Skip to main content
Key Specialties
Cardiology Diabetology Endocrinology Gastroenterology Geriatrics and Gerontology Gynecology and Obstetrics Hematology Infectious Disease Internal Medicine Nephrology Neurology Oncology Pediatrics Respiratory Medicine Rheumatology Surgery
Congress Coverage
2024 ACC Congress 2023 ESMO Congress 2023 EASD Congress 2023 ERS Congress 2023 ESC Congress
Clinical Collections
Advances in Alzheimer’s

At a glance: The ONWARDS insulin icodec trials

A round-up of the ONWARDS phase 3 clinical trials evaluating the novel weekly insulin icodec in people with diabetes.
ADVANCED SEARCH
Log in
Top
Cancer and Metastasis Reviews
Published in: Cancer and Metastasis Reviews 2-3/2018

01-09-2018

Lack of effective translational regulation of PLD expression and exosome biogenesis in triple-negative breast cancer cells

Author: Julian Gomez-Cambronero

Published in: Cancer and Metastasis Reviews | Issue 2-3/2018

Login to get access

Abstract

Triple-negative breast cancer (TNBC) is an aggressive subtype of breast cancer that is difficult to treat since cells lack the three receptors (ES, PR, or HER) that the most effective treatments target. We have used a well-established TNBC cell line (MDA-MB-231) from which we found evidence in support for a phospholipase D (PLD)-mediated tumor growth and metastasis: high levels of expression of PLD, as well as the absence of inhibitory miRs (such as miR-203) and 3′-mRNA PARN deadenylase activity in these cells. Such findings are not present in a luminal B cell line, MCF-7, and we propose a new miR•PARN•PLD node that is not uniform across breast cancer molecular subtypes and as such TNBC could be pharmacologically targeted differentially. We review the participation of PLD and phosphatidic acid (PA), its enzymatic product, as new “players” in breast cancer biology, with the aspects of regulation of the tumor microenvironment, macrophage polarization, regulation of PLD transcripts by specific miRs and deadenylases, and PLD-regulated exosome biogenesis. A new signaling miR•PARN•PLD node could serve as new biomarkers for TNBC abnormal signaling and metastatic disease staging, potentially before metastases are able to be visualized using conventional imaging.
Literature
1.
2.
Torre, L. A., Bray, F., Siegel, R. L., Ferlay, J., Lortet-Tieulent, J., & Jemal, A. (2015). Global cancer statistics, 2012. CA: a Cancer Journal for Clinicians, 65, 87–108.
3.
Jemal, A., Center, M. M., DeSantis, C., & Ward, E. M. (2010). Global patterns of cancer incidence and mortality rates and trends. Cancer Epidemiology, Biomarkers & Prevention: a Publication of the American Association for Cancer Research, cosponsored by the American Society of Preventive Oncology, 19, 1893–1907.CrossRef
4.
Kimbung, S., Loman, N., & Hedenfalk, I. (2015). Clinical and molecular complexity of breast cancer metastases. Seminars in Cancer Biology, 35, 85–95.PubMedCrossRef
5.
DeSantis, C. E., Fedewa, S. A., Goding Sauer, A., Kramer, J. L., Smith, R. A., & Jemal, A. (2016). Breast cancer statistics, 2015: convergence of incidence rates between black and white women. CA: a Cancer Journal for Clinicians, 66, 31–42.
6.
U.S. Cancer Statistics Working Group. (2015). United States Cancer Statistics: 1999–2012 incidence and mortality web-based report. Atlanta: U.S. Department of Health and Human Services, Centers for Disease Control and Prevention and National Cancer Institute.
7.
Leone, J. P., & Leone, B. A. (2015). Breast cancer brain metastases: the last frontier. Experimental Hematology & Oncology, 4, 33.CrossRef
8.
Fan, J., Chen, D., Du, H., Shen, C., & Che, G. (2015). Prognostic factors for resection of isolated pulmonary metastases in breast cancer patients: a systematic review and meta-analysis. Journal of Thoracic Disease, 7, 1441–1451.PubMedPubMedCentral
9.
10.
Adhikary, S., & Eilers, M. (2005). Transcriptional regulation and transformation by Myc proteins. Nature Reviews. Molecular Cell Biology, 6, 635–645.PubMedCrossRef
11.
Bredemeier, M., Kasimir-Bauer, S., Kolberg, H. C., Herold, T., Synoracki, S., Hauch, S., Edimiris, P., Bankfalvi, A., Tewes, M., Kimmig, R., & Aktas, B. (2017). Comparison of the PI3KCA pathway in circulating tumor cells and corresponding tumor tissue of patients with metastatic breast cancer. Molecular Medicine Reports, 15, 2957–2968.PubMedPubMedCentralCrossRef
12.
Hu, J., Banerjee, A., & Goss, D. J. (2005). Assembly of b/HLH/z proteins c-Myc, Max, and Mad1 with cognate DNA: importance of protein-protein and protein-DNA interactions. Biochemistry, 44, 11855–11863.PubMedPubMedCentralCrossRef
13.
Kim, D., Hong, A., Park, H. I., Shin, W. H., Yoo, L., Jeon, S. J., & Chung, K. C. (2017). Deubiquitinating enzyme USP22 positively regulates c-Myc stability and tumorigenic activity in mammalian and breast cancer cells. Journal of Cellular Physiology, 232, 3664–3676.PubMedCrossRef
14.
McGee, S. R., Tibiche, C., Trifiro, M., & Wang, E. (2017). Network analysis reveals a signaling regulatory loop in the PIK3CA-mutated breast cancer predicting survival outcome. Genomics, Proteomics & Bioinformatics, 15, 121–129.CrossRef
15.
Ren, J., Jin, F., Yu, Z., Zhao, L., Wang, L., Bai, X., Zhao, H., Yao, W., Mi, X., Wang, E., Olopade, O. I., & Wei, M. (2013). MYC overexpression and poor prognosis in sporadic breast cancer with BRCA1 deficiency. Tumour Biology: the Journal of the International Society for Oncodevelopmental Biology and Medicine, 34, 3945–3958.CrossRef
16.
