousens LS, et al. Purification and cDNA cloning of a receptor for basic fibroblast growth factor. Science 1989; 245: 57–60PubMedCrossRef
127.
go back to reference Kornbluth S, Paulson DE, Hanafusa H. Novel tyrosine kinase identified by phosphotyrosine antibody screening of cDN libraries. Mol Cell Biol 1988; 8: 5541–4PubMed Kornbluth S, Paulson DE, Hanafusa H. Novel tyrosine kinase identified by phosphotyrosine antibody screening of cDN libraries. Mol Cell Biol 1988; 8: 5541–4PubMed
128.
go back to reference Keegan K, Johnson DE, Williams LT, et al. Isolation of an additional member of the fibroblast growth factor receptor family FGFR-3. Proc Natl Acad Sci U S A 1991; 88: 1095–9PubMedCrossRef Keegan K, Johnson DE, Williams LT, et al. Isolation of an additional member of the fibroblast growth factor receptor family FGFR-3. Proc Natl Acad Sci U S A 1991; 88: 1095–9PubMedCrossRef
129.
go back to reference Partanan J, Makla TP, Eerola E, et al. FGFR-4,, a novel acidic fibroblast growth factor receptor with a distinct expression pattern. EMBO J 1991; 10: 1347–54 Partanan J, Makla TP, Eerola E, et al. FGFR-4,, a novel acidic fibroblast growth factor receptor with a distinct expression pattern. EMBO J 1991; 10: 1347–54
130.
go back to reference Avivi A, Zimmer Y, Yayon A, et al. Flg-2, a new member of the family of fibroblast growth factor receptors. Oncogene 1991; 6: 1089–92PubMed Avivi A, Zimmer Y, Yayon A, et al. Flg-2, a new member of the family of fibroblast growth factor receptors. Oncogene 1991; 6: 1089–92PubMed
131.
go back to reference Yan G, Fukabori Y, Nikolaropoulos S, et al. Heparin-binding keratinocyte growth factor is a candidate stromal-to-epithelial cell andromedin. Mol Endocrinol 1992; 6: 2123–8PubMedCrossRef Yan G, Fukabori Y, Nikolaropoulos S, et al. Heparin-binding keratinocyte growth factor is a candidate stromal-to-epithelial cell andromedin. Mol Endocrinol 1992; 6: 2123–8PubMedCrossRef
132.
go back to reference Yan G, Fukabori Y, McBride G, et al. Exon switching and activation of stromal and embryonic fibroblast growth factor (FGF): FGF receptor genes in prostate epithelial cells accompany stromal independence and malignancy. Mol Cell Biol 1993; 13: 4513–22PubMed Yan G, Fukabori Y, McBride G, et al. Exon switching and activation of stromal and embryonic fibroblast growth factor (FGF): FGF receptor genes in prostate epithelial cells accompany stromal independence and malignancy. Mol Cell Biol 1993; 13: 4513–22PubMed
133.
go back to reference Dvorak HF, Sioussat TM, Brown LF, et al. Distribution of vascular permeability factor (vascular endothelial growth factor) in tumors: concentration in tumor blood vessels. J Exp Med 1991; 174: 1275–8PubMedCrossRef Dvorak HF, Sioussat TM, Brown LF, et al. Distribution of vascular permeability factor (vascular endothelial growth factor) in tumors: concentration in tumor blood vessels. J Exp Med 1991; 174: 1275–8PubMedCrossRef
134.
go back to reference Plate KH, Breier G, Weich HA et al. Vascular endothelial growth factor is a potential tumour angiogenesis factor in human gliomas in vivo. Nature 1992; 359: 845–8PubMedCrossRef Plate KH, Breier G, Weich HA et al. Vascular endothelial growth factor is a potential tumour angiogenesis factor in human gliomas in vivo. Nature 1992; 359: 845–8PubMedCrossRef
135.
go back to reference Heldin CH, Westermark B. Platelet-derived growth factor: mechanism of action and possible in vivo function. Cell Regul 1990; 1: 555–66PubMed Heldin CH, Westermark B. Platelet-derived growth factor: mechanism of action and possible in vivo function. Cell Regul 1990; 1: 555–66PubMed
136.
go back to reference Bywater M, Rorsman F, Bongcam-Rudloff E, et al. Expression of recombinant platelet-derived growth factor A- and B -chain homodimers in Rat-1 cells and human fibroblasts reveals differences in protein processing and autocrine effects. Mol Cell Biol 1988; 8: 2753–62PubMed Bywater M, Rorsman F, Bongcam-Rudloff E, et al. Expression of recombinant platelet-derived growth factor A- and B -chain homodimers in Rat-1 cells and human fibroblasts reveals differences in protein processing and autocrine effects. Mol Cell Biol 1988; 8: 2753–62PubMed
137.
go back to reference Keating MT, Williams LT. Autocrine stimulation of intracellular PDGF receptors in v-sis transformed cells. Science 1988; 239: 914–6PubMedCrossRef Keating MT, Williams LT. Autocrine stimulation of intracellular PDGF receptors in v-sis transformed cells. Science 1988; 239: 914–6PubMedCrossRef
138.
go back to reference Huang SS, Huang JS. Rapid turnover of the platelet-derived growth factor receptor in sis-transformed cells and reversal by suramin: implications for the mechanism of autocrine transformation. J Biol Chem 1988; 263: 12608–18PubMed Huang SS, Huang JS. Rapid turnover of the platelet-derived growth factor receptor in sis-transformed cells and reversal by suramin: implications for the mechanism of autocrine transformation. J Biol Chem 1988; 263: 12608–18PubMed
139.
go back to reference Westermark B, Heldin CH. Platelet-derived growth factor in autocrine transformation. Cancer Res 51: 5087-92 Westermark B, Heldin CH. Platelet-derived growth factor in autocrine transformation. Cancer Res 51: 5087-92
140.
go back to reference Ponten F, Ren Z, Nister M, et al. Epithelial-stromal interactions in basal cell cancer: the PDGF system. J Invest Dermatol 1994; 102: 304–9PubMedCrossRef Ponten F, Ren Z, Nister M, et al. Epithelial-stromal interactions in basal cell cancer: the PDGF system. J Invest Dermatol 1994; 102: 304–9PubMedCrossRef
141.
go back to reference Funa K, Papanicolaou V, Juhlin C, et al. Expression of platelet-derived growth factor beta-receptors on stromal tissue cells in human carcinoid tumors. Cancer Res 1990; 50: 748–53PubMed Funa K, Papanicolaou V, Juhlin C, et al. Expression of platelet-derived growth factor beta-receptors on stromal tissue cells in human carcinoid tumors. Cancer Res 1990; 50: 748–53PubMed
142.
go back to reference Chaudhry A, Panpanicolaou V, Oberg K, et al. Expression of platelet-derived growth factor and its receptors in neuroendocrine tumors of the digestive system. Cancer Res 1992; 52: 1006–12PubMed Chaudhry A, Panpanicolaou V, Oberg K, et al. Expression of platelet-derived growth factor and its receptors in neuroendocrine tumors of the digestive system. Cancer Res 1992; 52: 1006–12PubMed
143.
go back to reference Sato N, Nariuchi H, Tsuruoka N, et al. Actions of TNF and IFN-gamma on angiogenesis in vitro.J Invest Dermatol 1990; 95: 85S–89SPubMedCrossRef Sato N, Nariuchi H, Tsuruoka N, et al. Actions of TNF and IFN-gamma on angiogenesis in vitro.J Invest Dermatol 1990; 95: 85S–89SPubMedCrossRef
144.
go back to reference Hermansson M, Nister M, Betsholtz C, et al. Endothelial cell hyperplasia in human glioblastoma: co-expression of mRNA for platelet-derived growth factor (PDGF) B chain and PDGF receptor suggests autocrine growth stimulation. Proc Natl Acad Sci U S A 1988; 85: 7748–52PubMedCrossRef Hermansson M, Nister M, Betsholtz C, et al. Endothelial cell hyperplasia in human glioblastoma: co-expression of mRNA for platelet-derived growth factor (PDGF) B chain and PDGF receptor suggests autocrine growth stimulation. Proc Natl Acad Sci U S A 1988; 85: 7748–52PubMedCrossRef
145.
go back to reference Beitz JG, Kim IS, Calabrese P, et al. Human microvascular endothelial cells express receptors for platelet-derived growth factor. Proc Natl Acad Sci U S A 1991; 88: 2021–5PubMedCrossRef Beitz JG, Kim IS, Calabrese P, et al. Human microvascular endothelial cells express receptors for platelet-derived growth factor. Proc Natl Acad Sci U S A 1991; 88: 2021–5PubMedCrossRef
146.
go back to reference Shibuya M, Yamguchi S, Yamane A, et al. Nucleotide sequences and expression of a novel human receptor-type tyrosine kinase gene (flt) closely related to the fins family. Oncogene 1990; 5: 519–24PubMed Shibuya M, Yamguchi S, Yamane A, et al. Nucleotide sequences and expression of a novel human receptor-type tyrosine kinase gene (flt) closely related to the fins family. Oncogene 1990; 5: 519–24PubMed
147.
go back to reference DeVries C, Escobedo JA, Ueono H, et al. The fms-like tyrosine kinase, a receptor for vascular endothelial growth factor. Science 1992; 255: 989–91CrossRef DeVries C, Escobedo JA, Ueono H, et al. The fms-like tyrosine kinase, a receptor for vascular endothelial growth factor. Science 1992; 255: 989–91CrossRef
148.
go back to reference Terman BI, Dougher-Vermazen M, Carrion ME, et al. Identification of the KDR tyrosine kinase as a receptor for vascular endothelial cell growth factor. Biochem Biophys Res Commun 1992; 187: 1579–86PubMedCrossRef Terman BI, Dougher-Vermazen M, Carrion ME, et al. Identification of the KDR tyrosine kinase as a receptor for vascular endothelial cell growth factor. Biochem Biophys Res Commun 1992; 187: 1579–86PubMedCrossRef
149.
go back to reference Millauer B, Wizigmann-Voos S, Schnurch H, et al. High affinity VEGF binding and developmental expression suggest Flk-1 as a major regulator of vasculogenesis and angiogenesis. Cell 1993; 72: 835–46PubMedCrossRef Millauer B, Wizigmann-Voos S, Schnurch H, et al. High affinity VEGF binding and developmental expression suggest Flk-1 as a major regulator of vasculogenesis and angiogenesis. Cell 1993; 72: 835–46PubMedCrossRef
150.
go back to reference Joukov V, Pajusola K, Kaipainen A, et al. A novel vascular endothelial growth factor, VEGF-C, is a ligand for the Flt4 (VEGFR-3) and KDR (VEGFR-2) receptor tyrosine kinases [published errata appears in EMBO J 1996; 15: 1751]. EMBO J 1996; 15: 290–8PubMed Joukov V, Pajusola K, Kaipainen A, et al. A novel vascular endothelial growth factor, VEGF-C, is a ligand for the Flt4 (VEGFR-3) and KDR (VEGFR-2) receptor tyrosine kinases [published errata appears in EMBO J 1996; 15: 1751]. EMBO J 1996; 15: 290–8PubMed
151.
go back to reference Waltenberger J, Claesson-Welsh L, Siegbahn A, et al. Different signal transduction properties of KDR and Flt1, two receptors for vascular endothelial growth factor. J Biol Chem 1994; 269: 26988–95PubMed Waltenberger J, Claesson-Welsh L, Siegbahn A, et al. Different signal transduction properties of KDR and Flt1, two receptors for vascular endothelial growth factor. J Biol Chem 1994; 269: 26988–95PubMed
152.
go back to reference Yoshida A, Anand-Apte B, Zetter BR. Differential endothelial migration and proliferation to basic fibroblast growth factor and vascular endothelial growth factor. Growth Factors 1996; 13: 57–64PubMedCrossRef Yoshida A, Anand-Apte B, Zetter BR. Differential endothelial migration and proliferation to basic fibroblast growth factor and vascular endothelial growth factor. Growth Factors 1996; 13: 57–64PubMedCrossRef
153.
go back to reference Ferrara N, Davis-Smith T. The biology of vascular endothelial growth factor. Endocr Rev 1997; 18: 4–25PubMedCrossRef Ferrara N, Davis-Smith T. The biology of vascular endothelial growth factor. Endocr Rev 1997; 18: 4–25PubMedCrossRef
154.
go back to reference Peters KG, DeVries C, Williams LT. Vascular endothelial growth factor expression during embryogenesis and tissue repair suggests a role in endothelial differentiation and blood vessel growth. Proc Natl Acad Sci U S A 1993; 90: 8915–9PubMedCrossRef Peters KG, DeVries C, Williams LT. Vascular endothelial growth factor expression during embryogenesis and tissue repair suggests a role in endothelial differentiation and blood vessel growth. Proc Natl Acad Sci U S A 1993; 90: 8915–9PubMedCrossRef
155.
go back to reference Fong GH, Rossant J, Gertsenstein M, et al. Role of the Flt-1 receptor tyrosine kinase in regulating the assembly of vascular endothelium. Nature 1995; 376: 66–70PubMedCrossRef Fong GH, Rossant J, Gertsenstein M, et al. Role of the Flt-1 receptor tyrosine kinase in regulating the assembly of vascular endothelium. Nature 1995; 376: 66–70PubMedCrossRef
156.
go back to reference Guo D, Jia Q, Song HY, et al. Vascular endothelial cells growth factor promotes tyrosine phosphorylation of mediators of signal transduction that contain SH2 domains: association with endothelial cell proliferation. J Biol Chem 1995; 270: 6729–33PubMedCrossRef Guo D, Jia Q, Song HY, et al. Vascular endothelial cells growth factor promotes tyrosine phosphorylation of mediators of signal transduction that contain SH2 domains: association with endothelial cell proliferation. J Biol Chem 1995; 270: 6729–33PubMedCrossRef
157.
go back to reference Kroll J, Waltenberger J. The vascular endothelial growth factor receptor KDR activates multiple signal transduction pathways in porcine aortic endothelial cells. J Biol Chem 1997; 272: 32521–7PubMedCrossRef Kroll J, Waltenberger J. The vascular endothelial growth factor receptor KDR activates multiple signal transduction pathways in porcine aortic endothelial cells. J Biol Chem 1997; 272: 32521–7PubMedCrossRef
158.
go back to reference Igarashi K, Shigeta K, Isohara T, et al. Sck interacts with KDR and Flt-1 via its SH2 domain. Biochem Biophys Res Commun 1998; 251: 77–82PubMedCrossRef Igarashi K, Shigeta K, Isohara T, et al. Sck interacts with KDR and Flt-1 via its SH2 domain. Biochem Biophys Res Commun 1998; 251: 77–82PubMedCrossRef
159.
go back to reference Igarashi K, Isohara T, Kato T, et al. Tyrosine 1213 of Flt-1 is a major binding site of Nck and SHP-2. Biochem Biophys Res Commun 1998; 246: 95–9PubMedCrossRef Igarashi K, Isohara T, Kato T, et al. Tyrosine 1213 of Flt-1 is a major binding site of Nck and SHP-2. Biochem Biophys Res Commun 1998; 246: 95–9PubMedCrossRef
160.
go back to reference Mukhopadhyay D, Nagy JA, Manseau EJ, et al. Vascular permeability factor/vascular endothelial growth factor-mediated signaling in mouse mesentery vascular endothelium. Cancer Res 1998; 58: 1278–84PubMed Mukhopadhyay D, Nagy JA, Manseau EJ, et al. Vascular permeability factor/vascular endothelial growth factor-mediated signaling in mouse mesentery vascular endothelium. Cancer Res 1998; 58: 1278–84PubMed
161.
go back to reference Clauss M, Gerlach M, Brett J, et al. Vascular permeability factor: a tumor-derived polypeptide that induces endothelial cell and monocyte procoagulant activity, and promotes monocyte migration. J Exp Med 1990; 172: 1535–45PubMedCrossRef Clauss M, Gerlach M, Brett J, et al. Vascular permeability factor: a tumor-derived polypeptide that induces endothelial cell and monocyte procoagulant activity, and promotes monocyte migration. J Exp Med 1990; 172: 1535–45PubMedCrossRef
162.
go back to reference Gruber BL, Marchese MJ, Kew R. Angiogenic factors stimulate mast-cell migration. Blood 1995; 86: 2488–93PubMed Gruber BL, Marchese MJ, Kew R. Angiogenic factors stimulate mast-cell migration. Blood 1995; 86: 2488–93PubMed
163.
go back to reference Barleon B, Sozzani S, Zhou D, et al. Migration of human monocytes in response to vascular endothelial growth factor (VEGF) is mediated via the VEGF receptor flt-1. Blood 1996; 87 3336–43PubMed Barleon B, Sozzani S, Zhou D, et al. Migration of human monocytes in response to vascular endothelial growth factor (VEGF) is mediated via the VEGF receptor flt-1. Blood 1996; 87 3336–43PubMed
164.
go back to reference Seetharam L, Gotoh N, Mara Y, et al. A unique signal transduction from FlT tyrosine kinase, a receptor for vascular endothelial growth factor VEGF. Oncogene 1995; 10: 135–47PubMed Seetharam L, Gotoh N, Mara Y, et al. A unique signal transduction from FlT tyrosine kinase, a receptor for vascular endothelial growth factor VEGF. Oncogene 1995; 10: 135–47PubMed
165.
go back to reference Keck PJ, Hauser SD, Krivi G, et al. Vascular permeability factor, an endothelial cell mitogen related to PDGF. Science 1989; 246: 1309–12PubMedCrossRef Keck PJ, Hauser SD, Krivi G, et al. Vascular permeability factor, an endothelial cell mitogen related to PDGF. Science 1989; 246: 1309–12PubMedCrossRef
166.
go back to reference Leung DL, Cachianes G, Kuang WJ, et al. Vascular endothelial growth factor is a secreted angiogenic mitogen. Science 1996; 246: 1306–9CrossRef Leung DL, Cachianes G, Kuang WJ, et al. Vascular endothelial growth factor is a secreted angiogenic mitogen. Science 1996; 246: 1306–9CrossRef
167.
go back to reference Plouet J, Schilling J, Gospodarowicz D. Isolation and characterization of newly identified endothelial cell mitogen produced by AtT-20 cells. EMBO J 1989; 8: 3801–6PubMed Plouet J, Schilling J, Gospodarowicz D. Isolation and characterization of newly identified endothelial cell mitogen produced by AtT-20 cells. EMBO J 1989; 8: 3801–6PubMed
168.
go back to reference Midy V, Plouet J. Vasculotropin/vascular endothelial growth factor induces differentiation in cultured osteoblasts. Biochem Biophys Res Commun 1994; 199: 380–6PubMedCrossRef Midy V, Plouet J. Vasculotropin/vascular endothelial growth factor induces differentiation in cultured osteoblasts. Biochem Biophys Res Commun 1994; 199: 380–6PubMedCrossRef
169.
go back to reference Ullrich A, Gray A, Tam AW, et al. Insulin-like growth factor 1 receptor primary structure: comparison with insulin receptor suggests structural determinants that define functional specificity. EMBO J 1986; 5: 2503–12PubMed Ullrich A, Gray A, Tam AW, et al. Insulin-like growth factor 1 receptor primary structure: comparison with insulin receptor suggests structural determinants that define functional specificity. EMBO J 1986; 5: 2503–12PubMed
170.