Samimi, G., Bernardini, M. Q., Brody, L. C., Caga-Anan, C. F., Campbell, I. G., Chenevix-Trench, G., Couch, F. J., Dean, M., de Hullu, J. A., Domchek, S. M., Drapkin, R., Spencer Feigelson, H., Friedlander, M., Gaudet, M. M., Harmsen, M. G., Hurley, K., James, P. A., Kwon, J. S., Lacbawan, F., Lheureux, S., Mai, P. L., Mechanic, L. E., Minasian, L. M., Myers, E. R., Robson, M. E., Ramus, S. J., Rezende, L. F., Shaw, P. A., Slavin, T. P., Swisher, E. M., Takenaka, M., Bowtell, D. D., & Sherman, M. E. (2017). Traceback: a proposed framework to increase identification and genetic counseling of BRCA1 and BRCA2 mutation carriers through family-based outreach. Journal of Clinical Oncology: Official Journal of the American Society of Clinical Oncology, 35, 2329–2337.CrossRef
17.
Zacksenhaus, E., Liu, J. C., Jiang, Z., Yao, Y., Xia, L., Shrestha, M., & Ben-David, Y. (2017). Transcription factors in breast cancer—lessons from recent genomic analyses and therapeutic implications. Advances in Protein Chemistry and Structural Biology, 107, 223–273.PubMedCrossRef
18.
Pulverer, B., Sommer, A., McArthur, G. A., Eisenman, R. N., & Luscher, B. (2000). Analysis of Myc/Max/Mad network members in adipogenesis: inhibition of the proliferative burst and differentiation by ectopically expressed Mad1. Journal of Cellular Physiology, 183, 399–410.PubMedCrossRef
19.
Gomez-Cambronero, J. (2014). Phosphatidic acid, phospholipase D and tumorigenesis. Advances in Biological Regulation, 54, 197–206.PubMedCrossRef
20.
Wang, X., Xu, L., & Zheng, L. (1994). Cloning and expression of phosphatidylcholine-hydrolyzing phospholipase D from Ricinus communis L. The Journal of Biological Chemistry, 269, 20312–20317.PubMed
21.
Speranza, F., Mahankali, M., Henkels, K. M., & Gomez-Cambronero, J. (2014). The molecular basis of leukocyte adhesion involving phosphatidic acid and phospholipase D. The Journal of Biological Chemistry, 289, 28885–28897.PubMedPubMedCentralCrossRef
22.
Henkels, K. M., Boivin, G. P., Dudley, E. S., Berberich, S. J., & Gomez-Cambronero, J. (2013). Phospholipase D (PLD) drives cell invasion, tumor growth and metastasis in a human breast cancer xenograph model. Oncogene, 32, 5551–5562.PubMedPubMedCentralCrossRef
23.
Meats, J. E., Steele, L., & Bowen, J. G. (1993). Identification of phospholipase D (PLD) activity in mouse peritoneal macrophages. Agents Actions, 39 Spec No, C14–C16.PubMedCrossRef
24.
Joseph, T., Wooden, R., Bryant, A., Zhong, M., Lu, Z., & Foster, D. A. (2001). Transformation of cells overexpressing a tyrosine kinase by phospholipase D1 and D2. Biochemical and Biophysical Research Communications, 289, 1019–1024.PubMedCrossRef
25.
Park, J. B., Lee, C. S., Jang, J. H., Ghim, J., Kim, Y. J., You, S., Hwang, D., Suh, P. G., & Ryu, S. H. (2012). Phospholipase signalling networks in cancer. Nature Reviews. Cancer, 12, 782–792.PubMedCrossRef
26.
Foster, D. A., & Xu, L. (2003). Phospholipase D in cell proliferation and cancer. Molecular Cancer Research, 1, 789–800.PubMed
27.
Gomez-Cambronero, J. (2014). Phospholipase D in cell signaling: from a myriad of cell functions to cancer growth and metastasis. The Journal of Biological Chemistry, 289, 22557–22566.PubMedPubMedCentralCrossRef
28.
Knoepp, S. M., Chahal, M. S., Xie, Y., Zhang, Z., Brauner, D. J., Hallman, M. A., Robinson, S. A., Han, S., Imai, M., Tomlinson, S., & Meier, K. E. (2008). Effects of active and inactive phospholipase D2 on signal transduction, adhesion, migration, invasion, and metastasis in EL4 lymphoma cells. Molecular Pharmacology, 74, 574–584.PubMedCrossRef
29.
Fite, K., & Gomez-Cambronero, J. (2016). Down-regulation of microRNAs (MiRs) 203, 887, 3619 and 182 prevents vimentin-triggered, phospholipase D (PLD)-mediated cancer cell invasion. The Journal of Biological Chemistry, 291, 719–730.PubMedCrossRef
30.
Frondorf, K., Henkels, K. M., Frohman, M. A., & Gomez-Cambronero, J. (2010). Phosphatidic acid (PA) is a leukocyte chemoattractant that acts through S6 kinase signaling. The Journal of Biological Chemistry, 285, 15837–15847.PubMedPubMedCentralCrossRef
31.
Mahankali, M., Peng, H. J., Cox, D., & Gomez-Cambronero, J. (2011). The mechanism of cell membrane ruffling relies on a phospholipase D2 (PLD2), Grb2 and Rac2 association. Cellular Signalling, 23, 1291–1298.PubMedPubMedCentralCrossRef
32.
Hatton, N., Lintz, E., Mahankali, M., Henkels, K. M., & Gomez-Cambronero, J. (2015). Phosphatidic acid increases epidermal growth factor receptor expression by stabilizing mRNA decay and by inhibiting lysosomal and proteasomal degradation of the internalized receptor. Molecular and Cellular Biology, 35, 3131–3144.PubMedPubMedCentral
33.
Mahankali, M., Farkaly, T., Bedi, S., Hostetler, H. A., & Gomez-Cambronero, J. (2015). Phosphatidic acid (PA) can displace PPARalpha/LXRalpha binding to the EGFR promoter causing its transrepression in luminal cancer cells. Scientific Reports, 5, 15379.PubMedPubMedCentralCrossRef
34.
Henkels, K., Taylor, T. E., Ganesan, R., Wilkins, B. A., Fite, K., & Gomez-Cambronero, J. (2016). A phosphatidic acid (PA) conveyor system of continuous intracellular transport from cell membrane to nucleus maintains EGF receptor homeostasis. Oncotarget Accepted, in press.
35.
Mahankali, M., Henkels, K. M., Speranza, F., & Gomez-Cambronero, J. (2015). A non-mitotic role for aurora kinase A as a direct activator of cell migration upon interaction with PLD, FAK and Src. Journal of Cell Science, 128, 516–526.PubMedPubMedCentralCrossRef
36.
Lee, C. S., Bae, Y. S., Lee, S. D., Suh, P. G., & Ryu, S. H. (2001). ATP-induced mitogenesis is modulated by phospholipase D2 through extracellular signal regulated protein kinase dephosphorylation in rat pheochromocytoma PC12 cells. Neuroscience Letters, 313, 117–120.PubMedCrossRef
37.
Kang, D. W., Lee, J. Y., Oh, D. H., Park, S. Y., Woo, T. M., Kim, M. K., Park, M. H., Jang, Y. H., & Min do, S. (2009). Triptolide-induced suppression of phospholipase D expression inhibits proliferation of MDA-MB-231 breast cancer cells. Experimental & Molecular Medicine, 41, 678–685.CrossRef
38.
Min, D. S., Kwon, T. K., Park, W. S., Chang, J. S., Park, S. K., Ahn, B. H., Ryoo, Z. Y., Lee, Y. H., Lee, Y. S., Rhie, D. J., Yoon, S. H., Hahn, S. J., Kim, M. S., & Jo, Y. H. (2001). Neoplastic transformation and tumorigenesis associated with overexpression of phospholipase D isozymes in cultured murine fibroblasts. Carcinogenesis, 22, 1641–1647.PubMedCrossRef
39.
Burkhardt, U., Beyer, S., & Klein, J. (2015). Role of phospholipases D1 and 2 in astroglial proliferation: effects of specific inhibitors and genetic deletion. European Journal of Pharmacology, 761, 398–404.PubMedCrossRef
40.
Burkhardt, U., Wojcik, B., Zimmermann, M., & Klein, J. (2013). Phospholipase D is a target for inhibition of astroglial proliferation by ethanol. Neuropharmacology, 79C, 1–9.
41.
Chen, Q., Hongu, T., Sato, T., Zhang, Y., Ali, W., Cavallo, J. A., van der Velden, A., Tian, H., Di Paolo, G., Nieswandt, B., Kanaho, Y., & Frohman, M. A. (2012). Key roles for the lipid signaling enzyme phospholipase d1 in the tumor microenvironment during tumor angiogenesis and metastasis. Science Signaling, 5, ra79.PubMedPubMedCentral
42.
Kantonen, S., Hatton, N., Mahankali, M., Henkels, K. M., Park, H., Cox, D., & Gomez-Cambronero, J. (2011). A novel phospholipase D2-Grb2-WASp heterotrimer regulates leukocyte phagocytosis in a two-step mechanism. Molecular and Cellular Biology, 31, 4524–4537.PubMedPubMedCentralCrossRef
43.
Knapek, K., Frondorf, K., Post, J., Short, S., Cox, D., & Gomez-Cambronero, J. (2010). The molecular basis of phospholipase D2-induced chemotaxis: elucidation of differential pathways in macrophages and fibroblasts. Molecular and Cellular Biology, 30, 4492–4506.PubMedPubMedCentralCrossRef
44.
Yamada, Y., Hamajima, N., Kato, T., Iwata, H., Yamamura, Y., Shinoda, M., Suyama, M., Mitsudomi, T., Tajima, K., Kusakabe, S., Yoshida, H., Banno, Y., Akao, Y., Tanaka, M., & Nozawa, Y. (2003). Association of a polymorphism of the phospholipase D2 gene with the prevalence of colorectal cancer. Journal of Molecular Medicine, 81, 126–131.PubMedCrossRef
45.
Zhao, Y., Ehara, H., Akao, Y., Shamoto, M., Nakagawa, Y., Banno, Y., Deguchi, T., Ohishi, N., Yagi, K., & Nozawa, Y. (2000). Increased activity and intranuclear expression of phospholipase D2 in human renal cancer. Biochemical and Biophysical Research Communications, 278, 140–143.PubMedCrossRef
46.
Cho, J. H., Hong, S. K., Kim, E. Y., Park, S. Y., Park, C. H., Kim, J. M., Kwon, O. J., Kwon, S. J., Lee, K. S., & Han, J. S. (2008). Overexpression of phospholipase D suppresses taxotere-induced cell death in stomach cancer cells. Biochimica et Biophysica Acta, 1783, 912–923.PubMedCrossRef
47.
Riebeling, C., Muller, C., & Geilen, C. C. (2003). Expression and regulation of phospholipase D isoenzymes in human melanoma cells and primary melanocytes. Melanoma Research, 13, 555–562.PubMedCrossRef
48.
Chen, Y., Zheng, Y., & Foster, D. A. (2003). Phospholipase D confers rapamycin resistance in human breast cancer cells. Oncogene, 22, 3937–3942.PubMedCrossRef
49.
Noh, D. Y., Ahn, S. J., Lee, R. A., Park, I. A., Kim, J. H., Suh, P. G., Ryu, S. H., Lee, K. H., & Han, J. S. (2000). Overexpression of phospholipase D1 in human breast cancer tissues. Cancer Letters, 161, 207–214.PubMedCrossRef
50.
Sanematsu, F., Nishikimi, A., Watanabe, M., Hongu, T., Tanaka, Y., Kanaho, Y., Cote, J. F., & Fukui, Y. (2013). Phosphatidic acid-dependent recruitment and function of the Rac activator DOCK1 during dorsal ruffle formation. The Journal of Biological Chemistry.
51.
Nishikimi, A., Fukuhara, H., Su, W., Hongu, T., Takasuga, S., Mihara, H., Cao, Q., Sanematsu, F., Kanai, M., Hasegawa, H., Tanaka, Y., Shibasaki, M., Kanaho, Y., Sasaki, T., Frohman, M. A., & Fukui, Y. (2009). Sequential regulation of DOCK2 dynamics by two phospholipids during neutrophil chemotaxis. Science, 324, 384–387.PubMedPubMedCentralCrossRef
52.
Henkels, K. M., Peng, H. J., Frondorf, K., & Gomez-Cambronero, J. (2010). A comprehensive model that explains the regulation of phospholipase D2 activity by phosphorylation-dephosphorylation. Molecular and Cellular Biology, 30, 2251–2263.PubMedPubMedCentralCrossRef
53.
Henkels, K. M., Short, S., Peng, H. J., Di Fulvio, M., & Gomez-Cambronero, J. (2009). PLD2 has both enzymatic and cell proliferation-inducing capabilities, that are differentially regulated by phosphorylation and dephosphorylation. Biochemical and Biophysical Research Communications, 389, 224–228.PubMedPubMedCentralCrossRef
54.
Di Fulvio, M., Frondorf, K., & Gomez-Cambronero, J. (2008). Mutation of Y179 on phospholipase D2 (PLD2) upregulates DNA synthesis in a PI3K-and Akt-dependent manner. Cellular Signalling, 20, 176–185.PubMedCrossRef
55.
Garcia-Teijido, P., Cabal, M. L., Fernandez, I. P., & Perez, Y. F. (2016). Tumor-infiltrating lymphocytes in triple negative breast cancer: the future of immune targeting. Clinical Medicine Insights. Oncology, 10, 31–39.PubMedPubMedCentral
56.