go back to reference Werner H, Woloschak M, Stannard B, et al. The insulin-like growth factor receptor: molecular biology, heterogeneity and regulation. In: LeRoith D, editor. Insulin-like growth factors: molecular and cellular aspects. Boca Raton (FL): CRC Press, 1991: 17–47 Werner H, Woloschak M, Stannard B, et al. The insulin-like growth factor receptor: molecular biology, heterogeneity and regulation. In: LeRoith D, editor. Insulin-like growth factors: molecular and cellular aspects. Boca Raton (FL): CRC Press, 1991: 17–47
171.
go back to reference Lowe WL. Biological actions of the insulin-like growth factors. In: Le Roith D, editor. Insulin-like growth factors: molecular and cellular aspects. Boca Raton (FL): CRC Press, 1991: 49–85 Lowe WL. Biological actions of the insulin-like growth factors. In: Le Roith D, editor. Insulin-like growth factors: molecular and cellular aspects. Boca Raton (FL): CRC Press, 1991: 49–85
172.
go back to reference Huang S, Terstappen LWMM. Formation of haematopoietic microenvironment and haematopoietic stem cells from single human bone marrow stem cells. Nature 1992; 360: 745–9PubMedCrossRef Huang S, Terstappen LWMM. Formation of haematopoietic microenvironment and haematopoietic stem cells from single human bone marrow stem cells. Nature 1992; 360: 745–9PubMedCrossRef
173.
go back to reference Goldring MB, Goldring SR. Cytokines and cell growth control. Crit Rev Eukaryot Gene Expr 1991; 1: 301–26PubMed Goldring MB, Goldring SR. Cytokines and cell growth control. Crit Rev Eukaryot Gene Expr 1991; 1: 301–26PubMed
174.
go back to reference Condorelli G, Bueno R, Smith RJ. Two alternatively spliced forms of the human insulin-like growth factor I receptor have distinct biological activities and internalization kinetics. J Biol Chem 1994; 269: 8510–6PubMed Condorelli G, Bueno R, Smith RJ. Two alternatively spliced forms of the human insulin-like growth factor I receptor have distinct biological activities and internalization kinetics. J Biol Chem 1994; 269: 8510–6PubMed
175.
go back to reference Ota A, Wilson GL, Le Roith D. Insulin-like growth factor I receptors on mouse neuroblastoma cells: two beta subunits are derived from differences in glycosylation. Eur J Biochem 1988; 174: 521–30PubMedCrossRef Ota A, Wilson GL, Le Roith D. Insulin-like growth factor I receptors on mouse neuroblastoma cells: two beta subunits are derived from differences in glycosylation. Eur J Biochem 1988; 174: 521–30PubMedCrossRef
176.
go back to reference Tavare JM, Siddle K. Mutational analysis of insulin receptor function: consensus and controversy. Biochim Biophys Acta 1993; 1178: 21–39PubMedCrossRef Tavare JM, Siddle K. Mutational analysis of insulin receptor function: consensus and controversy. Biochim Biophys Acta 1993; 1178: 21–39PubMedCrossRef
177.
go back to reference Siddle K, Soos, MA, Field CE, et al. Hybrid and atypical insulin/insulin-like growth factor I receptors. Hormone Res 1994; 41: 56–65PubMedCrossRef Siddle K, Soos, MA, Field CE, et al. Hybrid and atypical insulin/insulin-like growth factor I receptors. Hormone Res 1994; 41: 56–65PubMedCrossRef
178.
go back to reference Sun XJ, Rothenberg P, Kahn CR, et al. The structure of the insulin receptor substrate IRS-1 defines a unique signal transduction protein. Nature 1991; 352: 73–7PubMedCrossRef Sun XJ, Rothenberg P, Kahn CR, et al. The structure of the insulin receptor substrate IRS-1 defines a unique signal transduction protein. Nature 1991; 352: 73–7PubMedCrossRef
179.
go back to reference Sun XJ, Miralpeix M, Myers MG, et al. The expression and function of IRS-1 in insulin signal transmission. J Biol Chem 1992; 267: 22662–72PubMed Sun XJ, Miralpeix M, Myers MG, et al. The expression and function of IRS-1 in insulin signal transmission. J Biol Chem 1992; 267: 22662–72PubMed
180.
go back to reference Giorgetti S, Ballotti R, Kowalski-Chauvel A, et al. The insulin and insulin-like growth factor-1 receptor substrate IRS-1 associates with and activates phosphatidylinositol 3-kinase in vitro. J Biol Chem 1993; 268: 7358–64PubMed Giorgetti S, Ballotti R, Kowalski-Chauvel A, et al. The insulin and insulin-like growth factor-1 receptor substrate IRS-1 associates with and activates phosphatidylinositol 3-kinase in vitro. J Biol Chem 1993; 268: 7358–64PubMed
181.
go back to reference Yamauchi K, Pessin JE. Insulin receptor substrate-1 (IRSl)and Shc compete for a limited pool of Grb2 in mediating insulin downstream signalling. J Biol Chem 1994; 269: 31107–14PubMed Yamauchi K, Pessin JE. Insulin receptor substrate-1 (IRSl)and Shc compete for a limited pool of Grb2 in mediating insulin downstream signalling. J Biol Chem 1994; 269: 31107–14PubMed
182.
go back to reference Sasaoka T, Rose DW, Jhun BH, et al. Evidence for a functional role of Shc proteins in mitogenic signalling induced by insulin, insulin-like growth factor-1, and epidermal growth factor. J Biol Chem 1994; 269: 13689–94PubMed Sasaoka T, Rose DW, Jhun BH, et al. Evidence for a functional role of Shc proteins in mitogenic signalling induced by insulin, insulin-like growth factor-1, and epidermal growth factor. J Biol Chem 1994; 269: 13689–94PubMed
183.
go back to reference Heitner-Johnson D, LeRoith D. Insulin-like growth factor-I stimulated tyrosine phosphorylation of endogenous c-Crk. J Biol Chem 1995; 290: 5187–90 Heitner-Johnson D, LeRoith D. Insulin-like growth factor-I stimulated tyrosine phosphorylation of endogenous c-Crk. J Biol Chem 1995; 290: 5187–90
184.
go back to reference Matsuda M, Hshimoti Y, Muroya K, et al. CRK protein binds to two guanine nucleotide-releasing proteins for the Ras family and modulates nerve growth factor-induced activation of Ras in PC12 cells. Mol Cel Biol 1994; 14: 5495–500 Matsuda M, Hshimoti Y, Muroya K, et al. CRK protein binds to two guanine nucleotide-releasing proteins for the Ras family and modulates nerve growth factor-induced activation of Ras in PC12 cells. Mol Cel Biol 1994; 14: 5495–500
185.
go back to reference Clemmons DR, Van Wyk JJ. Somatomedin: physiological control and effects on cell proliferation. In: Baserga R, editor. Tissue growth factors. Berlin: Springer-Verlag KG, 1981; 161CrossRef Clemmons DR, Van Wyk JJ. Somatomedin: physiological control and effects on cell proliferation. In: Baserga R, editor. Tissue growth factors. Berlin: Springer-Verlag KG, 1981; 161CrossRef
186.
go back to reference Clemmons DR, Shaw DS. Variables controlling somatomedin production by cultured human fibroblasts. J Cell Physiol 1983; 115: 137–42PubMedCrossRef Clemmons DR, Shaw DS. Variables controlling somatomedin production by cultured human fibroblasts. J Cell Physiol 1983; 115: 137–42PubMedCrossRef
187.
go back to reference Baserga R, Sell C, Porcu P, et al. The role of the IGF-I receptor in the growth and transformation of mammalian cells. Cell Prolif 1994; 27: 63–71PubMedCrossRef Baserga R, Sell C, Porcu P, et al. The role of the IGF-I receptor in the growth and transformation of mammalian cells. Cell Prolif 1994; 27: 63–71PubMedCrossRef
188.
go back to reference Pietrzkowski Z, Wernicke D, Porcu P, et al. Inhibition of cell proliferation by peptide analogs of IGF-1. Cancer Res 1992; 52: 6447PubMed Pietrzkowski Z, Wernicke D, Porcu P, et al. Inhibition of cell proliferation by peptide analogs of IGF-1. Cancer Res 1992; 52: 6447PubMed
189.
go back to reference Travali S, Reiss K, Ferber A, et al. Constitutively expressed c-myb abrogates the requirement for insulin-like growth factor I in 3T3 fibroblasts. Mol Cell Biol 1991; 11: 731–6PubMed Travali S, Reiss K, Ferber A, et al. Constitutively expressed c-myb abrogates the requirement for insulin-like growth factor I in 3T3 fibroblasts. Mol Cell Biol 1991; 11: 731–6PubMed
190.
go back to reference Reiss K, Ferger A, Travali S, et al. The proto-oncogene c-myb increases the expression of insulin-like growth factor 1 and insulin-like growth factor 1 receptor messenger RNAs by a transcriptional mechanism. Cancer Res 1991; 51: 5997–6000PubMed Reiss K, Ferger A, Travali S, et al. The proto-oncogene c-myb increases the expression of insulin-like growth factor 1 and insulin-like growth factor 1 receptor messenger RNAs by a transcriptional mechanism. Cancer Res 1991; 51: 5997–6000PubMed
191.
go back to reference Pietrzkowski Z, Lammers, R, Carpenter G, et al. Constitutive expression of insulin-like growth factor 1 and insulin-like growth 1 receptor abrogates all requirements for exogenous growth factors. Cell Growth Differ 1992; 3: 199–205PubMed Pietrzkowski Z, Lammers, R, Carpenter G, et al. Constitutive expression of insulin-like growth factor 1 and insulin-like growth 1 receptor abrogates all requirements for exogenous growth factors. Cell Growth Differ 1992; 3: 199–205PubMed
192.
go back to reference Porcu P, Ferber A, Pietrzkowski Z, et al. The growth-stimulatory effect of Simian virus 40 T antigen requires the interaction of insulin-like growth factor 1 with its receptor. Mol Cell Biol 1992; 12: 5069–77PubMed Porcu P, Ferber A, Pietrzkowski Z, et al. The growth-stimulatory effect of Simian virus 40 T antigen requires the interaction of insulin-like growth factor 1 with its receptor. Mol Cell Biol 1992; 12: 5069–77PubMed
193.
go back to reference Reiss K, Porcu P, Sell C, et al. The insulin-like growth factor 1 receptor is required for the proliferation of hematopoietic cells. Oncogene 1992; 7: 2243–8PubMed Reiss K, Porcu P, Sell C, et al. The insulin-like growth factor 1 receptor is required for the proliferation of hematopoietic cells. Oncogene 1992; 7: 2243–8PubMed
194.
go back to reference Resnicoff M, Sell C, Rubini M, et al. Rat glioblastoma cells expressing an antisense RNA to the insulin-like growth factor-I (IGF-I) receptor are non-tumorigenic and induce of wild type tumors. Cancer Res 1994; 54: 2218–22PubMed Resnicoff M, Sell C, Rubini M, et al. Rat glioblastoma cells expressing an antisense RNA to the insulin-like growth factor-I (IGF-I) receptor are non-tumorigenic and induce of wild type tumors. Cancer Res 1994; 54: 2218–22PubMed
195.
go back to reference Pietrzkowski Z, Mulholland G, Gomella L, et al. Inhibition of growth of prostatic cancer cell lines by peptide analogs of IGF-1. Cancer Res 1993; 53: 1102–6PubMed Pietrzkowski Z, Mulholland G, Gomella L, et al. Inhibition of growth of prostatic cancer cell lines by peptide analogs of IGF-1. Cancer Res 1993; 53: 1102–6PubMed
196.
go back to reference Sell C, Rubini M, Rubin R, et al. Simian viras 40 large tumor antigen is unable to transform mouse embryonic fibroblasts lacking type-I IGF receptor. Proc Natl Acad Sci U S A 1993; 90: 11217–21PubMedCrossRef Sell C, Rubini M, Rubin R, et al. Simian viras 40 large tumor antigen is unable to transform mouse embryonic fibroblasts lacking type-I IGF receptor. Proc Natl Acad Sci U S A 1993; 90: 11217–21PubMedCrossRef
197.
go back to reference Baserga R, Sell C, Porcu P, et al. The role of the IGF-I receptor in the growth and transformation of mammalian cells. Cell Prolif 1994; 27: 63–71PubMedCrossRef Baserga R, Sell C, Porcu P, et al. The role of the IGF-I receptor in the growth and transformation of mammalian cells. Cell Prolif 1994; 27: 63–71PubMedCrossRef
198.
go back to reference Kan M, Zhang G, Zarnegar R, et al. Hepatocyte growth factor/hepatopoietin A stimulates the growth of rat kidney proximal tubule epithelial cells (RPTE), rat nonparenchymal liver cells, human melanoma cells, mouse keratinocytes and stimulates anchorage-independent growth of SV40-transformed RPTE. Biochem Biophys Res Commun 1991; 174: 331–7PubMedCrossRef Kan M, Zhang G, Zarnegar R, et al. Hepatocyte growth factor/hepatopoietin A stimulates the growth of rat kidney proximal tubule epithelial cells (RPTE), rat nonparenchymal liver cells, human melanoma cells, mouse keratinocytes and stimulates anchorage-independent growth of SV40-transformed RPTE. Biochem Biophys Res Commun 1991; 174: 331–7PubMedCrossRef
199.
go back to reference Stoker M, Gherardi E, Perryman M, et al. Scatter factor is a fibroblast-derived modulator of epithelial cell mobility. Nature 1987; 327: 239–342PubMedCrossRef Stoker M, Gherardi E, Perryman M, et al. Scatter factor is a fibroblast-derived modulator of epithelial cell mobility. Nature 1987; 327: 239–342PubMedCrossRef
200.
go back to reference Bussolino F, Di Renzo MF, Ziche M, et al. Hepatocyte growth factor is a potent angiogenic factor which stimulates endothelial cell motility and growth. J Cell Biol 1992; 119: 629–41PubMedCrossRef Bussolino F, Di Renzo MF, Ziche M, et al. Hepatocyte growth factor is a potent angiogenic factor which stimulates endothelial cell motility and growth. J Cell Biol 1992; 119: 629–41PubMedCrossRef
201.
go back to reference Grant DS, Kleinman, HK, Goldberg ID, et al. Scatter factor induces blood vessel formation in vivo. Proc Natl Acad Sci U S A 1993; 90: 1937–41PubMedCrossRef Grant DS, Kleinman, HK, Goldberg ID, et al. Scatter factor induces blood vessel formation in vivo. Proc Natl Acad Sci U S A 1993; 90: 1937–41PubMedCrossRef
202.
go back to reference Weidner KM, Behrens J, Vanderkerckhone J, et al. Scatter factor: molecular characteristics and effect on the invasiveness of epithelial cells. J Cell Biol 1990; 111: 2907–11CrossRef Weidner KM, Behrens J, Vanderkerckhone J, et al. Scatter factor: molecular characteristics and effect on the invasiveness of epithelial cells. J Cell Biol 1990; 111: 2907–11CrossRef
203.
go back to reference Weidner KM, Hartmann G, Naldini L, et al. Molecular characteristics of HGF/SF and its role in cell motility and invasion. EXS 1993; 65: 311–28PubMed Weidner KM, Hartmann G, Naldini L, et al. Molecular characteristics of HGF/SF and its role in cell motility and invasion. EXS 1993; 65: 311–28PubMed
204.
go back to reference Giordano S, Ponzetto D, Di Renzo MF, et al. Tyrosine kinase receptor indistinguishable from the c-met protein. Nature 2989; 339: 155–6CrossRef Giordano S, Ponzetto D, Di Renzo MF, et al. Tyrosine kinase receptor indistinguishable from the c-met protein. Nature 2989; 339: 155–6CrossRef
205.
go back to reference Gonzatti-Haces M, Seth A, Park M, et al. Characterization of the TPR-MET oncogene p65 and the MET protooncogene p140 protein tyrosine kinases. Proc Natl Acad Sci U S A 1988; 85: 21–5PubMedCrossRef Gonzatti-Haces M, Seth A, Park M, et al. Characterization of the TPR-MET oncogene p65 and the MET protooncogene p140 protein tyrosine kinases. Proc Natl Acad Sci U S A 1988; 85: 21–5PubMedCrossRef
206.
go back to reference Prat M, Crepaldi T, Gandino L, et al. C-terminal truncated forms of Met, the hepatocyte growth factor receptor. Mol Cell Biol 1991; 11: 5954–60PubMed Prat M, Crepaldi T, Gandino L, et al. C-terminal truncated forms of Met, the hepatocyte growth factor receptor. Mol Cell Biol 1991; 11: 5954–60PubMed
207.
go back to reference Crepaldi T, Prat M, Giordano S, et al. Generation of a truncated hepatocyte growth factor receptor in the endoplasmic reticulum. J Biol Chem 1994; 269: 1750–5PubMed Crepaldi T, Prat M, Giordano S, et al. Generation of a truncated hepatocyte growth factor receptor in the endoplasmic reticulum. J Biol Chem 1994; 269: 1750–5PubMed
208.
go back to reference Cooper CS. HGFR. In: Hardie G, Hanks S, editors. The protein kinase facts book. New York: Academic Press, 1995: 218–20CrossRef Cooper CS. HGFR. In: Hardie G, Hanks S, editors. The protein kinase facts book. New York: Academic Press, 1995: 218–20CrossRef
210.
go back to reference Callard RE, Gearing AJH. The cytokine facts book. London: Academic Press, 1994 Callard RE, Gearing AJH. The cytokine facts book. London: Academic Press, 1994
211.
go back to reference Lin H, Wang XF, Ng-Eaton E, et al. Expression cloning of the TGF-ß type II receptor a functional transmembrane serine/threonine kinase. Cell 1992; 68: 775–85PubMedCrossRef Lin H, Wang XF, Ng-Eaton E, et al. Expression cloning of the TGF-ß type II receptor a functional transmembrane serine/threonine kinase. Cell 1992; 68: 775–85PubMedCrossRef
212.
go back to reference Wrana JL, Attisano L, Carcamo J, et al. TGF-ß signals through a heteromeric protein kinase receptor complex. Cell 1992; 71: 1003–14PubMedCrossRef Wrana JL, Attisano L, Carcamo J, et al. TGF-ß signals through a heteromeric protein kinase receptor complex. Cell 1992; 71: 1003–14PubMedCrossRef
213.
go back to reference Kekow J, Wiedemann GJ. Transforming growth factor ß: a cytokine with multiple actions in oncology and potential clinical applications [review]. Int J Oncol 1995; 7: 177–82PubMed Kekow J, Wiedemann GJ. Transforming growth factor ß: a cytokine with multiple actions in oncology and potential clinical applications [review]. Int J Oncol 1995; 7: 177–82PubMed
214.
go back to reference Heldin CH, Miyazono K, ten Dijke P. TGFß-signalling from cell membrane to nucleus through SMAD proteins. Nature 1997; 390: 465–71PubMedCrossRef Heldin CH, Miyazono K, ten Dijke P. TGFß-signalling from cell membrane to nucleus through SMAD proteins. Nature 1997; 390: 465–71PubMedCrossRef
215.
go back to reference Yamashita H, ten Dijke P, Franzen P, et al. Formation of heterooligomeric complexes of type I and type II receptors for transforming growth factor-ß. J Biol Chem 1994; 269: 20172–8PubMed Yamashita H, ten Dijke P, Franzen P, et al. Formation of heterooligomeric complexes of type I and type II receptors for transforming growth factor-ß. J Biol Chem 1994; 269: 20172–8PubMed
216.
go back to reference Souchelnytskyi S, Tamaki K, Engstom U, et al. Phosphorylation of Ser465 and Ser467 in the C-terminus of Smad2 mediates interaction with Smad4 and is required for TGF-ß signalling. J Biol Chem 1997; 272: 28107–15PubMedCrossRef Souchelnytskyi S, Tamaki K, Engstom U, et al. Phosphorylation of Ser465 and Ser467 in the C-terminus of Smad2 mediates interaction with Smad4 and is required for TGF-ß signalling. J Biol Chem 1997; 272: 28107–15PubMedCrossRef
217.
go back to reference Nakao A, Afrakhte M, Moren A, et al. Identification of Smad7, a TGFß-inducible antagonist of TGF-ß signalling. Nature 1997; 389: 631–5PubMedCrossRef Nakao A, Afrakhte M, Moren A, et al. Identification of Smad7, a TGFß-inducible antagonist of TGF-ß signalling. Nature 1997; 389: 631–5PubMedCrossRef
218.
go back to reference Imamura T, Takase M, Nishihara A, et al. Smad6 inhibits signalling by the TGF-ß superfamily. Nature 1997; 389: 622–6PubMedCrossRef Imamura T, Takase M, Nishihara A, et al. Smad6 inhibits signalling by the TGF-ß superfamily. Nature 1997; 389: 622–6PubMedCrossRef
219.