Brady, N. J., Chuntova, P., & Schwertfeger, K. L. (2016). Macrophages: regulators of the inflammatory microenvironment during mammary gland development and breast cancer. Mediators of Inflammation, 2016, 4549676.PubMedPubMedCentralCrossRef
57.
Buchsbaum, R. J., & Oh, S. Y. (2016). Breast cancer-associated fibroblasts: where we are and where we need to go. Cancers, 8.
58.
59.
60.
Lewis, C. E., Leek, R., Harris, A., & McGee, J. O. (1995). Cytokine regulation of angiogenesis in breast cancer: the role of tumor-associated macrophages. Journal of Leukocyte Biology, 57, 747–751.PubMedCrossRef
61.
Bingle, L., Brown, N. J., & Lewis, C. E. (2002). The role of tumour-associated macrophages in tumour progression: implications for new anticancer therapies. The Journal of Pathology, 196, 254–265.PubMedCrossRef
62.
DeNardo, D. G., Brennan, D. J., Rexhepaj, E., Ruffell, B., Shiao, S. L., Madden, S. F., Gallagher, W. M., Wadhwani, N., Keil, S. D., Junaid, S. A., Rugo, H. S., Hwang, E. S., Jirstrom, K., West, B. L., & Coussens, L. M. (2011). Leukocyte complexity predicts breast cancer survival and functionally regulates response to chemotherapy. Cancer Discovery, 1, 54–67.PubMedPubMedCentralCrossRef
63.
Beck, A. H., Espinosa, I., Edris, B., Li, R., Montgomery, K., Zhu, S., Varma, S., Marinelli, R. J., van de Rijn, M., & West, R. B. (2009). The macrophage colony-stimulating factor 1 response signature in breast carcinoma. Clinical Cancer Research: an Official Journal of the American Association for Cancer Research, 15, 778–787.CrossRef
64.
Campbell, M. J., Tonlaar, N. Y., Garwood, E. R., Huo, D., Moore, D. H., Khramtsov, A. I., Au, A., Baehner, F., Chen, Y., Malaka, D. O., Lin, A., Adeyanju, O. O., Li, S., Gong, C., McGrath, M., Olopade, O. I., & Esserman, L. J. (2011). Proliferating macrophages associated with high grade, hormone receptor negative breast cancer and poor clinical outcome. Breast Cancer Research and Treatment, 128, 703–711.PubMedCrossRef
65.
Sharma, M., Beck, A. H., Webster, J. A., Espinosa, I., Montgomery, K., Varma, S., van de Rijn, M., Jensen, K. C., & West, R. B. (2010). Analysis of stromal signatures in the tumor microenvironment of ductal carcinoma in situ. Breast Cancer Research and Treatment, 123, 397–404.PubMedCrossRef
66.
Condeelis, J., & Pollard, J. W. (2006). Macrophages: obligate partners for tumor cell migration, invasion, and metastasis. Cell, 124, 263–266.PubMedCrossRef
67.
De Palma, M., & Lewis, C. E. (2013). Macrophage regulation of tumor responses to anticancer therapies. Cancer Cell, 23, 277–286.PubMedCrossRef
68.
69.
Lin, E. Y., & Pollard, J. W. (2007). Tumor-associated macrophages press the angiogenic switch in breast cancer. Cancer Research, 67, 5064–5066.PubMedCrossRef
70.
Lin, E. Y., Li, J. F., Bricard, G., Wang, W., Deng, Y., Sellers, R., Porcelli, S. A., & Pollard, J. W. (2007). Vascular endothelial growth factor restores delayed tumor progression in tumors depleted of macrophages. Molecular Oncology, 1, 288–302.PubMedPubMedCentralCrossRef
71.
DeNardo, D. G., Barreto, J. B., Andreu, P., Vasquez, L., Tawfik, D., Kolhatkar, N., & Coussens, L. M. (2009). CD4(+) T cells regulate pulmonary metastasis of mammary carcinomas by enhancing protumor properties of macrophages. Cancer Cell, 16, 91–102.PubMedPubMedCentralCrossRef
72.
Wyckoff, J., Wang, W., Lin, E. Y., Wang, Y., Pixley, F., Stanley, E. R., Graf, T., Pollard, J. W., Segall, J., & Condeelis, J. (2004). A paracrine loop between tumor cells and macrophages is required for tumor cell migration in mammary tumors. Cancer Research, 64, 7022–7029.PubMedCrossRef
73.
Su, S., Liu, Q., Chen, J., Chen, J., Chen, F., He, C., Huang, D., Wu, W., Lin, L., Huang, W., Zhang, J., Cui, X., Zheng, F., Li, H., Yao, H., Su, F., & Song, E. (2014). A positive feedback loop between mesenchymal-like cancer cells and macrophages is essential to breast cancer metastasis. Cancer Cell, 25, 605–620.PubMedCrossRef
74.
Ojalvo, L. S., Whittaker, C. A., Condeelis, J. S., & Pollard, J. W. (2010). Gene expression analysis of macrophages that facilitate tumor invasion supports a role for Wnt-signaling in mediating their activity in primary mammary tumors. Journal of Immunology, 184, 702–712.CrossRef
75.
Yang, M., Chen, J., Su, F., Yu, B., Su, F., Lin, L., Liu, Y., Huang, J. D., & Song, E. (2011). Microvesicles secreted by macrophages shuttle invasion-potentiating microRNAs into breast cancer cells. Molecular Cancer, 10, 117.PubMedPubMedCentralCrossRef
76.
77.
Qian, B. Z., Li, J., Zhang, H., Kitamura, T., Zhang, J., Campion, L. R., Kaiser, E. A., Snyder, L. A., & Pollard, J. W. (2011). CCL2 recruits inflammatory monocytes to facilitate breast-tumour metastasis. Nature, 475, 222–225.PubMedPubMedCentralCrossRef
78.
Qian, B., Deng, Y., Im, J. H., Muschel, R. J., Zou, Y., Li, J., Lang, R. A., & Pollard, J. W. (2009). A distinct macrophage population mediates metastatic breast cancer cell extravasation, establishment and growth. PLoS One, 4, e6562.PubMedPubMedCentralCrossRef
79.
Gratchev, A., Kzhyshkowska, J., Kannookadan, S., Ochsenreiter, M., Popova, A., Yu, X., Mamidi, S., Stonehouse-Usselmann, E., Muller-Molinet, I., Gooi, L., & Goerdt, S. (2008). Activation of a TGF-beta-specific multistep gene expression program in mature macrophages requires glucocorticoid-mediated surface expression of TGF-beta receptor II. Journal of Immunology, 180, 6553–6565.CrossRef
80.