220.
go back to reference Powell SM, Harper JC, Hamilton SR, et al. Inactivation of Smad4 in gastric carcinomas. Cancer Res 1997; 57: 4221–4PubMed Powell SM, Harper JC, Hamilton SR, et al. Inactivation of Smad4 in gastric carcinomas. Cancer Res 1997; 57: 4221–4PubMed
221.
go back to reference Riggins GJ, Kinzler KW, Vogelstein B, et al. Frequency of Smad gene mutations in human cancers. Cancer Res 1997; 57: 2578–80PubMed Riggins GJ, Kinzler KW, Vogelstein B, et al. Frequency of Smad gene mutations in human cancers. Cancer Res 1997; 57: 2578–80PubMed
222.
go back to reference Battegay EJ, Raines EW, Seifert RA, et al. TGF-ß induces bimodal proliferation of connective tissue cells via complex control of an autocrine PDGF loop. Cell 1990; 63: 515–24PubMedCrossRef Battegay EJ, Raines EW, Seifert RA, et al. TGF-ß induces bimodal proliferation of connective tissue cells via complex control of an autocrine PDGF loop. Cell 1990; 63: 515–24PubMedCrossRef
223.
go back to reference Luttrell DK, Lee A, Lansing TJ, et al. Involvement of pp60c-src with two major signaling pathways in human breast cancer. Proc Natl Acad Sci U S A 1994; 91: 83–7PubMedCrossRef Luttrell DK, Lee A, Lansing TJ, et al. Involvement of pp60c-src with two major signaling pathways in human breast cancer. Proc Natl Acad Sci U S A 1994; 91: 83–7PubMedCrossRef
224.
go back to reference Maa MC, Leu TH, McCarley DJ, et al. Potentiation of epidermal growth factor receptor-mediated oncogenesis by c-Src: Implications for the etiology of multiple human cancers. Proc Natl Acad Sci U S A 1995; 92: 6981–5PubMedCrossRef Maa MC, Leu TH, McCarley DJ, et al. Potentiation of epidermal growth factor receptor-mediated oncogenesis by c-Src: Implications for the etiology of multiple human cancers. Proc Natl Acad Sci U S A 1995; 92: 6981–5PubMedCrossRef
225.
go back to reference Wilson LK, Luttrell DK, Parsons JT, et al. pp60c-src tyrosine kinase, myristylation, and modulatory domains are required for enhanced mitogenic responsiveness to epidermal growth factor seen in cells overexpressing c-src. Mol Cell Biol 1989; 9: 1536–44PubMed Wilson LK, Luttrell DK, Parsons JT, et al. pp60c-src tyrosine kinase, myristylation, and modulatory domains are required for enhanced mitogenic responsiveness to epidermal growth factor seen in cells overexpressing c-src. Mol Cell Biol 1989; 9: 1536–44PubMed
226.
go back to reference Bolen JB. Nonreceptor tyrosine protein kinases. Oncogene 1993; 8: 2025–31PubMed Bolen JB. Nonreceptor tyrosine protein kinases. Oncogene 1993; 8: 2025–31PubMed
227.
go back to reference Chang JH, Wilson LK, Moyers JS, et al. Increased levels of p21ras-GTP and enhanced DNA synthesis accompany elevated tyrosyl phosphorylation of GAP-associated proteins, p190 and p62, in c-src overexpressors. Oncogene 1993; 8: 959–67PubMed Chang JH, Wilson LK, Moyers JS, et al. Increased levels of p21ras-GTP and enhanced DNA synthesis accompany elevated tyrosyl phosphorylation of GAP-associated proteins, p190 and p62, in c-src overexpressors. Oncogene 1993; 8: 959–67PubMed
228.
go back to reference Maa MC, Wilson LK, Moyers JS, et al. Identification and characterization of a cytoskeleton-associated, epidermal growth factor sensitive pp60c-src substrate. Oncogene 1992; 7: 2429–38PubMed Maa MC, Wilson LK, Moyers JS, et al. Identification and characterization of a cytoskeleton-associated, epidermal growth factor sensitive pp60c-src substrate. Oncogene 1992; 7: 2429–38PubMed
229.
go back to reference Hardie G, Hanks S, editors. The protein kinase facts book. New York: Academic Press, 1995 Hardie G, Hanks S, editors. The protein kinase facts book. New York: Academic Press, 1995
230.
go back to reference Zhang W, Sloan-Lancaster J, Kitchen J, et al. LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. Cell 1998; 92: 83–92PubMedCrossRef Zhang W, Sloan-Lancaster J, Kitchen J, et al. LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. Cell 1998; 92: 83–92PubMedCrossRef
231.
go back to reference Cartwright CA, Kamps MP, Meisler AI, et al. pp60c-src activation in human colon carcinoma. J Clin Invest 1989; 3: 2025–33CrossRef Cartwright CA, Kamps MP, Meisler AI, et al. pp60c-src activation in human colon carcinoma. J Clin Invest 1989; 3: 2025–33CrossRef
232.
go back to reference Ottenholf-Kaliff AE, Rijksen G, van Beurden EA, et al. Characterization of protein tyrosine kinases from human breast cancer: involvement of the c-src oncogene product. Cancer Res 1992; 52: 4773–8 Ottenholf-Kaliff AE, Rijksen G, van Beurden EA, et al. Characterization of protein tyrosine kinases from human breast cancer: involvement of the c-src oncogene product. Cancer Res 1992; 52: 4773–8
233.
go back to reference Rosen N, Bolen JB, Schwartz AM, et al. Analysis of pp60c-src protein kinase activity in human tumor cell lines and tissues. J Biol Chem 1986; 261: 13754–9PubMed Rosen N, Bolen JB, Schwartz AM, et al. Analysis of pp60c-src protein kinase activity in human tumor cell lines and tissues. J Biol Chem 1986; 261: 13754–9PubMed
234.
go back to reference Park J, Cartwright CA. Src activity increases and Yes activity decreases during mitosis of human colon carcinoma cells. Mol Cell Biol 1995; 15: 2374–82PubMed Park J, Cartwright CA. Src activity increases and Yes activity decreases during mitosis of human colon carcinoma cells. Mol Cell Biol 1995; 15: 2374–82PubMed
235.
go back to reference Park J, Meisler AI, Cartwright CA. c-Yes tyrosine kinase activity in human colon carcinoma. Oncogene 1993; 8: 2627–35PubMed Park J, Meisler AI, Cartwright CA. c-Yes tyrosine kinase activity in human colon carcinoma. Oncogene 1993; 8: 2627–35PubMed
236.
go back to reference Han NM, Curley SA, Gallick GE. Differential activation of pp60c-src and pp62c-yes in human colorectal carcinoma liver metastases. Clin Cancer Res 1996; 2: 1397–404PubMed Han NM, Curley SA, Gallick GE. Differential activation of pp60c-src and pp62c-yes in human colorectal carcinoma liver metastases. Clin Cancer Res 1996; 2: 1397–404PubMed
237.
go back to reference Willman CL, Stewart CC, Longacre TL, et al. Expression of the c-fgr and hck protein-tyrosine kinases in acute myeloid leukemic blasts is associated with early commitment and differentiation events in the monocytic and granulocytic lineages. Blood 1991; 77: 726–34PubMed Willman CL, Stewart CC, Longacre TL, et al. Expression of the c-fgr and hck protein-tyrosine kinases in acute myeloid leukemic blasts is associated with early commitment and differentiation events in the monocytic and granulocytic lineages. Blood 1991; 77: 726–34PubMed
238.
go back to reference Krueger J, Zhao YH, Murphy D, et al. Differential expression of p62c-yes in normal, hyperplastic and neoplastic human epidermis. Oncogene 1991; 6: 933–40PubMed Krueger J, Zhao YH, Murphy D, et al. Differential expression of p62c-yes in normal, hyperplastic and neoplastic human epidermis. Oncogene 1991; 6: 933–40PubMed
239.
go back to reference Seki T, Fujii G, Mori S, et al. Amplification of c-yes-1 protooncogene in a primary human gastric cancer. Jpn J Cancer Res 1985; 76: 907–10PubMed Seki T, Fujii G, Mori S, et al. Amplification of c-yes-1 protooncogene in a primary human gastric cancer. Jpn J Cancer Res 1985; 76: 907–10PubMed
240.
go back to reference Abts H, Juecker M, Diehl V, et al. Human chronic lymphocytic leukemia cells regularly express mRNAs of the protooncogenes lck and c-fgr. Leuk Res 1991; 15: 987–97PubMedCrossRef Abts H, Juecker M, Diehl V, et al. Human chronic lymphocytic leukemia cells regularly express mRNAs of the protooncogenes lck and c-fgr. Leuk Res 1991; 15: 987–97PubMedCrossRef
241.
go back to reference von Knethen A, Abts H, Kube D, et al. The expression of the P56-LCK proto-oncogene in B-cell lineage neoplasias. Ann Hematol 1993; 67: A66 von Knethen A, Abts H, Kube D, et al. The expression of the P56-LCK proto-oncogene in B-cell lineage neoplasias. Ann Hematol 1993; 67: A66
242.
go back to reference Rouer E, Dreyfus F, Melle J, et al. Selective increase of alternatively spliced Lck transcripts from the proximal promoter in hematopoietic malignancies. Leukemia 1993; 7: 246–50PubMed Rouer E, Dreyfus F, Melle J, et al. Selective increase of alternatively spliced Lck transcripts from the proximal promoter in hematopoietic malignancies. Leukemia 1993; 7: 246–50PubMed
243.
go back to reference Juecker M, Abts H, Eick D, et al. Over-expression of lck in Burkitt’s lymphoma cell lines [letter]. Leukemia 1991; 5: 528–30 Juecker M, Abts H, Eick D, et al. Over-expression of lck in Burkitt’s lymphoma cell lines [letter]. Leukemia 1991; 5: 528–30
244.
go back to reference Burnett RC, David JC, Harden AM, et al. The LCK gene is involved in the t(1;7)(p34;q34) in the T-cell acute lymphoblastic leukemia derived cell line, HSB-2. Genes, Chromosomes Cancer 1991; 3: 461–7PubMedCrossRef Burnett RC, David JC, Harden AM, et al. The LCK gene is involved in the t(1;7)(p34;q34) in the T-cell acute lymphoblastic leukemia derived cell line, HSB-2. Genes, Chromosomes Cancer 1991; 3: 461–7PubMedCrossRef
245.
go back to reference Koga Y, Kimura N, Minowada J, et al. Expression of the human T-cell-specific tyrosine kinase YT16 (lck) message in leukemic T-cell lines. Cancer Res 1988; 48: 856–9PubMed Koga Y, Kimura N, Minowada J, et al. Expression of the human T-cell-specific tyrosine kinase YT16 (lck) message in leukemic T-cell lines. Cancer Res 1988; 48: 856–9PubMed
246.
go back to reference Nakamura K, Chijiiwa Y, Nawata H. Augmented expression of LCK message directed from the downstream promoter in human colorectal cancer specimens. Eur J Cancer 1996; 32A: 1401–7PubMedCrossRef Nakamura K, Chijiiwa Y, Nawata H. Augmented expression of LCK message directed from the downstream promoter in human colorectal cancer specimens. Eur J Cancer 1996; 32A: 1401–7PubMedCrossRef
247.
go back to reference Mayer K, Ballhausen WG. Expression of alternatively spliced lck transcripts from the proximal promoter in colorectal cancer derived cell lines. Anticancer Res 1996; 16: 1733–7PubMed Mayer K, Ballhausen WG. Expression of alternatively spliced lck transcripts from the proximal promoter in colorectal cancer derived cell lines. Anticancer Res 1996; 16: 1733–7PubMed
248.
go back to reference Veilette A, Foss FM, Sausville EA, et al. Expression of the lck tyrosine kinase gene in human colon carcinoma and other non-lymphoid human tumor cell lines. Oncogene Res 1987; 1: 357–74 Veilette A, Foss FM, Sausville EA, et al. Expression of the lck tyrosine kinase gene in human colon carcinoma and other non-lymphoid human tumor cell lines. Oncogene Res 1987; 1: 357–74
249.
go back to reference McCracken S, Kim CS, Xu Y, et al. An alternative pathway of expression of p56-lck from type I promoter transcripts in colon carcinoma. Oncogene 1997; 15: 2929–37PubMedCrossRef McCracken S, Kim CS, Xu Y, et al. An alternative pathway of expression of p56-lck from type I promoter transcripts in colon carcinoma. Oncogene 1997; 15: 2929–37PubMedCrossRef
250.
go back to reference Foss FM, Veillette A, Sartor O, et al. Alterations in the expression of pp60(c-src) an p56(lck) associated with butyrate-induced differentiation of human colon carcinoma cells. Oncogen Res 1989; 5: 13–23 Foss FM, Veillette A, Sartor O, et al. Alterations in the expression of pp60(c-src) an p56(lck) associated with butyrate-induced differentiation of human colon carcinoma cells. Oncogen Res 1989; 5: 13–23
251.
go back to reference Nowell PC, Hungerford DA. A minute chromosome in human granulocyte leukemia. Science 1960; 132: 1497–500 Nowell PC, Hungerford DA. A minute chromosome in human granulocyte leukemia. Science 1960; 132: 1497–500
252.
go back to reference Zarn JA, Zimmermann SM, Pass MK, et al. Association of CD24 with the kinase c-fgr in a small cell lung cancer cell line and with the kinase lyn in an erythroleukemia cell line. Biochem Biophys Res Commun 1996; 225: 384–91PubMedCrossRef Zarn JA, Zimmermann SM, Pass MK, et al. Association of CD24 with the kinase c-fgr in a small cell lung cancer cell line and with the kinase lyn in an erythroleukemia cell line. Biochem Biophys Res Commun 1996; 225: 384–91PubMedCrossRef
253.
go back to reference Tesch H, Abst H, Juecker M, et al. Expression of c-fgr in EBV positive and negative B cell tumors. Leukemia 1989; 3: 897–8PubMed Tesch H, Abst H, Juecker M, et al. Expression of c-fgr in EBV positive and negative B cell tumors. Leukemia 1989; 3: 897–8PubMed
254.
go back to reference Cheah MS, Ley TJ, Tronick SR, et al. fgr proto-oncogene mRNA induced in B lymphocytes by Epstein-Barr virus infection. Nature 1986; 319: 238–40PubMedCrossRef Cheah MS, Ley TJ, Tronick SR, et al. fgr proto-oncogene mRNA induced in B lymphocytes by Epstein-Barr virus infection. Nature 1986; 319: 238–40PubMedCrossRef
255.
go back to reference Faulkner L, Katz DR, Brickell PM. Retinoic acid induces changes in c-fgr proto-oncogene mRNA levels in Burkitt’s lymphoma cells. Immunobiology 1993; 188: 460–8PubMedCrossRef Faulkner L, Katz DR, Brickell PM. Retinoic acid induces changes in c-fgr proto-oncogene mRNA levels in Burkitt’s lymphoma cells. Immunobiology 1993; 188: 460–8PubMedCrossRef
256.
go back to reference Sharp NA, Luscombe MJ, Clemens MJ. Regulation of c-fgr proto-oncogene expression in Burkitt’s lymphoma cells: effect of interferon treatment and relationship to EBV status and c-myc mRNA levels. Oncogene 1989; 4: 1043–6PubMed Sharp NA, Luscombe MJ, Clemens MJ. Regulation of c-fgr proto-oncogene expression in Burkitt’s lymphoma cells: effect of interferon treatment and relationship to EBV status and c-myc mRNA levels. Oncogene 1989; 4: 1043–6PubMed
257.
go back to reference Nishio H, Nakamura S, Horai T, et al. Clinical and histopathologic evaluation of the expression of Ha-ras and fes oncogene products in lung cancer. Cancer 1992; 69: 1130–6PubMedCrossRef Nishio H, Nakamura S, Horai T, et al. Clinical and histopathologic evaluation of the expression of Ha-ras and fes oncogene products in lung cancer. Cancer 1992; 69: 1130–6PubMedCrossRef
258.
go back to reference Goldman J, Kowalczuk MM, Lafuze JE. Detection of a putative fusion product formed from tumor necrosis factor receptor (TNFR) and the FES/FPS oncogene from probing of two adolescent T-cell ALL substracted cDNA libraries [abstract]. Proc Am Assoc Cancer Res 1994; 35: A3483 Goldman J, Kowalczuk MM, Lafuze JE. Detection of a putative fusion product formed from tumor necrosis factor receptor (TNFR) and the FES/FPS oncogene from probing of two adolescent T-cell ALL substracted cDNA libraries [abstract]. Proc Am Assoc Cancer Res 1994; 35: A3483
259.
go back to reference Morris C, Heisterkamp N, Hao QL, et al. The human tyrosine kinase gene (FER) maps to chromosome 5 and is deleted in myeloid leukemias with a del(5q). Cytogenics Cell Genet 1990; 53: 196–200CrossRef Morris C, Heisterkamp N, Hao QL, et al. The human tyrosine kinase gene (FER) maps to chromosome 5 and is deleted in myeloid leukemias with a del(5q). Cytogenics Cell Genet 1990; 53: 196–200CrossRef
260.
go back to reference Takemoto S, Mulloy JC, Cereseto A, et al. Proliferation of adult T cell leukemia/lymphoma cells is associated with the constitutive activation of JAK/STAT proteins. Proc Natl Acad Sci US A 1997; 94: 13897–902CrossRef Takemoto S, Mulloy JC, Cereseto A, et al. Proliferation of adult T cell leukemia/lymphoma cells is associated with the constitutive activation of JAK/STAT proteins. Proc Natl Acad Sci US A 1997; 94: 13897–902CrossRef
261.
go back to reference Meydan N, Grunberger T, Dadi H, et al. Inhibition of acute lymphoblastic leukaemia by a Jak-2 inhibitor. Nature 1996; 379: 645–8PubMedCrossRef Meydan N, Grunberger T, Dadi H, et al. Inhibition of acute lymphoblastic leukaemia by a Jak-2 inhibitor. Nature 1996; 379: 645–8PubMedCrossRef
262.