Hu, X., Chung, A. Y., Wu, I., Foldi, J., Chen, J., Ji, J. D., Tateya, T., Kang, Y. J., Han, J., Gessler, M., Kageyama, R., & Ivashkiv, L. B. (2008). Integrated regulation of Toll-like receptor responses by Notch and interferon-gamma pathways. Immunity, 29, 691–703.PubMedPubMedCentralCrossRef
81.
Ravasi, T., Wells, C., Forest, A., Underhill, D. M., Wainwright, B. J., Aderem, A., Grimmond, S., & Hume, D. A. (2002). Generation of diversity in the innate immune system: macrophage heterogeneity arises from gene-autonomous transcriptional probability of individual inducible genes. Journal of Immunology, 168, 44–50.CrossRef
82.
Riches, D. W. (1995). Signalling heterogeneity as a contributing factor in macrophage functional diversity. Seminars in Cell Biology, 6, 377–384.PubMedCrossRef
83.
Stout, R. D., Jiang, C., Matta, B., Tietzel, I., Watkins, S. K., & Suttles, J. (2005). Macrophages sequentially change their functional phenotype in response to changes in microenvironmental influences. Journal of Immunology, 175, 342–349.CrossRef
84.
Shaul, M. E., Bennett, G., Strissel, K. J., Greenberg, A. S., & Obin, M. S. (2010). Dynamic, M2-like remodeling phenotypes of CD11c+ adipose tissue macrophages during high-fat diet-induced obesity in mice. Diabetes, 59, 1171–1181.PubMedPubMedCentralCrossRef
85.
Xue, J., Schmidt, S. V., Sander, J., Draffehn, A., Krebs, W., Quester, I., De Nardo, D., Gohel, T. D., Emde, M., Schmidleithner, L., Ganesan, H., Nino-Castro, A., Mallmann, M. R., Labzin, L., Theis, H., Kraut, M., Beyer, M., Latz, E., Freeman, T. C., Ulas, T., & Schultze, J. L. (2014). Transcriptome-based network analysis reveals a spectrum model of human macrophage activation. Immunity, 40, 274–288.PubMedPubMedCentralCrossRef
86.
Pucci, F., Venneri, M. A., Biziato, D., Nonis, A., Moi, D., Sica, A., Di Serio, C., Naldini, L., & De Palma, M. (2009). A distinguishing gene signature shared by tumor-infiltrating Tie2-expressing monocytes, blood “resident” monocytes, and embryonic macrophages suggests common functions and developmental relationships. Blood, 114, 901–914.PubMedCrossRef
87.
Sica, A., & Bronte, V. (2007). Altered macrophage differentiation and immune dysfunction in tumor development. The Journal of Clinical Investigation, 117, 1155–1166.PubMedPubMedCentralCrossRef
88.
Biswas, S. K., Gangi, L., Paul, S., Schioppa, T., Saccani, A., Sironi, M., Bottazzi, B., Doni, A., Vincenzo, B., Pasqualini, F., Vago, L., Nebuloni, M., Mantovani, A., & Sica, A. (2006). A distinct and unique transcriptional program expressed by tumor-associated macrophages (defective NF-kappaB and enhanced IRF-3/STAT1 activation). Blood, 107, 2112–2122.PubMedCrossRef
89.
Hagemann, T., Lawrence, T., McNeish, I., Charles, K. A., Kulbe, H., Thompson, R. G., Robinson, S. C., & Balkwill, F. R. (2008). “Re-educating” tumor-associated macrophages by targeting NF-kappaB. The Journal of Experimental Medicine, 205, 1261–1268.PubMedPubMedCentralCrossRef
90.
Sierra, J. R., Corso, S., Caione, L., Cepero, V., Conrotto, P., Cignetti, A., Piacibello, W., Kumanogoh, A., Kikutani, H., Comoglio, P. M., Tamagnone, L., & Giordano, S. (2008). Tumor angiogenesis and progression are enhanced by Sema4D produced by tumor-associated macrophages. The Journal of Experimental Medicine, 205, 1673–1685.PubMedPubMedCentralCrossRef
91.
Torroella-Kouri, M., Silvera, R., Rodriguez, D., Caso, R., Shatry, A., Opiela, S., Ilkovitch, D., Schwendener, R. A., Iragavarapu-Charyulu, V., Cardentey, Y., Strbo, N., & Lopez, D. M. (2009). Identification of a subpopulation of macrophages in mammary tumor-bearing mice that are neither M1 nor M2 and are less differentiated. Cancer Research, 69, 4800–4809.PubMedCrossRef
92.
Lewis, C. E., & Pollard, J. W. (2006). Distinct role of macrophages in different tumor microenvironments. Cancer Research, 66, 605–612.PubMedCrossRef
93.
Ruffell, B., Affara, N. I., & Coussens, L. M. (2012). Differential macrophage programming in the tumor microenvironment. Trends in Immunology, 33, 119–126.PubMedPubMedCentralCrossRef
94.
Van Overmeire, E., Laoui, D., Keirsse, J., Van Ginderachter, J. A., & Sarukhan, A. (2014). Mechanisms driving macrophage diversity and specialization in distinct tumor microenvironments and parallelisms with other tissues. Frontiers in Immunology, 5, 127.PubMedPubMedCentral
95.
Egeblad, M., Ewald, A. J., Askautrud, H. A., Truitt, M. L., Welm, B. E., Bainbridge, E., Peeters, G., Krummel, M. F., & Werb, Z. (2008). Visualizing stromal cell dynamics in different tumor microenvironments by spinning disk confocal microscopy. Disease Models & Mechanisms, 1, 155–167 discussion 165.CrossRef
96.
Huang, Y., Yuan, J., Righi, E., Kamoun, W. S., Ancukiewicz, M., Nezivar, J., Santosuosso, M., Martin, J. D., Martin, M. R., Vianello, F., Leblanc, P., Munn, L. L., Huang, P., Duda, D. G., Fukumura, D., Jain, R. K., & Poznansky, M. C. (2012). Vascular normalizing doses of antiangiogenic treatment reprogram the immunosuppressive tumor microenvironment and enhance immunotherapy. Proceedings of the National Academy of Sciences of the United States of America, 109, 17561–17566.PubMedPubMedCentralCrossRef
97.
Franklin, R. A., Liao, W., Sarkar, A., Kim, M. V., Bivona, M. R., Liu, K., Pamer, E. G., & Li, M. O. (2014). The cellular and molecular origin of tumor-associated macrophages. Science, 344, 921–925.PubMedPubMedCentralCrossRef
98.