go back to reference Ratovitski EA, Kotzbauer PT, Milbrandt J, et al. Midkine induces tumor cell proliferation and binds to a high affinity signaling receptor associated with JAK tyrosine kinases. J Biol Chem 1998; 273: 3654–60PubMedCrossRef Ratovitski EA, Kotzbauer PT, Milbrandt J, et al. Midkine induces tumor cell proliferation and binds to a high affinity signaling receptor associated with JAK tyrosine kinases. J Biol Chem 1998; 273: 3654–60PubMedCrossRef
263.
go back to reference Murata T, Noguchi PD, Puri RK. IL-13 induces phosphorylation and activation of Jak2 Janus kinase in human colon carcinoma cell lines: similarities between IL-4 and IL-12 signaling. J Immunol 1996; 156: 2972–8PubMed Murata T, Noguchi PD, Puri RK. IL-13 induces phosphorylation and activation of Jak2 Janus kinase in human colon carcinoma cell lines: similarities between IL-4 and IL-12 signaling. J Immunol 1996; 156: 2972–8PubMed
264.
go back to reference Okamoto H, Nakamori S, Ohigashi H, et al. Involvement of focal adhesion kinase (FAK) in endothelial cell retraction during cancer cell invasion [abstract]. Proc Annu Meet Am Assoc Cancer Res 1997; 38: A349 Okamoto H, Nakamori S, Ohigashi H, et al. Involvement of focal adhesion kinase (FAK) in endothelial cell retraction during cancer cell invasion [abstract]. Proc Annu Meet Am Assoc Cancer Res 1997; 38: A349
265.
go back to reference Hubbard SL, Dirks P, Murakami M, et al. Expression of focal adhesion kinase (FAK) in human astrocytoma cell lines and brain tumors [abstract]. Proc Annu Meet Am Assoc Cancer Res 1996; 37: A315 Hubbard SL, Dirks P, Murakami M, et al. Expression of focal adhesion kinase (FAK) in human astrocytoma cell lines and brain tumors [abstract]. Proc Annu Meet Am Assoc Cancer Res 1996; 37: A315
266.
go back to reference Weiner TM, Liu ET, Cance WG. Overexpression of the focal adhesion kinase (FAK) gene in primary and metastatic human tumors [abstract]. 46th Annual Cancer Symposium of the Society of Surgical Oncology in Conjunction with Society of Head and Neck Surgeons; 1993 March 18–21; Los Angeles: 7 Weiner TM, Liu ET, Cance WG. Overexpression of the focal adhesion kinase (FAK) gene in primary and metastatic human tumors [abstract]. 46th Annual Cancer Symposium of the Society of Surgical Oncology in Conjunction with Society of Head and Neck Surgeons; 1993 March 18–21; Los Angeles: 7
267.
go back to reference Owens LV, Xu L, Craven RJ, et al. Overexpression of the focal adhesion kinase (p125-FAK) in invasive human tumors. Cancer Res 1995; 55: 2752–5PubMed Owens LV, Xu L, Craven RJ, et al. Overexpression of the focal adhesion kinase (p125-FAK) in invasive human tumors. Cancer Res 1995; 55: 2752–5PubMed
268.
go back to reference Han NM, Fleming RYD, Curley SA, et al. Overexpression of focal adhesion kinase (P125(FAK)) in human colorectal-carcinoma liver metastases: independence from c-src or c-yes activation. Ann Surg Oncol 1997; 4: 264–8PubMedCrossRef Han NM, Fleming RYD, Curley SA, et al. Overexpression of focal adhesion kinase (P125(FAK)) in human colorectal-carcinoma liver metastases: independence from c-src or c-yes activation. Ann Surg Oncol 1997; 4: 264–8PubMedCrossRef
269.
go back to reference Judson PL, He X, Cance WG, et al. FAK, a tyrosine kinase implicated in invasion and metastasis, is overexpressed in ovarian carcinoma. Gynecol Oncol 1998; 68: 82 Judson PL, He X, Cance WG, et al. FAK, a tyrosine kinase implicated in invasion and metastasis, is overexpressed in ovarian carcinoma. Gynecol Oncol 1998; 68: 82
270.
go back to reference Jenq WM, Cooper DR, Ramirez G. Integrin expression on cell adhesion function and up-regulation of P125-FAK and paxillin in metastatic renal carcinoma cells. Mol Biol Cell 1996; 7: 424A Jenq WM, Cooper DR, Ramirez G. Integrin expression on cell adhesion function and up-regulation of P125-FAK and paxillin in metastatic renal carcinoma cells. Mol Biol Cell 1996; 7: 424A
271.
go back to reference Tremblay L, Hauck W, Aprikian AG, et al. Focal adhesion kinase (pp125-FAK) expression, activation and association with paxillin and p50-csk in human metastatic prostate carcinoma. Int J Cancer 1996; 68: 164–71PubMedCrossRef Tremblay L, Hauck W, Aprikian AG, et al. Focal adhesion kinase (pp125-FAK) expression, activation and association with paxillin and p50-csk in human metastatic prostate carcinoma. Int J Cancer 1996; 68: 164–71PubMedCrossRef
272.
go back to reference Akasaka T, Van Leeuwen RL, Yoshinaga IG, et al. Focal adhesion kinase (p125(FAK)) expression correlates with motility of human melanoma cell lines. J Invest Dermatol 1995; 105: 104–8PubMedCrossRef Akasaka T, Van Leeuwen RL, Yoshinaga IG, et al. Focal adhesion kinase (p125(FAK)) expression correlates with motility of human melanoma cell lines. J Invest Dermatol 1995; 105: 104–8PubMedCrossRef
273.
go back to reference McCormack SJ, Brazinski SE, Moore JL, et al. Activation of the focal adhesion kinase signal transduction pathway in cervical carcinoma cell lines and human genital epithelial cells immortalized with human papillomavirus type 18. Oncogene 1997; 15: 265–74PubMedCrossRef McCormack SJ, Brazinski SE, Moore JL, et al. Activation of the focal adhesion kinase signal transduction pathway in cervical carcinoma cell lines and human genital epithelial cells immortalized with human papillomavirus type 18. Oncogene 1997; 15: 265–74PubMedCrossRef
274.
go back to reference Cotter TG. BCR-ABL: an anti-apoptosis gene in chronic myelogenous leukemia. Leuk Lymph 1995; 18: 231–6CrossRef Cotter TG. BCR-ABL: an anti-apoptosis gene in chronic myelogenous leukemia. Leuk Lymph 1995; 18: 231–6CrossRef
275.
go back to reference Van Etten RA, Jackson P, Baltimore D. The mouse type IVc-abl gene product is a nuclear protein, and activation of transforming ability is associated with cytoplasmic localization. Cell 1989; 58: 669–78PubMedCrossRef Van Etten RA, Jackson P, Baltimore D. The mouse type IVc-abl gene product is a nuclear protein, and activation of transforming ability is associated with cytoplasmic localization. Cell 1989; 58: 669–78PubMedCrossRef
276.
go back to reference Kipreos ET, Wang JYJ. Cell cycle-regulated binding of c-Abl tyrosine kinase to DNA. Science 1992; 256: 382–5PubMedCrossRef Kipreos ET, Wang JYJ. Cell cycle-regulated binding of c-Abl tyrosine kinase to DNA. Science 1992; 256: 382–5PubMedCrossRef
277.
go back to reference Jackson P, Baltimore D. N-terminal mutations activates the leukemogenic potential of the myristoylated form of c-abl. EMBOJ 1989; 8: 449–56 Jackson P, Baltimore D. N-terminal mutations activates the leukemogenic potential of the myristoylated form of c-abl. EMBOJ 1989; 8: 449–56
278.
go back to reference Muller AJ, Young JC, Pendergast AM, et al. BCR first exon sequences specifically activates the BCR/ABL tyrosine kinase oncogene of Philadelphia chromosome positive human leukemias. Mol Cell Biol 1991; 11: 1785–92PubMed Muller AJ, Young JC, Pendergast AM, et al. BCR first exon sequences specifically activates the BCR/ABL tyrosine kinase oncogene of Philadelphia chromosome positive human leukemias. Mol Cell Biol 1991; 11: 1785–92PubMed
279.
go back to reference Oppi C, Shore SK, Reddy EP. Nucleotide sequence of testis-derived cDNAs: implications for testis specific transcription and abl oncogene activation. Proc Natl Acad Sci U S A 1987; 84: 8200–4PubMedCrossRef Oppi C, Shore SK, Reddy EP. Nucleotide sequence of testis-derived cDNAs: implications for testis specific transcription and abl oncogene activation. Proc Natl Acad Sci U S A 1987; 84: 8200–4PubMedCrossRef
280.
go back to reference Sawyers CL, McLaughlin J, Goga A, et al. The nuclear tyrosine kinase c-Abl negatively regulates cell growth. Cell 1994; 77: 121–31PubMedCrossRef Sawyers CL, McLaughlin J, Goga A, et al. The nuclear tyrosine kinase c-Abl negatively regulates cell growth. Cell 1994; 77: 121–31PubMedCrossRef
281.
go back to reference Yuan ZM, Huang Y, Whang Y, et al. Role for c-Abl tyrosine kinase in growth arrest response to DNA damage. Nature 1996; 382: 272–4PubMedCrossRef Yuan ZM, Huang Y, Whang Y, et al. Role for c-Abl tyrosine kinase in growth arrest response to DNA damage. Nature 1996; 382: 272–4PubMedCrossRef
282.
go back to reference Okabe M, Uehara Y, Nishima T, et al. in vivo antitumor activity of herbimycin A, a tyrosine kinase inhibitor, targeted against bcr/abl oncoprotein in mice bearing bcr/abl-transfected cells. Leuk Res 1994; 18: 867–73PubMedCrossRef Okabe M, Uehara Y, Nishima T, et al. in vivo antitumor activity of herbimycin A, a tyrosine kinase inhibitor, targeted against bcr/abl oncoprotein in mice bearing bcr/abl-transfected cells. Leuk Res 1994; 18: 867–73PubMedCrossRef
283.
go back to reference Hanks S, Quinn AM, Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 1988; 241: 42–52PubMedCrossRef Hanks S, Quinn AM, Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 1988; 241: 42–52PubMedCrossRef
284.
285.
go back to reference Ihle JN, Witthuhn BA, Quelle FW, et al. Signalling by the cytokine receptor superfamily: JAKs and STATs. Trends Biochem Sci 1994; 19: 222–7PubMedCrossRef Ihle JN, Witthuhn BA, Quelle FW, et al. Signalling by the cytokine receptor superfamily: JAKs and STATs. Trends Biochem Sci 1994; 19: 222–7PubMedCrossRef
286.
go back to reference Silvennoinen O, Schindler C, Schlessinger J, et al. Ras-independent growth factor signalling by transcription factor tyrosine phosphorylation. Science 1993; 261: 1736–9PubMedCrossRef Silvennoinen O, Schindler C, Schlessinger J, et al. Ras-independent growth factor signalling by transcription factor tyrosine phosphorylation. Science 1993; 261: 1736–9PubMedCrossRef
287.
go back to reference Stahl N, Yancopoulos GD. The alphas, betas, and kinases of cytokine receptor complexes. Cell 1993; 74: 587–90PubMedCrossRef Stahl N, Yancopoulos GD. The alphas, betas, and kinases of cytokine receptor complexes. Cell 1993; 74: 587–90PubMedCrossRef
288.
go back to reference Velazquez L, Fellous M, Stark GR, et al. A protein tyrosine kinase in the interferon alpha/beta signalling pathway. Cell 1992; 70: 313–22PubMedCrossRef Velazquez L, Fellous M, Stark GR, et al. A protein tyrosine kinase in the interferon alpha/beta signalling pathway. Cell 1992; 70: 313–22PubMedCrossRef
289.
go back to reference Watling D, Guschin D, Muller M, et al. Complementation by the protein tyrosine kinase JAK2 of a mutant cell line defective in the interferon-gamma signal transduction pathway. Nature 1993; 366: 166–70PubMedCrossRef Watling D, Guschin D, Muller M, et al. Complementation by the protein tyrosine kinase JAK2 of a mutant cell line defective in the interferon-gamma signal transduction pathway. Nature 1993; 366: 166–70PubMedCrossRef
290.
go back to reference Muller M, Briscoe J, Laxton C, et al. The protein tyrosine kinase JAK1 complements defects in interferon-alpha/beta and — gamma signal transduction. Nature 1993; 366: 129–35PubMedCrossRef Muller M, Briscoe J, Laxton C, et al. The protein tyrosine kinase JAK1 complements defects in interferon-alpha/beta and — gamma signal transduction. Nature 1993; 366: 129–35PubMedCrossRef
291.
go back to reference Cance WG, Craven RJ, Weiner TM, et al. Novel protein kinases expressed in human breast cancer. Int J Cancer 1993; 54: 571–7PubMedCrossRef Cance WG, Craven RJ, Weiner TM, et al. Novel protein kinases expressed in human breast cancer. Int J Cancer 1993; 54: 571–7PubMedCrossRef
292.
go back to reference Miyazaki T, Kawahara A, Fujii H, et al. Functional activation of Jak1 and Jak3 by selective association with IL-2 receptor subunits. Science 1994; 266: 1045–7PubMedCrossRef Miyazaki T, Kawahara A, Fujii H, et al. Functional activation of Jak1 and Jak3 by selective association with IL-2 receptor subunits. Science 1994; 266: 1045–7PubMedCrossRef
293.
go back to reference Rodig S, Meraz MA, White JM, et al. Disruption of the Jak1 gene demonstrates obligatory and nonredundant roles of the Jaks in cytokine-induced biologic responses. Cell 1998; 93: 373–83PubMedCrossRef Rodig S, Meraz MA, White JM, et al. Disruption of the Jak1 gene demonstrates obligatory and nonredundant roles of the Jaks in cytokine-induced biologic responses. Cell 1998; 93: 373–83PubMedCrossRef
294.
go back to reference Parganas E, Wang, D, Stravopodis D, et al. Jak2 is essential for signaling through a variety of cytokine receptors. Cell 1998; 93: 385–95PubMedCrossRef Parganas E, Wang, D, Stravopodis D, et al. Jak2 is essential for signaling through a variety of cytokine receptors. Cell 1998; 93: 385–95PubMedCrossRef
295.
go back to reference Neubauer H, Cumao A, Müller M, et al. Jak2 deficiency defines an essential developmental checkpoint in definitive hematopoiesis. Cell 1998; 93: 397–409PubMedCrossRef Neubauer H, Cumao A, Müller M, et al. Jak2 deficiency defines an essential developmental checkpoint in definitive hematopoiesis. Cell 1998; 93: 397–409PubMedCrossRef
296.
go back to reference Shuai K, Stark GR, Kerr TM, et al. A single phosphotyrosine residue of Stat91 required for gene activation by interferon-gamma. Science 1993; 261: 1744–6PubMedCrossRef Shuai K, Stark GR, Kerr TM, et al. A single phosphotyrosine residue of Stat91 required for gene activation by interferon-gamma. Science 1993; 261: 1744–6PubMedCrossRef
297.
go back to reference Leung S, Li X, Stark GR. STATs find that hanging together can be stimulating. Science 1996; 273: 750PubMedCrossRef Leung S, Li X, Stark GR. STATs find that hanging together can be stimulating. Science 1996; 273: 750PubMedCrossRef
298.
go back to reference Lutticken C, Wegenka UM, Yuan J, et al. Association of transcription factor APRF and protein kinase Jak1 with the interleukin-6 signal transducer gp 130. Science 1994; 263: 89–92PubMedCrossRef Lutticken C, Wegenka UM, Yuan J, et al. Association of transcription factor APRF and protein kinase Jak1 with the interleukin-6 signal transducer gp 130. Science 1994; 263: 89–92PubMedCrossRef
299.
go back to reference Pearse RN, Feinman R, Shuai K, et al. Interferon gamma-induced transcription of the high-affinity Fc receptor for IgG requires assembly of a complex that includes the 91-kDa subunit of transcription factor ISGF 3. Proc Natl Acad Sci U S A 1993; 90: 4314–8PubMedCrossRef Pearse RN, Feinman R, Shuai K, et al. Interferon gamma-induced transcription of the high-affinity Fc receptor for IgG requires assembly of a complex that includes the 91-kDa subunit of transcription factor ISGF 3. Proc Natl Acad Sci U S A 1993; 90: 4314–8PubMedCrossRef
300.
go back to reference Silvennoinen W, Witthuhn BA, Quelle FW, et al. Structure of the murine Jak2 protein-tyrosine kinase and its role in interleukin 3 signal transduction. Proc Natl Acad Sci U S A 1993; 90: 8429–33PubMedCrossRef Silvennoinen W, Witthuhn BA, Quelle FW, et al. Structure of the murine Jak2 protein-tyrosine kinase and its role in interleukin 3 signal transduction. Proc Natl Acad Sci U S A 1993; 90: 8429–33PubMedCrossRef
301.
go back to reference Sadowski HB, Shuai K, Darnell JE, et al. A common nuclear signal transduction pathway activated by growth factor and cytokine receptors. Science 1993; 261: 1739–44PubMedCrossRef Sadowski HB, Shuai K, Darnell JE, et al. A common nuclear signal transduction pathway activated by growth factor and cytokine receptors. Science 1993; 261: 1739–44PubMedCrossRef
302.
go back to reference Ruff-Jamison S, Chen K, Cohen S. Induction by EGF and interferon-gamma of tyrosine phosphorylated DNA binding proteins in mouse liver nuclei. Science 1993; 261: 1733–6PubMedCrossRef Ruff-Jamison S, Chen K, Cohen S. Induction by EGF and interferon-gamma of tyrosine phosphorylated DNA binding proteins in mouse liver nuclei. Science 1993; 261: 1733–6PubMedCrossRef
303.
go back to reference Zachary I, Rozengurt E. Focal adhesion kinase (p125FAK): a point of convergence in the action of neuropeptides, integrins, and oncogenes. Cell 1992; 71: 891–4PubMedCrossRef Zachary I, Rozengurt E. Focal adhesion kinase (p125FAK): a point of convergence in the action of neuropeptides, integrins, and oncogenes. Cell 1992; 71: 891–4PubMedCrossRef
304.
go back to reference Schaller MD, Hildebrand JD, Shannon JD, et al. Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src. Mol Cell Biol 1994; 14: 1680–8PubMed Schaller MD, Hildebrand JD, Shannon JD, et al. Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src. Mol Cell Biol 1994; 14: 1680–8PubMed
305.
go back to reference Hanks SK, Calalb MB, Harper MC, et al. Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. Proc Natl Acad Sci U S A 1992; 89: 8487–91PubMedCrossRef Hanks SK, Calalb MB, Harper MC, et al. Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. Proc Natl Acad Sci U S A 1992; 89: 8487–91PubMedCrossRef
306.
go back to reference Tani T, Von Koskull H, Virtanan I. Focal adhesion kinase pp125-FAK is associated with both intercellular junctions and matrix adhesion sites in vivo. Histochem Cell Biol 1996; 105: 17–25PubMedCrossRef Tani T, Von Koskull H, Virtanan I. Focal adhesion kinase pp125-FAK is associated with both intercellular junctions and matrix adhesion sites in vivo. Histochem Cell Biol 1996; 105: 17–25PubMedCrossRef
307.