Hagemann, T., Wilson, J., Burke, F., Kulbe, H., Li, N. F., Pluddemann, A., Charles, K., Gordon, S., & Balkwill, F. R. (2006). Ovarian cancer cells polarize macrophages toward a tumor-associated phenotype. Journal of Immunology, 176, 5023–5032.CrossRef
99.
Mantovani, A., Allavena, P., Sica, A., & Balkwill, F. (2008). Cancer-related inflammation. Nature, 454, 436–444.PubMedCrossRef
100.
Roca, H., Varsos, Z. S., Sud, S., Craig, M. J., Ying, C., & Pienta, K. J. (2009). CCL2 and interleukin-6 promote survival of human CD11b+ peripheral blood mononuclear cells and induce M2-type macrophage polarization. The Journal of Biological Chemistry, 284, 34342–34354.PubMedPubMedCentralCrossRef
101.
Hsu, D. S., Wang, H. J., Tai, S. K., Chou, C. H., Hsieh, C. H., Chiu, P. H., Chen, N. J., & Yang, M. H. (2014). Acetylation of snail modulates the cytokinome of cancer cells to enhance the recruitment of macrophages. Cancer Cell, 26, 534–548.PubMedCrossRef
102.
Sinha, P., Clements, V. K., Bunt, S. K., Albelda, S. M., & Ostrand-Rosenberg, S. (2007). Cross-talk between myeloid-derived suppressor cells and macrophages subverts tumor immunity toward a type 2 response. Journal of Immunology, 179, 977–983.CrossRef
103.
Movahedi, K., Laoui, D., Gysemans, C., Baeten, M., Stange, G., Van den Bossche, J., Mack, M., Pipeleers, D., In't Veld, P., De Baetselier, P., & Van Ginderachter, J. A. (2010). Different tumor microenvironments contain functionally distinct subsets of macrophages derived from Ly6C(high) monocytes. Cancer Research, 70, 5728–5739.PubMedCrossRef
104.
Murdoch, C., Giannoudis, A., & Lewis, C. E. (2004). Mechanisms regulating the recruitment of macrophages into hypoxic areas of tumors and other ischemic tissues. Blood, 104, 2224–2234.PubMedCrossRef
105.
Obeid, E., Nanda, R., Fu, Y. X., & Olopade, O. I. (2013). The role of tumor-associated macrophages in breast cancer progression (review). International Journal of Oncology, 43, 5–12.PubMedPubMedCentralCrossRef
106.
Pyonteck, S. M., Akkari, L., Schuhmacher, A. J., Bowman, R. L., Sevenich, L., Quail, D. F., Olson, O. C., Quick, M. L., Huse, J. T., Teijeiro, V., Setty, M., Leslie, C. S., Oei, Y., Pedraza, A., Zhang, J., Brennan, C. W., Sutton, J. C., Holland, E. C., Daniel, D., & Joyce, J. A. (2013). CSF-1R inhibition alters macrophage polarization and blocks glioma progression. Nature Medicine, 19, 1264–1272.PubMedPubMedCentralCrossRef
107.
108.
Galdiero, M. R., Bonavita, E., Barajon, I., Garlanda, C., Mantovani, A., & Jaillon, S. (2013). Tumor associated macrophages and neutrophils in cancer. Immunobiology, 218, 1402–1410.PubMedCrossRef
109.
Allavena, P., Sica, A., Solinas, G., Porta, C., & Mantovani, A. (2008). The inflammatory micro-environment in tumor progression: the role of tumor-associated macrophages. Critical Reviews in Oncology/Hematology, 66, 1–9.PubMedCrossRef
110.
Laoui, D., Movahedi, K., Van Overmeire, E., Van den Bossche, J., Schouppe, E., Mommer, C., Nikolaou, A., Morias, Y., De Baetselier, P., & Van Ginderachter, J. A. (2011). Tumor-associated macrophages in breast cancer: distinct subsets, distinct functions. The International Journal of Developmental Biology, 55, 861–867.PubMedCrossRef
111.
Achyut, B. R., & Arbab, A. S. (2016). Myeloid cell signatures in tumor microenvironment predicts therapeutic response in cancer. OncoTargets and Therapy, 9, 1047–1055.PubMedPubMedCentral
112.
Italiani, P., & Boraschi, D. (2014). From monocytes to M1/M2 macrophages: phenotypical vs. functional differentiation. Frontiers in Immunology, 5, 514.PubMedPubMedCentralCrossRef
113.
Mukhtar, R. A., Nseyo, O., Campbell, M. J., & Esserman, L. J. (2011). Tumor-associated macrophages in breast cancer as potential biomarkers for new treatments and diagnostics. Expert Review of Molecular Diagnostics, 11, 91–100.PubMedCrossRef
114.
Gregory, A. D., & Houghton, A. M. (2011). Tumor-associated neutrophils: new targets for cancer therapy. Cancer Research, 71, 2411–2416.PubMedCrossRef
115.
De Larco, J. E., Wuertz, B. R., & Furcht, L. T. (2004). The potential role of neutrophils in promoting the metastatic phenotype of tumors releasing interleukin-8. Clinical Cancer Research : an Official Journal of the American Association for Cancer Research, 10, 4895–4900.CrossRef
116.
De Larco, J. E., Wuertz, B. R., Yee, D., Rickert, B. L., & Furcht, L. T. (2003). Atypical methylation of the interleukin-8 gene correlates strongly with the metastatic potential of breast carcinoma cells. Proceedings of the National Academy of Sciences of the United States of America, 100, 13988–13993.PubMedPubMedCentralCrossRef
117.
Sparmann, A., & Bar-Sagi, D. (2004). Ras-induced interleukin-8 expression plays a critical role in tumor growth and angiogenesis. Cancer Cell, 6, 447–458.PubMedCrossRef
118.
Mantovani, A., Sozzani, S., Locati, M., Allavena, P., & Sica, A. (2002). Macrophage polarization: tumor-associated macrophages as a paradigm for polarized M2 mononuclear phagocytes. Trends in Immunology, 23, 549–555.PubMedCrossRef
119.
Leek, R. D., Lewis, C. E., Whitehouse, R., Greenall, M., Clarke, J., & Harris, A. L. (1996). Association of macrophage infiltration with angiogenesis and prognosis in invasive breast carcinoma. Cancer Research, 56, 4625–4629.PubMed
120.
Bingle, L., Lewis, C. E., Corke, K. P., Reed, M. W., & Brown, N. J. (2006). Macrophages promote angiogenesis in human breast tumour spheroids in vivo. British Journal of Cancer, 94, 101–107.PubMedPubMedCentralCrossRef
121.