go back to reference Aprikian AG, Tremblay L, Han K, et al. Bombesin stimulates the motility of human prostate-carcinoma cells through tyrosine phosphorylation of focal adhesion kinase and of integrin-associated proteins. Int J Cancer 1997; 72: 498–504PubMedCrossRef Aprikian AG, Tremblay L, Han K, et al. Bombesin stimulates the motility of human prostate-carcinoma cells through tyrosine phosphorylation of focal adhesion kinase and of integrin-associated proteins. Int J Cancer 1997; 72: 498–504PubMedCrossRef
308.
go back to reference Duncan MD, Harmon JW, Duncan KLK. Actin disruption inhibits bombesin stimulation of focal adhesion kinase (pp125-FAK) in prostate carcinoma. J Surg Res 1996; 63: 359–63PubMedCrossRef Duncan MD, Harmon JW, Duncan KLK. Actin disruption inhibits bombesin stimulation of focal adhesion kinase (pp125-FAK) in prostate carcinoma. J Surg Res 1996; 63: 359–63PubMedCrossRef
309.
go back to reference Matsumoto K, Matsumoto J, Nakamura T, et al. Hepatocyte growth factor-scatter factor induces tyrosine phosphorylation of focal adhesion kinase (p125-FAK) and promotes migration and invasion by oral squamous cell carcinoma cells. J Biol Chem 1994; 269: 31807–13PubMed Matsumoto K, Matsumoto J, Nakamura T, et al. Hepatocyte growth factor-scatter factor induces tyrosine phosphorylation of focal adhesion kinase (p125-FAK) and promotes migration and invasion by oral squamous cell carcinoma cells. J Biol Chem 1994; 269: 31807–13PubMed
310.
go back to reference Jiang WG, Hiscox S, Nakamura T, et al. Hepatocyte growth factor induces tyrosine phosphorylation of focal adhesion kinase (FAK) and paxillin and enhances cell-matrix interactions. Oncol Rep 1996; 3: 819–23PubMed Jiang WG, Hiscox S, Nakamura T, et al. Hepatocyte growth factor induces tyrosine phosphorylation of focal adhesion kinase (FAK) and paxillin and enhances cell-matrix interactions. Oncol Rep 1996; 3: 819–23PubMed
311.
go back to reference Canbay E, Norman M, Kilic E, et al. Prolactin stimulates the JAK2 and focal adhesion kinase pathways in human breast carcinoma T47-D cells. Biochem J 1997; 324: 231–6PubMed Canbay E, Norman M, Kilic E, et al. Prolactin stimulates the JAK2 and focal adhesion kinase pathways in human breast carcinoma T47-D cells. Biochem J 1997; 324: 231–6PubMed
312.
go back to reference Yu G, Smithgall TE, Glazer RI. K562 leukemia cells transfected with the human c-fes gene acquire the ability to undergo myeloid differentiation. J Biol Chem 1989; 264: 10276–81PubMed Yu G, Smithgall TE, Glazer RI. K562 leukemia cells transfected with the human c-fes gene acquire the ability to undergo myeloid differentiation. J Biol Chem 1989; 264: 10276–81PubMed
313.
go back to reference Van de Ven WJM. The protein kinases: Fes/Fps. In: Hardie G, Hanks S, editors. The protein kinase facts book. New York: Academic Press, 1995: 92–4 Van de Ven WJM. The protein kinases: Fes/Fps. In: Hardie G, Hanks S, editors. The protein kinase facts book. New York: Academic Press, 1995: 92–4
314.
go back to reference Hao QL, Heisterkamp N, Groffen J. Isolation and sequence analysis of a novel human tyrosine kinase. Mol Cell Biol 1989; 9: 1587–93PubMed Hao QL, Heisterkamp N, Groffen J. Isolation and sequence analysis of a novel human tyrosine kinase. Mol Cell Biol 1989; 9: 1587–93PubMed
315.
go back to reference Feldman RA, Gabrilove JL, Tam JP, et al. Specific expression of the human cellular fps/fes-encoded protein NCP92 in normal and leukemic myeloid cells. Proc Natl Acad Sci U S A 1985; 82: 2379–83PubMedCrossRef Feldman RA, Gabrilove JL, Tam JP, et al. Specific expression of the human cellular fps/fes-encoded protein NCP92 in normal and leukemic myeloid cells. Proc Natl Acad Sci U S A 1985; 82: 2379–83PubMedCrossRef
316.
go back to reference MacDonald I, Levy J, Pawson T. Expression of the mammalian c-fes protein in hematopoietic cells and identification of a distinct fes-related protein. Mol Cell Biol 1985; 5: 2543–51PubMed MacDonald I, Levy J, Pawson T. Expression of the mammalian c-fes protein in hematopoietic cells and identification of a distinct fes-related protein. Mol Cell Biol 1985; 5: 2543–51PubMed
317.
go back to reference Slamon D, de Kemion JR, Verma IM, et al. Expression of cellular oncogenes in human malignancies. Science 1984; 224: 256–62PubMedCrossRef Slamon D, de Kemion JR, Verma IM, et al. Expression of cellular oncogenes in human malignancies. Science 1984; 224: 256–62PubMedCrossRef
318.
go back to reference Greer P, Haigh J, Mbamalu G, et al. The fps/fes protein-tyrosine kinase promotes angiogenesis in transgenic mice. Mol Cell Biol 1994; 14: 6755–63PubMed Greer P, Haigh J, Mbamalu G, et al. The fps/fes protein-tyrosine kinase promotes angiogenesis in transgenic mice. Mol Cell Biol 1994; 14: 6755–63PubMed
319.
go back to reference Sithanandam G, Kolch W, Duh FM, et al. Complete coding sequence of a human B-raf cDNA and detection of B-raf protein kinase with isozyme specific antibodies. Oncogene 1990; 5: 1775–80PubMed Sithanandam G, Kolch W, Duh FM, et al. Complete coding sequence of a human B-raf cDNA and detection of B-raf protein kinase with isozyme specific antibodies. Oncogene 1990; 5: 1775–80PubMed
320.
go back to reference Marais R, Light Y, Paterson HF, et al. Differential regulation of Raf-1, A-Raf, and B-Raf by oncogenic Ras and tyrosine kinases. J Biol Chem 1997; 272: 4378–83PubMedCrossRef Marais R, Light Y, Paterson HF, et al. Differential regulation of Raf-1, A-Raf, and B-Raf by oncogenic Ras and tyrosine kinases. J Biol Chem 1997; 272: 4378–83PubMedCrossRef
321.
go back to reference Bernards A. Neurofibromatosis type I and Ras-mediated signalling: filling in the GAPs. Biochim Biophys Acta 1995; 1242: 43–59PubMed Bernards A. Neurofibromatosis type I and Ras-mediated signalling: filling in the GAPs. Biochim Biophys Acta 1995; 1242: 43–59PubMed
322.
go back to reference Adari H, Lowy DR, Willumsen BF, et al. Guanosine triphosphatase activating protein (GAP) interacts with the p21 ras effector binding domain. Science 1988; 240: 518–21PubMedCrossRef Adari H, Lowy DR, Willumsen BF, et al. Guanosine triphosphatase activating protein (GAP) interacts with the p21 ras effector binding domain. Science 1988; 240: 518–21PubMedCrossRef
323.
go back to reference Rodriguez-Viciana P, Warne PH, Dhand R, et al. Phosphatidylinositol-3-OH kinase as a direct target of ras. Nature 1994; 370: 527–32PubMedCrossRef Rodriguez-Viciana P, Warne PH, Dhand R, et al. Phosphatidylinositol-3-OH kinase as a direct target of ras. Nature 1994; 370: 527–32PubMedCrossRef
324.
go back to reference Willumsen BM, Vass WC, Velu TJ, et al. Mutational analysis of a ras catalytic domain. Mol Cell Biol 1991; 11: 6026–33PubMed Willumsen BM, Vass WC, Velu TJ, et al. Mutational analysis of a ras catalytic domain. Mol Cell Biol 1991; 11: 6026–33PubMed
325.
go back to reference Amar S, Glozman A, Chung D, et al. Selective inhibition of oncogenic ras-p21 in vivo by agents that block its interaction with jun-N-kinase (JNK) and jun proteins: implications for the design of selective chemotherapeutic agents. Cancer Chemother Pharmacol 1997; 41: 79–85PubMedCrossRef Amar S, Glozman A, Chung D, et al. Selective inhibition of oncogenic ras-p21 in vivo by agents that block its interaction with jun-N-kinase (JNK) and jun proteins: implications for the design of selective chemotherapeutic agents. Cancer Chemother Pharmacol 1997; 41: 79–85PubMedCrossRef
326.
go back to reference Hiwasa T. Ras inhibitors [review]. Oncol Rep 1994; 3: 7–14 Hiwasa T. Ras inhibitors [review]. Oncol Rep 1994; 3: 7–14
327.
go back to reference Marais R, Light Y, Mason C, et al. Requirement of Ras-GTP-Raf complexes for activation of Raf-1 by protein kinase C [published erratum appears in Science 1998; 280: 987]. Science 1998; 280: 109–12PubMedCrossRef Marais R, Light Y, Mason C, et al. Requirement of Ras-GTP-Raf complexes for activation of Raf-1 by protein kinase C [published erratum appears in Science 1998; 280: 987]. Science 1998; 280: 109–12PubMedCrossRef
328.
go back to reference Blagosklonny MV, Giannakakou P, El-Deiry WS, et al. Raf-1/bcl-2 phosphorylation: a tep from microtubule damage to cell death. Cancer Res 1997; 57: 103–5 Blagosklonny MV, Giannakakou P, El-Deiry WS, et al. Raf-1/bcl-2 phosphorylation: a tep from microtubule damage to cell death. Cancer Res 1997; 57: 103–5
329.
go back to reference Wang HG, Rapp UR, Reed JC. Bcl-2 targets the protein kinase Raf-1 to mitochondria. Cell 1996; 87: 629–38PubMedCrossRef Wang HG, Rapp UR, Reed JC. Bcl-2 targets the protein kinase Raf-1 to mitochondria. Cell 1996; 87: 629–38PubMedCrossRef
330.
go back to reference Kroemer G. The proto-oncogene Bcl-2 and its role in regulating apoptosis [published erratum appears in Nat Med 1997; 3: 934]. Nat Med 1997; 3: 614–20PubMedCrossRef Kroemer G. The proto-oncogene Bcl-2 and its role in regulating apoptosis [published erratum appears in Nat Med 1997; 3: 934]. Nat Med 1997; 3: 614–20PubMedCrossRef
331.
332.
go back to reference Ouyang H, Furukawa T, Abe T, et al. The Bax gene, the promoter of apoptosis, is mutated in genetically unstable cancers of the colorectum, stomach and endometrium. Clin Cancer Res 1998; 4: 1071–4PubMed Ouyang H, Furukawa T, Abe T, et al. The Bax gene, the promoter of apoptosis, is mutated in genetically unstable cancers of the colorectum, stomach and endometrium. Clin Cancer Res 1998; 4: 1071–4PubMed
333.
go back to reference Brimmell M, Mendiola R, Mangion J, et al. Bax frameshift mutations in cell lines derived from human haematopoietic malignancies are associated with resistance to apoptosis and microsatellite instability. Oncogene 1998; 16: 1803–12PubMedCrossRef Brimmell M, Mendiola R, Mangion J, et al. Bax frameshift mutations in cell lines derived from human haematopoietic malignancies are associated with resistance to apoptosis and microsatellite instability. Oncogene 1998; 16: 1803–12PubMedCrossRef
334.
go back to reference Bos JL. ras oncogenes in human cancer: a review. Cancer Res 1989; 49: 4682–9PubMed Bos JL. ras oncogenes in human cancer: a review. Cancer Res 1989; 49: 4682–9PubMed
335.
go back to reference Kiaris H, Spandidos DA. Mutations or ras genes in human tumours [review]. Int J Oncol 1995; 7: 413–21PubMed Kiaris H, Spandidos DA. Mutations or ras genes in human tumours [review]. Int J Oncol 1995; 7: 413–21PubMed
336.
go back to reference Ravi R, Bedi A, Fuchs EJ, et al. CD95 (Fas)-induced caspase-mediated proteolysis of NF-κB. Cancer Res 1998; 58: 882–6PubMed Ravi R, Bedi A, Fuchs EJ, et al. CD95 (Fas)-induced caspase-mediated proteolysis of NF-κB. Cancer Res 1998; 58: 882–6PubMed
337.
go back to reference Sithanandam G, Dean M, Brennscheidt U, et al. Loss of heterozygosity at the c-raf locus in small cell lung carcinoma. Oncogene 1989; 4: 451–5PubMed Sithanandam G, Dean M, Brennscheidt U, et al. Loss of heterozygosity at the c-raf locus in small cell lung carcinoma. Oncogene 1989; 4: 451–5PubMed
338.
go back to reference Berger DH, Jardines, LA, Chang H, et al. Activation of Rf-1 in human pancreatic adenocarcinoma. J Surg Res 1997; 69: 199–204PubMedCrossRef Berger DH, Jardines, LA, Chang H, et al. Activation of Rf-1 in human pancreatic adenocarcinoma. J Surg Res 1997; 69: 199–204PubMedCrossRef
339.
go back to reference Callans LS, Naama H, Khandelwal M, et al. Raf-1 protein expression in human breast cancer cells. Anns Surg Oncol 1995; 2: 38–42CrossRef Callans LS, Naama H, Khandelwal M, et al. Raf-1 protein expression in human breast cancer cells. Anns Surg Oncol 1995; 2: 38–42CrossRef
340.
go back to reference Patel BK, Ray S, Whiteside TL, et al. Correlation of constitutive activation of raf-1 with morphological transformation and abrogation of tyrosine phosphorylation of distinct sets of proteins in human squamous carcinoma cells. Mol Carcinogen 1993; 18: 1–6CrossRef Patel BK, Ray S, Whiteside TL, et al. Correlation of constitutive activation of raf-1 with morphological transformation and abrogation of tyrosine phosphorylation of distinct sets of proteins in human squamous carcinoma cells. Mol Carcinogen 1993; 18: 1–6CrossRef
341.
go back to reference Riva C, Lavieille JP, Reyt E, et al. Differential c-myc, c-jun, c-raf and p53 expression in squamous cell carcinoma of the head and neck: implication in drug and radioresistance. Eur J Cancer Oral Oncol 1995; 31B (Pt B): 384–91CrossRef Riva C, Lavieille JP, Reyt E, et al. Differential c-myc, c-jun, c-raf and p53 expression in squamous cell carcinoma of the head and neck: implication in drug and radioresistance. Eur J Cancer Oral Oncol 1995; 31B (Pt B): 384–91CrossRef
342.
go back to reference Eggstein S, Manthey G, Hirsch T, et al. Raf-1 kinase, epidermal growth factor receptors, and mutant Ras proteins in colonic carcinomas. Dig Dis Sci 1996; 41: 1069–75PubMedCrossRef Eggstein S, Manthey G, Hirsch T, et al. Raf-1 kinase, epidermal growth factor receptors, and mutant Ras proteins in colonic carcinomas. Dig Dis Sci 1996; 41: 1069–75PubMedCrossRef
343.
go back to reference Okuda K, Matulonis U, Salgia R, et al. Factor independence of human myeloid leukemia cell lines is associated with increased phosphorylation of the proto-oncogene Raf-1. Exp Hematol 1994; 22: 1111–7PubMed Okuda K, Matulonis U, Salgia R, et al. Factor independence of human myeloid leukemia cell lines is associated with increased phosphorylation of the proto-oncogene Raf-1. Exp Hematol 1994; 22: 1111–7PubMed
344.
go back to reference Schmidt CA, Oettle H, Ludwig WD, et al. Overexpression of the Raf-1 proto-oncogene in human myeloid leukemia. Leuk Res 1994; 18:409–13PubMedCrossRef Schmidt CA, Oettle H, Ludwig WD, et al. Overexpression of the Raf-1 proto-oncogene in human myeloid leukemia. Leuk Res 1994; 18:409–13PubMedCrossRef
345.
go back to reference Callans LS, Naama H, Khandelwal M, et al. Raf-1 phosphorylation in human breast cancer cells (Meeting abstract). Soc. Surg. Oncol., 46th Annual Cancer Symposium in Conjunction with Society of Head and Neck Surgeons; 1993 March 18–21, Los Angeles (CA), 20 Callans LS, Naama H, Khandelwal M, et al. Raf-1 phosphorylation in human breast cancer cells (Meeting abstract). Soc. Surg. Oncol., 46th Annual Cancer Symposium in Conjunction with Society of Head and Neck Surgeons; 1993 March 18–21, Los Angeles (CA), 20
346.
go back to reference Patel BK, Kasid U. Nucleotide sequence analysis of c-raf-1 cDNA and promoter from a radiation-resistant human squamous carcinoma cell line: deletion within exon 17. Mol Carcinogen 1993; 8: 7–12CrossRef Patel BK, Kasid U. Nucleotide sequence analysis of c-raf-1 cDNA and promoter from a radiation-resistant human squamous carcinoma cell line: deletion within exon 17. Mol Carcinogen 1993; 8: 7–12CrossRef
347.
go back to reference Storm SM, Rapp UR. Oncogene activation: c-raf-1 gene mutations in experimental and naturally occurring tumors. Toxicology Lett 1993; 67: 201–10CrossRef Storm SM, Rapp UR. Oncogene activation: c-raf-1 gene mutations in experimental and naturally occurring tumors. Toxicology Lett 1993; 67: 201–10CrossRef
348.
go back to reference Teyssier JR, Henry I, Dozier C, et al. Recurrent deletion of the short arm of chromosome 3 in human renal cell carcinoma: shift of the c-raf 1 locus. J Natl Cancer Inst 1986; 77: 1187–95PubMed Teyssier JR, Henry I, Dozier C, et al. Recurrent deletion of the short arm of chromosome 3 in human renal cell carcinoma: shift of the c-raf 1 locus. J Natl Cancer Inst 1986; 77: 1187–95PubMed
349.
go back to reference Ikeda S, Sumii H, Akiyama K, et al. Amplification of both c-myc and c-raf-1 oncogenes in a human osteosarcoma. Jpn J Cancer Res 1989; 80: 6–9PubMedCrossRef Ikeda S, Sumii H, Akiyama K, et al. Amplification of both c-myc and c-raf-1 oncogenes in a human osteosarcoma. Jpn J Cancer Res 1989; 80: 6–9PubMedCrossRef
350.
go back to reference Xerri L, Charpin C, Hassoun J, et al. Mos oncogene expression in human ovarian tumors. Anticancer Res 1991; 11: 1629–34PubMed Xerri L, Charpin C, Hassoun J, et al. Mos oncogene expression in human ovarian tumors. Anticancer Res 1991; 11: 1629–34PubMed
351.
go back to reference Lidereau R, Mathieu-Mahul D, Theillet C, et al. Presence of an allelic EcoRI restriction fragment of the c-mos locus in leukocyte and tumor cell DNAs of breast cancer patients. Proc Natl Acad Sci U S A 1985; 82: 7068–70PubMedCrossRef Lidereau R, Mathieu-Mahul D, Theillet C, et al. Presence of an allelic EcoRI restriction fragment of the c-mos locus in leukocyte and tumor cell DNAs of breast cancer patients. Proc Natl Acad Sci U S A 1985; 82: 7068–70PubMedCrossRef
352.