Balkwill, F. R., Capasso, M., & Hagemann, T. (2012). The tumor microenvironment at a glance. Journal of Cell Science, 125, 5591–5596.PubMedCrossRef
122.
Pekarek, L. A., Starr, B. A., Toledano, A. Y., & Schreiber, H. (1995). Inhibition of tumor growth by elimination of granulocytes. The Journal of Experimental Medicine, 181, 435–440.PubMedCrossRef
123.
Nozawa, H., Chiu, C., & Hanahan, D. (2006). Infiltrating neutrophils mediate the initial angiogenic switch in a mouse model of multistage carcinogenesis. Proceedings of the National Academy of Sciences of the United States of America, 103, 12493–12498.PubMedPubMedCentralCrossRef
124.
Fritz, J. M., Tennis, M. A., Orlicky, D. J., Lin, H., Ju, C., Redente, E. F., Choo, K. S., Staab, T. A., Bouchard, R. J., Merrick, D. T., Malkinson, A. M., & Dwyer-Nield, L. D. (2014). Depletion of tumor-associated macrophages slows the growth of chemically induced mouse lung adenocarcinomas. Frontiers in Immunology, 5, 587.PubMedPubMedCentralCrossRef
125.
Hanahan, D., & Weinberg, R. A. (2011). Hallmarks of cancer: the next generation. Cell, 144, 646–674.PubMedCrossRef
126.
Mantovani, A. (2011). B cells and macrophages in cancer: yin and yang. Nature Medicine, 17, 285–286.PubMedCrossRef
127.
Gallego-Ortega, D., Ledger, A., Roden, D. L., Law, A. M., Magenau, A., Kikhtyak, Z., Cho, C., Allerdice, S. L., Lee, H. J., Valdes-Mora, F., Herrmann, D., Salomon, R., Young, A. I., Lee, B. Y., Sergio, C. M., Kaplan, W., Piggin, C., Conway, J. R., Rabinovich, B., Millar, E. K., Oakes, S. R., Chtanova, T., Swarbrick, A., Naylor, M. J., O'Toole, S., Green, A. R., Timpson, P., Gee, J. M., Ellis, I. O., Clark, S. J., & Ormandy, C. J. (2015). ELF5 drives lung metastasis in luminal breast cancer through recruitment of Gr1+ CD11b+ myeloid-derived suppressor cells. PLoS Biology, 13, e1002330.PubMedPubMedCentralCrossRef
128.
Coffelt, S. B., Kersten, K., Doornebal, C. W., Weiden, J., Vrijland, K., Hau, C. S., Verstegen, N. J., Ciampricotti, M., Hawinkels, L. J., Jonkers, J., & de Visser, K. E. (2015). IL-17-producing gammadelta T cells and neutrophils conspire to promote breast cancer metastasis. Nature, 522, 345–348.PubMedPubMedCentralCrossRef
129.
Garcia-Mendoza, M. G., Inman, D. R., Ponik, S. M., Jeffery, J. J., Sheerar, D. S., Van Doorn, R. R., & Keely, P. J. (2016). Neutrophils drive accelerated tumor progression in the collagen-dense mammary tumor microenvironment. Breast Cancer Research: BCR, 18, 49.PubMedCrossRef
130.
Tabaries, S., Ouellet, V., Hsu, B. E., Annis, M. G., Rose, A. A., Meunier, L., Carmona, E., Tam, C. E., Mes-Masson, A. M., & Siegel, P. M. (2015). Granulocytic immune infiltrates are essential for the efficient formation of breast cancer liver metastases. Breast Cancer Research: BCR, 17, 45.PubMedCrossRef
131.
Marini, O., Spina, C., Mimiola, E., Cassaro, A., Malerba, G., Todeschini, G., Perbellini, O., Scupoli, M., Carli, G., Facchinelli, D., Cassatella, M., Scapini, P., & Tecchio, C. (2016). Identification of granulocytic myeloid-derived suppressor cells (G-MDSCs) in the peripheral blood of Hodgkin and non-Hodgkin lymphoma patients. Oncotarget.
132.
Cavallo, F., Giovarelli, M., Gulino, A., Vacca, A., Stoppacciaro, A., Modesti, A., & Forni, G. (1992). Role of neutrophils and CD4+ T lymphocytes in the primary and memory response to nonimmunogenic murine mammary adenocarcinoma made immunogenic by IL-2 gene. Journal of Immunology, 149, 3627–3635.
133.
Musiani, P., Allione, A., Modica, A., Lollini, P. L., Giovarelli, M., Cavallo, F., Belardelli, F., Forni, G., & Modesti, A. (1996). Role of neutrophils and lymphocytes in inhibition of a mouse mammary adenocarcinoma engineered to release IL-2, IL-4, IL-7, IL-10, IFN-alpha, IFN-gamma, and TNF-alpha. Laboratory Investigation: a Journal of Technical Methods and Pathology, 74, 146–157.
134.
Colombo, M. P., & Trinchieri, G. (2002). Interleukin-12 in anti-tumor immunity and immunotherapy. Cytokine & Growth Factor Reviews, 13, 155–168.CrossRef
135.
Gajewski, T. F., Louahed, J., & Brichard, V. G. (2010). Gene signature in melanoma associated with clinical activity: a potential clue to unlock cancer immunotherapy. Cancer Journal, 16, 399–403.CrossRef
136.
Hadden, J. W. (1999). The immunology and immunotherapy of breast cancer: an update. International Journal of Immunopharmacology, 21, 79–101.PubMedCrossRef
137.
Queen, M. M., Ryan, R. E., Holzer, R. G., Keller-Peck, C. R., & Jorcyk, C. L. (2005). Breast cancer cells stimulate neutrophils to produce oncostatin M: potential implications for tumor progression. Cancer Research, 65, 8896–8904.PubMedCrossRef
138.
Di Carlo, E., Rovero, S., Boggio, K., Quaglino, E., Amici, A., Smorlesi, A., Forni, G., & Musiani, P. (2001). Inhibition of mammary carcinogenesis by systemic interleukin 12 or p185neu DNA vaccination in Her-2/neu transgenic BALB/c mice. Clinical Cancer Research: an Official Journal of the American Association for Cancer Research, 7, 830s–837s.
139.
Rimando, J., Campbell, J., Kim, J. H., Tang, S. C., & Kim, S. (2016). The pretreatment neutrophil/lymphocyte ratio is associated with all-cause mortality in black and white patients with non-metastatic breast cancer. Frontiers in Oncology, 6, 81.PubMedPubMedCentralCrossRef
140.