go back to reference Parkar MH, Seid JM, Stringer BM, et al. Abnormal expression of the MOS proto-oncogene in human thyroid medullary carcinoma. Cancer Lett 1988; 15: 185–9CrossRef Parkar MH, Seid JM, Stringer BM, et al. Abnormal expression of the MOS proto-oncogene in human thyroid medullary carcinoma. Cancer Lett 1988; 15: 185–9CrossRef
353.
go back to reference Lidereau R, Cole ST, Larsen CJ, et al. A single point mutation responsible for c-mos polymorphism in cancer patients. Oncogene 1987; 1: 235–7PubMed Lidereau R, Cole ST, Larsen CJ, et al. A single point mutation responsible for c-mos polymorphism in cancer patients. Oncogene 1987; 1: 235–7PubMed
354.
go back to reference Csaikl F, Mullauer L, Schwabe M, et al. Mutations of c-myc and c-mos genes lead to aberrant transcription of c-myc [abstract]. Blut 1987; 55: 244 Csaikl F, Mullauer L, Schwabe M, et al. Mutations of c-myc and c-mos genes lead to aberrant transcription of c-myc [abstract]. Blut 1987; 55: 244
355.
go back to reference Staal SP Molecular cloning of the AKT oncogene and its human homologous AKT1 and AKT2: amplification of AKT1 in a primary human gastric adenocarcinoma. Proc Natl Acad Sci U S A 1987; 84: 5034–7PubMedCrossRef Staal SP Molecular cloning of the AKT oncogene and its human homologous AKT1 and AKT2: amplification of AKT1 in a primary human gastric adenocarcinoma. Proc Natl Acad Sci U S A 1987; 84: 5034–7PubMedCrossRef
356.
go back to reference Ahmad S, Singh N, Bellacosa A, et al. Endogenous regulation of the protooncogene protein serine-threonine kinase, c-AKT by estradiol and insulin growth factor-1 in MCF-7 breast carcinoma cells [abstract]. Proc Am Assoc Cancer Res 1998; 38: 232 Ahmad S, Singh N, Bellacosa A, et al. Endogenous regulation of the protooncogene protein serine-threonine kinase, c-AKT by estradiol and insulin growth factor-1 in MCF-7 breast carcinoma cells [abstract]. Proc Am Assoc Cancer Res 1998; 38: 232
357.
go back to reference Schmidt CM, McKillop IH, Cahill PA, et al. Functionally significant Gi-protein linked MAPK pathway in primary human hepatocellular carcinoma [abstract]. Hepatol 1997; 26: 263ACrossRef Schmidt CM, McKillop IH, Cahill PA, et al. Functionally significant Gi-protein linked MAPK pathway in primary human hepatocellular carcinoma [abstract]. Hepatol 1997; 26: 263ACrossRef
358.
go back to reference Takahashi T, Murohashi I, Kishimoto K, et al. Hyperexpression of mitogen-activated protein kinase (p42-p44 MAPK) in malignant lymphoid neoplasms [abstract]. Blood 1997; 90: 165B Takahashi T, Murohashi I, Kishimoto K, et al. Hyperexpression of mitogen-activated protein kinase (p42-p44 MAPK) in malignant lymphoid neoplasms [abstract]. Blood 1997; 90: 165B
359.
go back to reference Attar BM, Atten MJ, Holian O. MAPK activity is down-regulated in human colon adenocarcinoma: correlation with PCK activity. Anticancer Res 1996; 16: 395–9PubMed Attar BM, Atten MJ, Holian O. MAPK activity is down-regulated in human colon adenocarcinoma: correlation with PCK activity. Anticancer Res 1996; 16: 395–9PubMed
360.
go back to reference Frexes-Steed M, Woodard B A, Kern S, et al. Growth regulation by the ras-MAPK pathway in human pancreatic ductal carcinoma [abstract]. Gastroenterol 1997; 112: A564 Frexes-Steed M, Woodard B A, Kern S, et al. Growth regulation by the ras-MAPK pathway in human pancreatic ductal carcinoma [abstract]. Gastroenterol 1997; 112: A564
361.
go back to reference Yee D, Gooch JL, Jackson JG. IGF-I, insulin, and IL4 activated IRS 1 in human breast cancer cells: Differential IRS 1 tyrosine phosphorylation by IGF-I is associated with increased MAPK and PI3K activation [abstract]. Proc Am Assoc Cancer Res Ann Meeting 1997; 38: 435 Yee D, Gooch JL, Jackson JG. IGF-I, insulin, and IL4 activated IRS 1 in human breast cancer cells: Differential IRS 1 tyrosine phosphorylation by IGF-I is associated with increased MAPK and PI3K activation [abstract]. Proc Am Assoc Cancer Res Ann Meeting 1997; 38: 435
362.
go back to reference Sun SC, Elwood J, Beraud C, et al. Human T-cell leukemia-virus type-I tax activation of NF-kappa-B/Rel involves phosphorylation and degradation of I-kappa-B-alpha and rela (p65)-mediated induction of the c-rel gene. Mol Cell Biol 1994; 14: 7377–84PubMed Sun SC, Elwood J, Beraud C, et al. Human T-cell leukemia-virus type-I tax activation of NF-kappa-B/Rel involves phosphorylation and degradation of I-kappa-B-alpha and rela (p65)-mediated induction of the c-rel gene. Mol Cell Biol 1994; 14: 7377–84PubMed
363.
go back to reference Bours V, Dejardin E, Goujon-Letawe F, et al. The NF-kappa B transcription factor and cancer: high expression of NF-kappa B- and I kappa B-related proteins in tumor cell lines. Biochem Pharmacol 1994; 47: 145–9PubMedCrossRef Bours V, Dejardin E, Goujon-Letawe F, et al. The NF-kappa B transcription factor and cancer: high expression of NF-kappa B- and I kappa B-related proteins in tumor cell lines. Biochem Pharmacol 1994; 47: 145–9PubMedCrossRef
364.
go back to reference Gilmore TD. Role of rel family genes in normal and malignant lymphoid cell growth. Cancer Surv 1992; 15: 69–87PubMed Gilmore TD. Role of rel family genes in normal and malignant lymphoid cell growth. Cancer Surv 1992; 15: 69–87PubMed
365.
go back to reference Feuillard J, Korner M, Israel A, et al. Differential nuclear localization of p50, p52, and RelB proteins in human accessory cells of the immune response in situ. Eur J Immunol 1996; 26: 2547–51PubMedCrossRef Feuillard J, Korner M, Israel A, et al. Differential nuclear localization of p50, p52, and RelB proteins in human accessory cells of the immune response in situ. Eur J Immunol 1996; 26: 2547–51PubMedCrossRef
366.
go back to reference Sovak MA, Bellas RE, Kim DW, et al. Aberrant nuclear factor-kappa-B-Rel expression and the pathogenesis of breast cancer. J Clin Invest 1997; 100: 2952–60PubMedCrossRef Sovak MA, Bellas RE, Kim DW, et al. Aberrant nuclear factor-kappa-B-Rel expression and the pathogenesis of breast cancer. J Clin Invest 1997; 100: 2952–60PubMedCrossRef
367.
go back to reference Dejardin E, Bonizzi G, Bellahcene A, et al. Highly-expressed p100/p52 (NFKB2) sequesters other NF-kappa B -related proteins in the cytoplasm of human breast cancer cells. Oncogene 1995; 11: 1835–41PubMed Dejardin E, Bonizzi G, Bellahcene A, et al. Highly-expressed p100/p52 (NFKB2) sequesters other NF-kappa B -related proteins in the cytoplasm of human breast cancer cells. Oncogene 1995; 11: 1835–41PubMed
368.
go back to reference Maxwell SA, Johnson M, Mukhopadhyay T. Expression and regulation of nuclear factor-kappa B (NFκ-B)/REL in non-small cell lung carcinoma and transformed cell lines [abstract]. Int J Oncol 1995; 7: 984 Maxwell SA, Johnson M, Mukhopadhyay T. Expression and regulation of nuclear factor-kappa B (NFκ-B)/REL in non-small cell lung carcinoma and transformed cell lines [abstract]. Int J Oncol 1995; 7: 984
369.
go back to reference Visconti R, Cerutti J, Battista S, et al. Expression of the neoplastic phenotype by human thyroid carcinoma cell lines requires NF-kappa-B p65 protein expression. Oncogene 1997; 15: 1987–94PubMedCrossRef Visconti R, Cerutti J, Battista S, et al. Expression of the neoplastic phenotype by human thyroid carcinoma cell lines requires NF-kappa-B p65 protein expression. Oncogene 1997; 15: 1987–94PubMedCrossRef
370.
go back to reference Mukhopadhyay T, Roth JA, Maxwell SA. Altered expression of the p50 subunit of the NF-kappa B transcription factor complex in non-small cell lung carcinoma. Oncogene 1995; 11: 999–1003PubMed Mukhopadhyay T, Roth JA, Maxwell SA. Altered expression of the p50 subunit of the NF-kappa B transcription factor complex in non-small cell lung carcinoma. Oncogene 1995; 11: 999–1003PubMed
371.
go back to reference Maxwell SA, Mukhopadhyay T. A novel NF-kappa B p65 spliced transcript lacking exons 6 and 7 in a non-small cell lung carcinoma cell line. Gene 1995; 166: 399–400CrossRef Maxwell SA, Mukhopadhyay T. A novel NF-kappa B p65 spliced transcript lacking exons 6 and 7 in a non-small cell lung carcinoma cell line. Gene 1995; 166: 399–400CrossRef
372.
go back to reference Bargou RC, Emmerich F, Krappmann D, et al. Constitutive nuclear factor-kappa-B-RelA activation is required for proliferation and survival of Hodgkin’s disease tumor cells. J Clin Invest 1997; 100: 2961–9PubMedCrossRef Bargou RC, Emmerich F, Krappmann D, et al. Constitutive nuclear factor-kappa-B-RelA activation is required for proliferation and survival of Hodgkin’s disease tumor cells. J Clin Invest 1997; 100: 2961–9PubMedCrossRef
373.
go back to reference Nakshatri H, Bhat-Nakshatri P, Martin DA, et al. Constitutive activation of NF-kappa-B during progression of breast cancer to hormone-independent growth. Mol Cell Biol 1997; 17: 3629–39PubMed Nakshatri H, Bhat-Nakshatri P, Martin DA, et al. Constitutive activation of NF-kappa-B during progression of breast cancer to hormone-independent growth. Mol Cell Biol 1997; 17: 3629–39PubMed
374.
go back to reference Trecca D, Guerrini L, Frachhiolla NS, et al. Identification of a tumor-associated mutant of the NF-kappa B RelA gene with reduced DNA-binding and transactivating activities. Oncogene 1997; 14: 791–9PubMedCrossRef Trecca D, Guerrini L, Frachhiolla NS, et al. Identification of a tumor-associated mutant of the NF-kappa B RelA gene with reduced DNA-binding and transactivating activities. Oncogene 1997; 14: 791–9PubMedCrossRef
375.
go back to reference Yew N, Strobel M, Vande Woude GF. Mos and the cell cycle: the molecular basis of the transformed phenotype. Curr Opin Genet Devel 1993; 3: 19–25CrossRef Yew N, Strobel M, Vande Woude GF. Mos and the cell cycle: the molecular basis of the transformed phenotype. Curr Opin Genet Devel 1993; 3: 19–25CrossRef
376.
go back to reference Sagata N, Watanabe N, Vande Woude GF, Ikawa Y. The c-mos proto-oncogene product is a cytostatic factor responsible for meiotic arrest in vertebrate eggs. Nature 1989; 342: 512–8PubMedCrossRef Sagata N, Watanabe N, Vande Woude GF, Ikawa Y. The c-mos proto-oncogene product is a cytostatic factor responsible for meiotic arrest in vertebrate eggs. Nature 1989; 342: 512–8PubMedCrossRef
377.
go back to reference Vande Woude GF. Mos gen products (vertrebrates). In: Hardie G, Hanks S, editors. The protein kinase facts book. New York: Academic Press, 1995: 358–60 Vande Woude GF. Mos gen products (vertrebrates). In: Hardie G, Hanks S, editors. The protein kinase facts book. New York: Academic Press, 1995: 358–60
378.
go back to reference Nebreda AR, Hill C, Gomez N, et al. The protein kinase mos activates MAP kinase kinase in vitro and stimulates the MAP kinase pathway in mammalian somatic cells in vivo. FEBS Lett 1993; 333: 183–7PubMedCrossRef Nebreda AR, Hill C, Gomez N, et al. The protein kinase mos activates MAP kinase kinase in vitro and stimulates the MAP kinase pathway in mammalian somatic cells in vivo. FEBS Lett 1993; 333: 183–7PubMedCrossRef
379.
go back to reference Pham CD, Arlinghaus RB, Zheng CF, et al. Characterization of mek1 phosphorylation by the v-mos protein. Oncogene 1995; 10: 1683–8PubMed Pham CD, Arlinghaus RB, Zheng CF, et al. Characterization of mek1 phosphorylation by the v-mos protein. Oncogene 1995; 10: 1683–8PubMed
380.
go back to reference Marshall CJ. MAP kinase kinase kinase, MAP kinase kinase and MAP kinase. Curr Opin Genet Dev 1994; 4: 82–9PubMedCrossRef Marshall CJ. MAP kinase kinase kinase, MAP kinase kinase and MAP kinase. Curr Opin Genet Dev 1994; 4: 82–9PubMedCrossRef
381.
go back to reference Davis RJ. MAPKs: new JNK expands the group. Trends Biochem 1994; 19: 470–3CrossRef Davis RJ. MAPKs: new JNK expands the group. Trends Biochem 1994; 19: 470–3CrossRef
382.
go back to reference Waskiewicz AJ, Cooper JA. Mitogen and stress response pathways: MAP kinase cascades and phosphatase regulation in mammals and yeast. Curr Opin Cell Biol 1995; 7: 798–805PubMedCrossRef Waskiewicz AJ, Cooper JA. Mitogen and stress response pathways: MAP kinase cascades and phosphatase regulation in mammals and yeast. Curr Opin Cell Biol 1995; 7: 798–805PubMedCrossRef
383.
go back to reference Matsuda S, Kawasaki H, Moriguchi T, et al. Activation of protein kinase cascades by osmotic shock. J Biol Chem 1995; 270: 12781–6PubMedCrossRef Matsuda S, Kawasaki H, Moriguchi T, et al. Activation of protein kinase cascades by osmotic shock. J Biol Chem 1995; 270: 12781–6PubMedCrossRef
384.
go back to reference Ichijo H, Nishida E, Irie K, et al. Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK and p38 signaling pathways. Science 1997; 275: 90–4PubMedCrossRef Ichijo H, Nishida E, Irie K, et al. Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK and p38 signaling pathways. Science 1997; 275: 90–4PubMedCrossRef
385.
go back to reference Maeda T, Takekawa M, Saito H. Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-containing osmosensor. Science 1995; 269: 554–8PubMedCrossRef Maeda T, Takekawa M, Saito H. Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-containing osmosensor. Science 1995; 269: 554–8PubMedCrossRef
386.
go back to reference Wang TH, Henley DC, Ichijo H, et al. Involvement of Ras and apoptosis signal-regulating kinase (ASK-1) in activation of the JNK/SAPK cascade by treatment with paclitaxel or vinblastine [abstract]. Proc Am Assoc Cancer Res 1998; 39: 89 Wang TH, Henley DC, Ichijo H, et al. Involvement of Ras and apoptosis signal-regulating kinase (ASK-1) in activation of the JNK/SAPK cascade by treatment with paclitaxel or vinblastine [abstract]. Proc Am Assoc Cancer Res 1998; 39: 89
387.
go back to reference Saitoh M, Nishitoh H, Fuji M, et al. Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1. EMBO J 1998; 17(9): 2596–606PubMedCrossRef Saitoh M, Nishitoh H, Fuji M, et al. Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1. EMBO J 1998; 17(9): 2596–606PubMedCrossRef
388.
go back to reference Ko YG, Seol WG, Kim TH, et al. Functional interaction or human glutaminyl-t RNA synthetase and apoptosis signal-structure kinsase (Ask) 1 [abstract]. Mol Biol Cell 1999; 10: 1909 Ko YG, Seol WG, Kim TH, et al. Functional interaction or human glutaminyl-t RNA synthetase and apoptosis signal-structure kinsase (Ask) 1 [abstract]. Mol Biol Cell 1999; 10: 1909
389.
go back to reference Alessi DR, Saito Y, Campbell DG, et al. Identification of the sites in MAP kinase kinase-1 phosphorylated by p74raf−1. EMBO J 1994; 13: 1610–9PubMed Alessi DR, Saito Y, Campbell DG, et al. Identification of the sites in MAP kinase kinase-1 phosphorylated by p74raf−1. EMBO J 1994; 13: 1610–9PubMed
390.
go back to reference Vaillancourt RR, Gardner AM, Johnson GL. B-Raf-dependent regulation of the MEK-1/mitogen-activated protein kinase pathway in PC12 cells and regulation by cyclic AMP. Mol Cell Biol 1994; 14: 6522–30PubMed Vaillancourt RR, Gardner AM, Johnson GL. B-Raf-dependent regulation of the MEK-1/mitogen-activated protein kinase pathway in PC12 cells and regulation by cyclic AMP. Mol Cell Biol 1994; 14: 6522–30PubMed
391.
go back to reference Papin CA, Eychene A, Brunet G, et al. B-raf protein isoforms interact with and phosphorylate mek-1 on serine residue-218 and residue 222. Oncogene 1995; 10: 1647–51PubMed Papin CA, Eychene A, Brunet G, et al. B-raf protein isoforms interact with and phosphorylate mek-1 on serine residue-218 and residue 222. Oncogene 1995; 10: 1647–51PubMed
392.
go back to reference Seger R, Ahn NG, Posada J, et al. Purification and characterization of mitogen-activated protein kinase activator(s) from epidermal growth factor-stimulated A431 cells. J Biol Chem 1992; 257: 14373–81 Seger R, Ahn NG, Posada J, et al. Purification and characterization of mitogen-activated protein kinase activator(s) from epidermal growth factor-stimulated A431 cells. J Biol Chem 1992; 257: 14373–81
393.
go back to reference Anderson NG, Mailer JL, Tonks NK, et al. Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase. Nature 1990; 343: 651–3PubMedCrossRef Anderson NG, Mailer JL, Tonks NK, et al. Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase. Nature 1990; 343: 651–3PubMedCrossRef
394.
go back to reference Evan G, Wyllie A, Gilbert C, et al. Induction of apoptosis in fibroblasts by the c-myc protein. Cell 1992; 69: 119–25PubMedCrossRef Evan G, Wyllie A, Gilbert C, et al. Induction of apoptosis in fibroblasts by the c-myc protein. Cell 1992; 69: 119–25PubMedCrossRef
396.
go back to reference Franke TF, Kaplan DR, Cantley LC. P13’K: downstream AKTion blocks apoptosis. Cell 1997; 88: 435–7PubMedCrossRef Franke TF, Kaplan DR, Cantley LC. P13’K: downstream AKTion blocks apoptosis. Cell 1997; 88: 435–7PubMedCrossRef
397.
go back to reference Datta SR, Dudek H, Tao X, et al. Akt phosphorylation of BAD couples survival signals to the cell intrinsic death machinery. Cell 1997; 91: 231–41PubMedCrossRef Datta SR, Dudek H, Tao X, et al. Akt phosphorylation of BAD couples survival signals to the cell intrinsic death machinery. Cell 1997; 91: 231–41PubMedCrossRef
398.
go back to reference Marte BM, Downward J. PKB/Akt: connecting phosphoinositide 3-kinase to cell survival and beyond. Trends Biochem Sci 1997; 22: 355–8PubMedCrossRef Marte BM, Downward J. PKB/Akt: connecting phosphoinositide 3-kinase to cell survival and beyond. Trends Biochem Sci 1997; 22: 355–8PubMedCrossRef
399.
go back to reference Van Antwerp DJ, Martin SJ, Kafri T, et al. Suppression of TNF-α-induced apoptosis by NF-κB. Science 1996; 274: 787–89PubMedCrossRef Van Antwerp DJ, Martin SJ, Kafri T, et al. Suppression of TNF-α-induced apoptosis by NF-κB. Science 1996; 274: 787–89PubMedCrossRef
400.
go back to reference Malinin NL, Boldin MP, Kovalenko AV, et al. MAP3K-related kinase involved in NF-κB induction by TNF, CD95 and IL-1. Nature 1997; 385: 540–4PubMedCrossRef Malinin NL, Boldin MP, Kovalenko AV, et al. MAP3K-related kinase involved in NF-κB induction by TNF, CD95 and IL-1. Nature 1997; 385: 540–4PubMedCrossRef
401.
402.
go back to reference Woronicz JD, Gao X, Cao Z, et al. IκB kinase-ß: NF-κB activation and complex formation with IkB kinase-α and NIK. Science 1997; 278: 866–9PubMedCrossRef Woronicz JD, Gao X, Cao Z, et al. IκB kinase-ß: NF-κB activation and complex formation with IkB kinase-α and NIK. Science 1997; 278: 866–9PubMedCrossRef
403.
go back to reference Verma IM, Stevenson JK, Schwartz EM, et al. Rel/NF kappa B/I kappa B family: intimate tales of association and disassociation. Genes Dev 1995; 9: 2723–35PubMedCrossRef Verma IM, Stevenson JK, Schwartz EM, et al. Rel/NF kappa B/I kappa B family: intimate tales of association and disassociation. Genes Dev 1995; 9: 2723–35PubMedCrossRef
404.
go back to reference Beuerle PA, Baltimore D. Activation of DNA-binding activity in an apparently cytoplasmic precursor of the NF-kappa B transcription factor. Cell 1988; 53: 211–7CrossRef Beuerle PA, Baltimore D. Activation of DNA-binding activity in an apparently cytoplasmic precursor of the NF-kappa B transcription factor. Cell 1988; 53: 211–7CrossRef
405.
go back to reference Haskill S, Berg AA, Tompkins SM, et al. Characterization of an immediate-early gene induced in adherent monocytes that encodes I kappa B-like activity. Cell 1991; 65: 1281–9PubMedCrossRef Haskill S, Berg AA, Tompkins SM, et al. Characterization of an immediate-early gene induced in adherent monocytes that encodes I kappa B-like activity. Cell 1991; 65: 1281–9PubMedCrossRef
406.
go back to reference Ganchi PA, Sun SC, Greene WC, et al. I kappa B/MAD-3 masks the nuclear localization signal of NF-kappa B p65 and requires the transactivation domain to inhibit NF-kappa B p65 DNA binding. Mol Biol Cell 1992; 3: 1339–52PubMed Ganchi PA, Sun SC, Greene WC, et al. I kappa B/MAD-3 masks the nuclear localization signal of NF-kappa B p65 and requires the transactivation domain to inhibit NF-kappa B p65 DNA binding. Mol Biol Cell 1992; 3: 1339–52PubMed
407.
go back to reference Brown LF, Berse B, Jackman RW, et al. Expression of vascular permeability factor (vascular endothelial growth factor) and its receptors in breast cancer. Hum Pathol 1995; 26: 86–91PubMedCrossRef Brown LF, Berse B, Jackman RW, et al. Expression of vascular permeability factor (vascular endothelial growth factor) and its receptors in breast cancer. Hum Pathol 1995; 26: 86–91PubMedCrossRef
408.
go back to reference Brockman JA, Scherer DC, McKinsey TA, et al. Coupling of a signal response domain in I kappa B alpha to multiple pathways for NF-kappa B activation. Mol Cell Biol 1995; 15: 2809–18PubMed Brockman JA, Scherer DC, McKinsey TA, et al. Coupling of a signal response domain in I kappa B alpha to multiple pathways for NF-kappa B activation. Mol Cell Biol 1995; 15: 2809–18PubMed
409.
go back to reference Traenckner EB, Pahl HL, Henkel T, et al. Phosphorylation of human I kappa B-alpha on serines 32 and 36 controls I kappa B-alpha proteolysis and NF-kappa B activation in response to diverse stimuli. EMBO J 1995; 14: 2876–83PubMed Traenckner EB, Pahl HL, Henkel T, et al. Phosphorylation of human I kappa B-alpha on serines 32 and 36 controls I kappa B-alpha proteolysis and NF-kappa B activation in response to diverse stimuli. EMBO J 1995; 14: 2876–83PubMed
410.
go back to reference Chen Z, Hagler J, Palombella VJ, et al. Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway. Genes Dev 1995; 9: 1586–97PubMedCrossRef Chen Z, Hagler J, Palombella VJ, et al. Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway. Genes Dev 1995; 9: 1586–97PubMedCrossRef
411.
go back to reference Mercurio F, Zhu H, Murray BW, et al. IKK-1 and IKK-2: cytokine-activated IκB kinases essential for NF-κB activation. Science 1997; 278: 860–6PubMedCrossRef Mercurio F, Zhu H, Murray BW, et al. IKK-1 and IKK-2: cytokine-activated IκB kinases essential for NF-κB activation. Science 1997; 278: 860–6PubMedCrossRef
412.
go back to reference DiDonato JA, Hayakawa M, Rothwarf DM, et al. A cytokine-responsive IkappaB kinase that activates the transcription factor NF-kappaB. Nature 1997; 388: 548–54PubMedCrossRef DiDonato JA, Hayakawa M, Rothwarf DM, et al. A cytokine-responsive IkappaB kinase that activates the transcription factor NF-kappaB. Nature 1997; 388: 548–54PubMedCrossRef
413.
go back to reference Chen RH, Tung R, Abate C, et al. Cytoplasmic to nuclear signal transduction by mitogen-activated protein kinase and 90 kDa ribosomal S6 kinase. Biochem Soc Trans 1993; 21: 895–900PubMed Chen RH, Tung R, Abate C, et al. Cytoplasmic to nuclear signal transduction by mitogen-activated protein kinase and 90 kDa ribosomal S6 kinase. Biochem Soc Trans 1993; 21: 895–900PubMed
414.
go back to reference Xing J, Ginty DD, Greenberg ME. Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase. Science 1996; 273: 969–3CrossRef Xing J, Ginty DD, Greenberg ME. Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase. Science 1996; 273: 969–3CrossRef
415.
go back to reference Ghoda L, Lin X, Greene WC. The 90-kDa ribosomal S6 kinase (pp90rsk) phosphorylates the N-terminal regulatory domain of IκBα and stimulates its degradation in vitro. J Biol Chem 1997; 272: 21281–8PubMedCrossRef Ghoda L, Lin X, Greene WC. The 90-kDa ribosomal S6 kinase (pp90rsk) phosphorylates the N-terminal regulatory domain of IκBα and stimulates its degradation in vitro. J Biol Chem 1997; 272: 21281–8PubMedCrossRef
416.
go back to reference Boldin M, Varfolomeev EE, Pancer Z, et al. A novel protein that interacts with the death domain of Fas/APO 1 contains a sequence motif related to the death domain. J Biol Chem 1995; 270: 7795–8PubMedCrossRef Boldin M, Varfolomeev EE, Pancer Z, et al. A novel protein that interacts with the death domain of Fas/APO 1 contains a sequence motif related to the death domain. J Biol Chem 1995; 270: 7795–8PubMedCrossRef
417.
go back to reference Peter ME, Kischkel FC, Hellrandt S, et al. CD95 (APO-1/Fas)-associating signaling proteins. Cell Death Differ 1996; 3: 161–70PubMed Peter ME, Kischkel FC, Hellrandt S, et al. CD95 (APO-1/Fas)-associating signaling proteins. Cell Death Differ 1996; 3: 161–70PubMed
418.
go back to reference Alnemri ES, Livingson DJ, Nicholson DW, et al. Human ICE/CED-3 protease nomenclature [letter]. Cell 1996; 87: 171PubMedCrossRef Alnemri ES, Livingson DJ, Nicholson DW, et al. Human ICE/CED-3 protease nomenclature [letter]. Cell 1996; 87: 171PubMedCrossRef
419.
go back to reference Muzio M, Chinnaiyan AM, Kischkel FC, et al. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell 1996; 85: 817–27PubMedCrossRef Muzio M, Chinnaiyan AM, Kischkel FC, et al. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell 1996; 85: 817–27PubMedCrossRef
420.
go back to reference Boldin MP, Goncharov TM, Goltsev YV, et al. Involvement of MACH, a novel MORT-1/FADD-interacting protease, in Fas/APO-1 and TNF receptor-induced cell death. Cell 1996; 85: 803–15PubMedCrossRef Boldin MP, Goncharov TM, Goltsev YV, et al. Involvement of MACH, a novel MORT-1/FADD-interacting protease, in Fas/APO-1 and TNF receptor-induced cell death. Cell 1996; 85: 803–15PubMedCrossRef
421.
go back to reference Kischkel FC, Hellbrandt S, Behrmann I, et al. Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins (CAP) form a death-inducing signaling complex (DISC) with the receptor. EMBO J 1995; 14: 5579–88PubMed Kischkel FC, Hellbrandt S, Behrmann I, et al. Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins (CAP) form a death-inducing signaling complex (DISC) with the receptor. EMBO J 1995; 14: 5579–88PubMed
422.
go back to reference Medema JP, Scaffidi C, Kischkel FC, et al. FLICE is activated by association with the CD95 death-inducing signaling complex (DISC). EMBO J 1997; 16: 2794–804PubMedCrossRef Medema JP, Scaffidi C, Kischkel FC, et al. FLICE is activated by association with the CD95 death-inducing signaling complex (DISC). EMBO J 1997; 16: 2794–804PubMedCrossRef
423.
go back to reference Froelich CJ, Dixit VM, Yang X. Lymphocyte granule-mediated apoptosis: matters of viral mimicry and deadly proteases. Immunol Today 1998; 19: 30–6PubMedCrossRef Froelich CJ, Dixit VM, Yang X. Lymphocyte granule-mediated apoptosis: matters of viral mimicry and deadly proteases. Immunol Today 1998; 19: 30–6PubMedCrossRef
424.
go back to reference Müller R, Mumberg D, Lucibello FC. Signals and genes in the control ofthe cell cycle progression. BBA 1993; 1155: 151–79PubMed Müller R, Mumberg D, Lucibello FC. Signals and genes in the control ofthe cell cycle progression. BBA 1993; 1155: 151–79PubMed
425.
go back to reference Müller R. Transcriptional regulation during the mammalian cell cycle. Trends Genet 1995; 11: 173–8PubMedCrossRef Müller R. Transcriptional regulation during the mammalian cell cycle. Trends Genet 1995; 11: 173–8PubMedCrossRef
426.
go back to reference Bürger C, Wick M, Brüsselbach S, et al. Differential induction of ‘metabolic genes’ after mitogen stimulation and during normal cell cycle progression. J Cell Sci 1994; 107: 241–52PubMed Bürger C, Wick M, Brüsselbach S, et al. Differential induction of ‘metabolic genes’ after mitogen stimulation and during normal cell cycle progression. J Cell Sci 1994; 107: 241–52PubMed
429.
go back to reference Hunter T, Pines J. Cyclins and cancer. II: Cyclin D and cdk inhibitors come of age. Cell 1994; 79: 573–82PubMedCrossRef Hunter T, Pines J. Cyclins and cancer. II: Cyclin D and cdk inhibitors come of age. Cell 1994; 79: 573–82PubMedCrossRef
430.
go back to reference Peter M, Herskowitz I. Joining the complex: cyclin-dependent kinase inhibitory proteins and the cell cycle. Cell 1984; 79: 181–4CrossRef Peter M, Herskowitz I. Joining the complex: cyclin-dependent kinase inhibitory proteins and the cell cycle. Cell 1984; 79: 181–4CrossRef
431.
go back to reference Hannon GF, Beach D. p15INK4B is a potential effector of TGFfl-induced cell cycle arrest. Nature 1994; 371: 257–61PubMedCrossRef Hannon GF, Beach D. p15INK4B is a potential effector of TGFfl-induced cell cycle arrest. Nature 1994; 371: 257–61PubMedCrossRef
432.
go back to reference Guan KL, Jenkins CW, Li Y, et al. Growth suppression by p18, a p16INK4/MTS1- and p14INK4B/MTS2-related cdk6 inhibitor, correlates with wild-type pRb function. Genes Dev 1994; 8: 2939–52PubMedCrossRef Guan KL, Jenkins CW, Li Y, et al. Growth suppression by p18, a p16INK4/MTS1- and p14INK4B/MTS2-related cdk6 inhibitor, correlates with wild-type pRb function. Genes Dev 1994; 8: 2939–52PubMedCrossRef
433.
go back to reference Noda A, Ning Y, Venable SF, Pereira-Smith OM, et al. Cloning of senescent cell-derived inhibitors of DNA synthesis using an expression screen. Exp Cell Res 1994; 211: 90PubMedCrossRef Noda A, Ning Y, Venable SF, Pereira-Smith OM, et al. Cloning of senescent cell-derived inhibitors of DNA synthesis using an expression screen. Exp Cell Res 1994; 211: 90PubMedCrossRef
434.
go back to reference DeBondt HL, Rosenblatt J, Jancarik J, et al. Crystal structure of cyclin-dependent kinase 2. Nature 1993; 363: 595–602CrossRef DeBondt HL, Rosenblatt J, Jancarik J, et al. Crystal structure of cyclin-dependent kinase 2. Nature 1993; 363: 595–602CrossRef
435.
go back to reference Lees EM, Harlow E. Sequences within the conserved cyclin box of human cyclin A are sufficient for binding to and activation of cdc2 kinase. Mol Cell Biol 1993; 13: 1194–201PubMed Lees EM, Harlow E. Sequences within the conserved cyclin box of human cyclin A are sufficient for binding to and activation of cdc2 kinase. Mol Cell Biol 1993; 13: 1194–201PubMed
436.
go back to reference Endicott JA, Nurse P, Johnson LN. Mutational analysis supports a structural model for the cell cycle kinase p 34. Protein Eng 1994; 7: 243–53PubMedCrossRef Endicott JA, Nurse P, Johnson LN. Mutational analysis supports a structural model for the cell cycle kinase p 34. Protein Eng 1994; 7: 243–53PubMedCrossRef
437.
go back to reference Solomon MJ. The function(s) of CAK, the p34cdc2-activating kinase. Trends Biochem Sci 1994; 19: 496–500PubMedCrossRef Solomon MJ. The function(s) of CAK, the p34cdc2-activating kinase. Trends Biochem Sci 1994; 19: 496–500PubMedCrossRef
438.
go back to reference Ducommun B, Brambilla P, Felix MA, et al. cdc2 phosphorylation is required for its interaction with cyclin. EMBO J 1991 10: 3311–9PubMed Ducommun B, Brambilla P, Felix MA, et al. cdc2 phosphorylation is required for its interaction with cyclin. EMBO J 1991 10: 3311–9PubMed
439.
go back to reference Desai D, Wessling HC, Fisher RP, et al. Effects of phosphorylation by CAK on cyclin binding by cdc2 and cdk 2. Mol Cell Biol 1995; 15: 345–50PubMed Desai D, Wessling HC, Fisher RP, et al. Effects of phosphorylation by CAK on cyclin binding by cdc2 and cdk 2. Mol Cell Biol 1995; 15: 345–50PubMed
440.
go back to reference Zhang J, Sanchez RJ, Wang S, et al. Substrate specificity of cdc2 kinase from human HeLa cells as determined with synthetic peptides and molecular modelling. Arch Biochem Biophys 1994; 351: 415–24CrossRef Zhang J, Sanchez RJ, Wang S, et al. Substrate specificity of cdc2 kinase from human HeLa cells as determined with synthetic peptides and molecular modelling. Arch Biochem Biophys 1994; 351: 415–24CrossRef
441.
go back to reference Rickert P, Seghezzi W, Shanahan F, et al. Cyclin C/cdk8 is a novel CTD kinase associated with RNA polymerase II. Oncogene 1996; 12: 2631–40PubMed Rickert P, Seghezzi W, Shanahan F, et al. Cyclin C/cdk8 is a novel CTD kinase associated with RNA polymerase II. Oncogene 1996; 12: 2631–40PubMed
442.
go back to reference Galaktionov K, Beach D. Specific activation of cdc25 tyrosine phosphatases by B-type cyclin: evidence for multiple roles of mitotic cyclins. Cell 1991; 67: 1181–94PubMedCrossRef Galaktionov K, Beach D. Specific activation of cdc25 tyrosine phosphatases by B-type cyclin: evidence for multiple roles of mitotic cyclins. Cell 1991; 67: 1181–94PubMedCrossRef
443.
go back to reference Zheng XF, Ruderman JV. Functional analysis of the P box, a domain in cyclin B required for the activation of Cdc 25. Cell 1993; 78: 155–64 Zheng XF, Ruderman JV. Functional analysis of the P box, a domain in cyclin B required for the activation of Cdc 25. Cell 1993; 78: 155–64
444.
go back to reference Karp JE, Broder S. Molecular foundations of cancer: new targets for intervention. Nat Med 1995; 1: 309–20PubMedCrossRef Karp JE, Broder S. Molecular foundations of cancer: new targets for intervention. Nat Med 1995; 1: 309–20PubMedCrossRef
445.
go back to reference Soufir N, Avril MF, Chompret A, et al. Prevalence of p16 and CDK4 germline mutations in 48 melanoma-prone families in France. Human Mol Genetics 1998; 7: 209–16CrossRef Soufir N, Avril MF, Chompret A, et al. Prevalence of p16 and CDK4 germline mutations in 48 melanoma-prone families in France. Human Mol Genetics 1998; 7: 209–16CrossRef
446.
go back to reference Wölfel T, Hauer M, Schneider J, et al. A p16INK4a insensitive CDK4 mutant targeted by cytolytic T lymphocyte in a human melanoma. Science 1995; 269: 2181–4CrossRef Wölfel T, Hauer M, Schneider J, et al. A p16INK4a insensitive CDK4 mutant targeted by cytolytic T lymphocyte in a human melanoma. Science 1995; 269: 2181–4CrossRef
447.
go back to reference Keyomarsi K, Pardee AB. Redundant cyclin overexpression and gene amplification in breast cancer cells. Proc Natl Acad Sci U S A 1993; 90: 1112–26PubMedCrossRef Keyomarsi K, Pardee AB. Redundant cyclin overexpression and gene amplification in breast cancer cells. Proc Natl Acad Sci U S A 1993; 90: 1112–26PubMedCrossRef
448.
go back to reference Keyomarsi K, O’Leary N, Molnar G, et al. Cyclin E, a potential prognostic marker for breast cancer. Cancer Res 1994; 54: 380–5PubMed Keyomarsi K, O’Leary N, Molnar G, et al. Cyclin E, a potential prognostic marker for breast cancer. Cancer Res 1994; 54: 380–5PubMed
449.
450.
go back to reference Mulligan GJ, Jacks T. The retinoblastoma gene family: cousins with overlapping interests. Trends Genet 1998; 14: 223PubMedCrossRef Mulligan GJ, Jacks T. The retinoblastoma gene family: cousins with overlapping interests. Trends Genet 1998; 14: 223PubMedCrossRef
451.
go back to reference Grana X, Garriga J, Mayol X. Role of the retinoblastoma protein family, pRb, p107 and p130 in the negative control of cell growth. Oncogene 1998; 17: 3365–83PubMedCrossRef Grana X, Garriga J, Mayol X. Role of the retinoblastoma protein family, pRb, p107 and p130 in the negative control of cell growth. Oncogene 1998; 17: 3365–83PubMedCrossRef
452.
go back to reference Sedlacek HH, Czech J, Naik R, et al. Flavopiridol (L86-8275; NSC 64890), a new kinase inhibitor for tumor therapy. Int J Oncol 1996; 9: 1143–68PubMed Sedlacek HH, Czech J, Naik R, et al. Flavopiridol (L86-8275; NSC 64890), a new kinase inhibitor for tumor therapy. Int J Oncol 1996; 9: 1143–68PubMed
453.
go back to reference Lipson KE, Wang X, Chen H, et al. SU101, and not its major metabolite, inhibits PDGF-dependent receptor tyrosine phosphorylation, cell cycle progression, and human tumor cell growth. Proc Am Assoc Cancer Res 1998; 39: 558 Lipson KE, Wang X, Chen H, et al. SU101, and not its major metabolite, inhibits PDGF-dependent receptor tyrosine phosphorylation, cell cycle progression, and human tumor cell growth. Proc Am Assoc Cancer Res 1998; 39: 558
454.
go back to reference Blaskovich MA, Wang H, Hamilton AD, et al. Selective inhibition of PDGF-dependent receptor tyrosine phosphorylation and MAP kinase activation by tryptophan derivatives [abstract]. Proc Am Assoc Cancer Res 1998; 39: 559 Blaskovich MA, Wang H, Hamilton AD, et al. Selective inhibition of PDGF-dependent receptor tyrosine phosphorylation and MAP kinase activation by tryptophan derivatives [abstract]. Proc Am Assoc Cancer Res 1998; 39: 559
455.
go back to reference Vincent PW, Akinson BE, Zhou H, et al. Characterization of the in vivo activity of a novel EGF receptor family kinase inhibitor, PD 169414 [abstract]. Proc Am Assoc Cancer Res 1998; 39: 560 Vincent PW, Akinson BE, Zhou H, et al. Characterization of the in vivo activity of a novel EGF receptor family kinase inhibitor, PD 169414 [abstract]. Proc Am Assoc Cancer Res 1998; 39: 560
456.
go back to reference Miller PE, Robinson J, Moyer JD, et al. CP-358,774, a selective EGFR kinase inhibitor, inhibits phosphorylation of SHC and retinoblastoma protein in human tumor xenografts [abstract]. Proc Am Assoc Cancer Res 1998; 39: 560 Miller PE, Robinson J, Moyer JD, et al. CP-358,774, a selective EGFR kinase inhibitor, inhibits phosphorylation of SHC and retinoblastoma protein in human tumor xenografts [abstract]. Proc Am Assoc Cancer Res 1998; 39: 560
457.
go back to reference Mett H, Buchdunger E. Müller M. CGP 59326, a potent protein tyrosine kinase (PTK) inhibitor which selectively blocks growth of epidermal growth factor receptor (EGFR) expressing tumor cells [abstract]. Proc Am Assoc Cancer Res 1998; 39: 560 Mett H, Buchdunger E. Müller M. CGP 59326, a potent protein tyrosine kinase (PTK) inhibitor which selectively blocks growth of epidermal growth factor receptor (EGFR) expressing tumor cells [abstract]. Proc Am Assoc Cancer Res 1998; 39: 560
458.
go back to reference Fong TAT, Shawver LK, App H, et al. SU5416: a potent and selective Flk-1/KDR kinase inhibitor that blocks Flk-1 phosphorylation, endothelial cell mitogenesis and tumor growth. Proc Am Assoc Cancer Res 1998; 39: 560 Fong TAT, Shawver LK, App H, et al. SU5416: a potent and selective Flk-1/KDR kinase inhibitor that blocks Flk-1 phosphorylation, endothelial cell mitogenesis and tumor growth. Proc Am Assoc Cancer Res 1998; 39: 560
459.
go back to reference Kraker AJ, Moore CW, Hartl BG, et al. Effects of c-src selective pyrido[2,3-d]-pyrimidine tyrosine kinase inhibitors on the phophorylation of p130cas, paxillin, and STAT3 and on proliferation in human carcinoma cell lines [abstract]. Proc Am Assoc Cancer Res 1998; 39: 559 Kraker AJ, Moore CW, Hartl BG, et al. Effects of c-src selective pyrido[2,3-d]-pyrimidine tyrosine kinase inhibitors on the phophorylation of p130cas, paxillin, and STAT3 and on proliferation in human carcinoma cell lines [abstract]. Proc Am Assoc Cancer Res 1998; 39: 559
460.
go back to reference Gay B, Furet P, Fretz H, et al. Design of a highly potent inhibitor of Grb2 SH2 domain with cellular and in vivo activity [abstract]. Proc Am Assoc Cancer Res 1998; 39: 559 Gay B, Furet P, Fretz H, et al. Design of a highly potent inhibitor of Grb2 SH2 domain with cellular and in vivo activity [abstract]. Proc Am Assoc Cancer Res 1998; 39: 559
461.
go back to reference Buchdunger E, Cioiffi C, Cozens R, et al. Preclinical evaluation of CGP 57148, a potent protein-tyrosine kinase inhibitor as a therapeutic agent for PH+ leukemias and solid tumors [abstract]. Proc Am Assoc Cancer Res 1998; 39: 559 Buchdunger E, Cioiffi C, Cozens R, et al. Preclinical evaluation of CGP 57148, a potent protein-tyrosine kinase inhibitor as a therapeutic agent for PH+ leukemias and solid tumors [abstract]. Proc Am Assoc Cancer Res 1998; 39: 559
462.
go back to reference Heimbrook DC, Huber HE, Stordivant SM, et al. Identification of potent, selective kinase inhibitors of Raf Proc Am Assoc Cancer Res 1998; 39: 558 Heimbrook DC, Huber HE, Stordivant SM, et al. Identification of potent, selective kinase inhibitors of Raf Proc Am Assoc Cancer Res 1998; 39: 558
463.
go back to reference Meyer T, Zimmermann J, Geiger T, et al. CGP 60474, a protein kinase inhibitor with potent antitumor activity in vivo at well tolerated doses [abstract]. Proc Am Assoc Cancer Res 1998; 39: 558 Meyer T, Zimmermann J, Geiger T, et al. CGP 60474, a protein kinase inhibitor with potent antitumor activity in vivo at well tolerated doses [abstract]. Proc Am Assoc Cancer Res 1998; 39: 558
464.
go back to reference Senderowicz A, Headlee D, Stinson S, et al. Phase I trial of a novel cyclin-dependent kinase inhibitor flavopiridol in patients with refractory neoplasms. Clin Oncol 1998; 16(9): 2986–99 Senderowicz A, Headlee D, Stinson S, et al. Phase I trial of a novel cyclin-dependent kinase inhibitor flavopiridol in patients with refractory neoplasms. Clin Oncol 1998; 16(9): 2986–99
465.
go back to reference Werner JL, Kelsen DP, Karpeh M, et al. The cyclin dependent kinase inhibitor flavopiridol is an active and unexpectedly toxic agent in advanced gastric cancer [abstract]. Proceedings of the 34th Annual Meeting of the American Society of Clinical Oncology: 1998 May 16–19; Los Angeles, 234a Werner JL, Kelsen DP, Karpeh M, et al. The cyclin dependent kinase inhibitor flavopiridol is an active and unexpectedly toxic agent in advanced gastric cancer [abstract]. Proceedings of the 34th Annual Meeting of the American Society of Clinical Oncology: 1998 May 16–19; Los Angeles, 234a
466.
go back to reference Schwartz GK, Werner JL, Maslak P, et al. Flavopiridol enhances the biological effects of paclitaxel: a phase I trial in patients with advance solid tumors. Proceedings of the 34th Annual Meeting of the American Society of Clinical Oncology: 1998 May 16–19; Los Angeles, 188a Schwartz GK, Werner JL, Maslak P, et al. Flavopiridol enhances the biological effects of paclitaxel: a phase I trial in patients with advance solid tumors. Proceedings of the 34th Annual Meeting of the American Society of Clinical Oncology: 1998 May 16–19; Los Angeles, 188a
467.
go back to reference Parker BW, Senderowicz AM, Nieves-Neira W, et al. DNA fragmentation and apoptosis of lymphoma and prostate cancer cell lines after flavopiridol treatment [abstract]. Proc Am Assoc Cancer Res 1996; 37: 398 Parker BW, Senderowicz AM, Nieves-Neira W, et al. DNA fragmentation and apoptosis of lymphoma and prostate cancer cell lines after flavopiridol treatment [abstract]. Proc Am Assoc Cancer Res 1996; 37: 398
468.
go back to reference Schwartz GK, Farsi K, Danso D, et al. The protein kinase C inhibitors UCN-01 and flavopiridol significantly enhance the cytotoxic effect of chemotherapy by promoting apoptosis in gastric and breast cancer cells [abstract]. Proc Am Soc Oncol 1996; 15: 501 Schwartz GK, Farsi K, Danso D, et al. The protein kinase C inhibitors UCN-01 and flavopiridol significantly enhance the cytotoxic effect of chemotherapy by promoting apoptosis in gastric and breast cancer cells [abstract]. Proc Am Soc Oncol 1996; 15: 501
469.
go back to reference Brüsselbach S, Nettelbeck DM, Sedlacek HH, et al. Cell cycle-independent induction of apoptosis by the anti-tumor drug Flavopiridol in endothelial cells. Int J Cancer 1998; 77: 146–52PubMedCrossRef Brüsselbach S, Nettelbeck DM, Sedlacek HH, et al. Cell cycle-independent induction of apoptosis by the anti-tumor drug Flavopiridol in endothelial cells. Int J Cancer 1998; 77: 146–52PubMedCrossRef
470.
go back to reference Bible KC, Kaufmann SM. Flavopiridol: a cytotoxic flavone that induces cell death in noncycling A549 human lung carcinoma cells. Cancer Res 1996; 56: 4856–61PubMed Bible KC, Kaufmann SM. Flavopiridol: a cytotoxic flavone that induces cell death in noncycling A549 human lung carcinoma cells. Cancer Res 1996; 56: 4856–61PubMed
471.
go back to reference Simizu S, Imoto M, Masuda N, et al. Involvement of hydrogen peroxide production in erbstatin-induced apoptosis in human small cell lung carcinoma cells. Cancer Res 1996; 56: 4978–82PubMed Simizu S, Imoto M, Masuda N, et al. Involvement of hydrogen peroxide production in erbstatin-induced apoptosis in human small cell lung carcinoma cells. Cancer Res 1996; 56: 4978–82PubMed
472.
go back to reference Palumbo GA, Yarom N, Gazit A, et al. The tyrphostin AG17 induces apoptosis and inhibition of cdk2 activity in a lymphoma cell line that overexpresses bcl-2. Cancer Res 1997; 57: 2434–9PubMed Palumbo GA, Yarom N, Gazit A, et al. The tyrphostin AG17 induces apoptosis and inhibition of cdk2 activity in a lymphoma cell line that overexpresses bcl-2. Cancer Res 1997; 57: 2434–9PubMed
473.
go back to reference Moyer JD, Barbacci EG, Iwata KK, et al. Induction of apoptosis and cell cycle arrest by CP-358,774, an inhibitor of epidermal growth factor receptor tyrosine kinase. Cancer Res 1997; 57: 4838–48PubMed Moyer JD, Barbacci EG, Iwata KK, et al. Induction of apoptosis and cell cycle arrest by CP-358,774, an inhibitor of epidermal growth factor receptor tyrosine kinase. Cancer Res 1997; 57: 4838–48PubMed
474.
go back to reference Wei Y, Zhao X, Kariya Y, et al. Induction of apoptosis by quercetin: involvement of heat shock protein. Cancer Res 1994; 54: 4952–7PubMed Wei Y, Zhao X, Kariya Y, et al. Induction of apoptosis by quercetin: involvement of heat shock protein. Cancer Res 1994; 54: 4952–7PubMed
475.
go back to reference Akiyama T, Ishida J, Nakagawa S, et al. Genistein, a specific inhibitor of tyrosine-specific protein kinases. J Biol Chem 1987; 262: 5592–5PubMed Akiyama T, Ishida J, Nakagawa S, et al. Genistein, a specific inhibitor of tyrosine-specific protein kinases. J Biol Chem 1987; 262: 5592–5PubMed
476.
go back to reference Yamashita Y, Kawada S, Nakano H. Induction of mammalian topoisomerase II-dependent DNA cleavage by non-intercalative flavonoids, genistein, and phorbol. Biochem Pharmacol 1990; 39: 187–93CrossRef Yamashita Y, Kawada S, Nakano H. Induction of mammalian topoisomerase II-dependent DNA cleavage by non-intercalative flavonoids, genistein, and phorbol. Biochem Pharmacol 1990; 39: 187–93CrossRef
477.
go back to reference Constantinou A, Kiguchi K, Hubennan E. Induction of differentiation and DNA strand breakage in human HL-60 and K-562 leukemia cells by genistein. Cancer Res 1990; 50: 2618–24PubMed Constantinou A, Kiguchi K, Hubennan E. Induction of differentiation and DNA strand breakage in human HL-60 and K-562 leukemia cells by genistein. Cancer Res 1990; 50: 2618–24PubMed
478.
go back to reference Okura A, Arakawa H, Oka H, et al. Effect of genistein on topoisomerase activity and on the growth of (Val 12) Ha-rastransformed NHI-3T3 cells. Biochem Biophys Res Commun 1988; 157: 183–9PubMedCrossRef Okura A, Arakawa H, Oka H, et al. Effect of genistein on topoisomerase activity and on the growth of (Val 12) Ha-rastransformed NHI-3T3 cells. Biochem Biophys Res Commun 1988; 157: 183–9PubMedCrossRef
479.
go back to reference Rao CV, Wang CX, Simi B, et al. Enhancement of experimental colon cancer by genistein. Cancer Res 1997; 57: 3717–22PubMed Rao CV, Wang CX, Simi B, et al. Enhancement of experimental colon cancer by genistein. Cancer Res 1997; 57: 3717–22PubMed
480.
go back to reference Zava DT, Duwe G. Estrogenic and antiproliferative properties of genistein and other flavonoids in human breast cancer cells in vitro. Nutr Cancer 1997; 27: 31–40PubMedCrossRef Zava DT, Duwe G. Estrogenic and antiproliferative properties of genistein and other flavonoids in human breast cancer cells in vitro. Nutr Cancer 1997; 27: 31–40PubMedCrossRef
481.
go back to reference Sato S, Kohno K, Izumi H, et al. Differential effects of pKI H-7 on activation of human MDRI promoter. Cell Pharmacol 1995; 2: 153–7 Sato S, Kohno K, Izumi H, et al. Differential effects of pKI H-7 on activation of human MDRI promoter. Cell Pharmacol 1995; 2: 153–7
482.
go back to reference Li JJ, Westergaard C, Ghosh P, et al. Inhibitors of both nuclear factor-kappaB and activator protein-1 activation block the neoplastic transformation response. Cancer Res 1997; 57: 3569–76PubMed Li JJ, Westergaard C, Ghosh P, et al. Inhibitors of both nuclear factor-kappaB and activator protein-1 activation block the neoplastic transformation response. Cancer Res 1997; 57: 3569–76PubMed
483.
go back to reference Monia BP, Sasmor H, Johnston JF, et al. Sequence-specific antitumor activity of a phosphorothioate oligodeoxyribonucleotide targeted to human C-raf kinase supports an antisense mechanism of action in vivo. Proc Natl Acad Sci U S A 1996; 93: 15481–4PubMedCrossRef Monia BP, Sasmor H, Johnston JF, et al. Sequence-specific antitumor activity of a phosphorothioate oligodeoxyribonucleotide targeted to human C-raf kinase supports an antisense mechanism of action in vivo. Proc Natl Acad Sci U S A 1996; 93: 15481–4PubMedCrossRef
484.
go back to reference Monia BP, Johnston JF, Geiger T, et al. Antitumor activity of a phosphorothioate antisense oligodeoxynucleotide targeted against C-raf kinase. Nat Med 1996; 2: 668–75PubMedCrossRef Monia BP, Johnston JF, Geiger T, et al. Antitumor activity of a phosphorothioate antisense oligodeoxynucleotide targeted against C-raf kinase. Nat Med 1996; 2: 668–75PubMedCrossRef
485.
go back to reference Filgueira W, De Azevedo jr, Mueller-Dieckmann HJ, et al. Structural basis for specific and potency of a flavonoid inhibitor of human cdk2, a cell cycle kinase. Proc Natl Acad Sci U S A 1996; 93: 2735CrossRef Filgueira W, De Azevedo jr, Mueller-Dieckmann HJ, et al. Structural basis for specific and potency of a flavonoid inhibitor of human cdk2, a cell cycle kinase. Proc Natl Acad Sci U S A 1996; 93: 2735CrossRef
486.
go back to reference Pollman MJ, Hall JL, Mann MJ, et al. Inhibition of neointimal cell bcl-x expression induces apoptosis and regression of vascular disease. Nature Med 1998; 4: 222–7PubMedCrossRef Pollman MJ, Hall JL, Mann MJ, et al. Inhibition of neointimal cell bcl-x expression induces apoptosis and regression of vascular disease. Nature Med 1998; 4: 222–7PubMedCrossRef
487.
go back to reference Kraemer HP, Sedlacek HH. The human tumor clonogenic assay for the prediction of tumor sensitivity. In: Beger HG, Büchler M, Reisfeld RA, et al., editors. Cancer therapy. Berlin: Springer Verlag, 1989: 244–7 Kraemer HP, Sedlacek HH. The human tumor clonogenic assay for the prediction of tumor sensitivity. In: Beger HG, Büchler M, Reisfeld RA, et al., editors. Cancer therapy. Berlin: Springer Verlag, 1989: 244–7
488.
go back to reference Jäger W, Zembsch B, Wolschann P, et al. Metabolism of the anticancer drug flavopiridol, a new inhibitor of cyclin dependent kinases, in rat liver. Life Sci 1998; 62: 1861–73PubMedCrossRef Jäger W, Zembsch B, Wolschann P, et al. Metabolism of the anticancer drug flavopiridol, a new inhibitor of cyclin dependent kinases, in rat liver. Life Sci 1998; 62: 1861–73PubMedCrossRef
Metadata
Title
Kinase Inhibitors in Cancer Therapy
A Look Ahead
Author
Dr H. H. Sedlacek
Publication date
01-03-2000
Publisher
Springer International Publishing
Published in
Drugs / Issue 3/2000
Print ISSN: 0012-6667
Electronic ISSN: 1179-1950
DOI
https://doi.org/10.2165/00003495-200059030-00004

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