Benito-Martin, A., Di Giannatale, A., Ceder, S., & Peinado, H. (2015). The new deal: a potential role for secreted vesicles in innate immunity and tumor progression. Frontiers in Immunology, 6, 66.PubMedPubMedCentralCrossRef
141.
Fite, K., Elkhadragy, L., & Gomez-Cambronero, J. (2016). A repertoire of microRNAs regulates cancer cell starvation by targeting phospholipase D in a feedback loop that operates maximally in cancer cells. Molecular and Cellular Biology, 36, 1078–1089.PubMedPubMedCentralCrossRef
142.
Foster, D. A. (2004). Targeting mTOR-mediated survival signals in anticancer therapeutic strategies. Expert Review of Anticancer Therapy, 4, 691–701.PubMedCrossRef
143.
Rodrik, V., Zheng, Y., Harrow, F., Chen, Y., & Foster, D. A. (2005). Survival signals generated by estrogen and phospholipase D in MCF-7 breast cancer cells are dependent on Myc. Molecular and Cellular Biology, 25, 7917–7925.PubMedPubMedCentralCrossRef
144.
Mathivanan, S., Ji, H., & Simpson, R. J. (2010). Exosomes: extracellular organelles important in intercellular communication. Journal of Proteomics, 73, 1907–1920.PubMedCrossRef
145.
Nilsson, J., Skog, J., Nordstrand, A., Baranov, V., Mincheva-Nilsson, L., Breakefield, X. O., & Widmark, A. (2009). Prostate cancer-derived urine exosomes: a novel approach to biomarkers for prostate cancer. British Journal of Cancer, 100, 1603–1607.PubMedPubMedCentralCrossRef
146.
Kvistborg, P., & Yewdell, J. W. (2018). Enhancing responses to cancer immunotherapy. Science, 359, 516–517.PubMedCrossRef
147.
Wolchok, J. D., Rollin, L., & Larkin, J. (2017). Nivolumab and ipilimumab in advanced melanoma. The New England Journal of Medicine, 377, 2503–2504.PubMedCrossRef
148.
Chowell, D., Morris, L. G., Grigg, C. M., Weber, J. K., Samstein, R. M., Makarov, V., Kuo, F., Kendall, S. M., Requena, D., & Riaz, N. (2018). Patient HLA class I genotype influences cancer response to checkpoint blockade immunotherapy. Science, 359, 582–587.PubMedCrossRef
149.
Robinson, J., Guethlein, L. A., Cereb, N., Yang, S. Y., Norman, P. J., Marsh, S. G., & Parham, P. (2017). Distinguishing functional polymorphism from random variation in the sequences of > 10,000 HLA-A,-B and-C alleles. PLoS Genetics, 13, e1006862.PubMedPubMedCentralCrossRef
150.
Schumacher, T. N., & Schreiber, R. D. (2015). Neoantigens in cancer immunotherapy. Science, 348, 69–74.PubMedCrossRef
151.
Villarroya-Beltri, C., Baixauli, F., Gutierrez-Vazquez, C., Sanchez-Madrid, F., & Mittelbrunn, M. (2014). Sorting it out: regulation of exosome loading. Seminars in Cancer Biology, 28, 3–13.PubMedPubMedCentralCrossRef
152.
Saenz-Cuesta, M., Mittelbrunn, M., & Otaegui, D. (2015). Editorial: Novel clinical applications of extracellular vesicles. Frontiers in Immunology, 6, 381.PubMedPubMedCentral
153.
Mittelbrunn, M., & Sanchez-Madrid, F. (2012). Intercellular communication: diverse structures for exchange of genetic information. Nature Reviews. Molecular Cell Biology, 13, 328–335.PubMedPubMedCentralCrossRef
154.
Liu, F., Lang, R., Zhao, J., Zhang, X., Pringle, G. A., Fan, Y., Yin, D., Gu, F., Yao, Z., & Fu, L. (2011). CD8(+) cytotoxic T cell and FOXP3(+) regulatory T cell infiltration in relation to breast cancer survival and molecular subtypes. Breast Cancer Research and Treatment, 130, 645–655.PubMedCrossRef
155.
Fatima, F., & Nawaz, M. (2015). Stem cell-derived exosomes: roles in stromal remodeling, tumor progression, and cancer immunotherapy. Chinese Journal of Cancer, 34, 541–553.PubMedCrossRef
156.
Zhang, X., Yuan, X., Shi, H., Wu, L., Qian, H., & Xu, W. (2015). Exosomes in cancer: small particle, big player. Journal of Hematology & Oncology, 8, 83.CrossRef
157.
Ko, J., Carpenter, E., & Issadore, D. (2016). Detection and isolation of circulating exosomes and microvesicles for cancer monitoring and diagnostics using micro-/nano-based devices. The Analyst, 141, 450–460.PubMedPubMedCentralCrossRef
158.
Balaj, L., Lessard, R., Dai, L., Cho, Y. J., Pomeroy, S. L., Breakefield, X. O., & Skog, J. (2011). Tumour microvesicles contain retrotransposon elements and amplified oncogene sequences. Nature Communications, 2, 180.PubMedPubMedCentralCrossRef
159.
Zhou, W., Fong, M. Y., Min, Y., Somlo, G., Liu, L., Palomares, M. R., Yu, Y., Chow, A., O’Connor, S. T., Chin, A. R., Yen, Y., Wang, Y., Marcusson, E. G., Chu, P., Wu, J., Wu, X., Li, A. X., Li, Z., Gao, H., Ren, X., Boldin, M. P., Lin, P. C., & Wang, S. E. (2014). Cancer-secreted miR-105 destroys vascular endothelial barriers to promote metastasis. Cancer Cell, 25, 501–515.PubMedPubMedCentralCrossRef
160.
Melo, S. A., Sugimoto, H., O'Connell, J. T., Kato, N., Villanueva, A., Vidal, A., Qiu, L., Vitkin, E., Perelman, L. T., Melo, C. A., Lucci, A., Ivan, C., Calin, G. A., & Kalluri, R. (2014). Cancer exosomes perform cell-independent microRNA biogenesis and promote tumorigenesis. Cancer Cell, 26, 707–721.PubMedPubMedCentralCrossRef
161.
Skog, J., Wurdinger, T., van Rijn, S., Meijer, D. H., Gainche, L., Sena-Esteves, M., Curry Jr., W. T., Carter, B. S., Krichevsky, A. M., & Breakefield, X. O. (2008). Glioblastoma microvesicles transport RNA and proteins that promote tumour growth and provide diagnostic biomarkers. Nature Cell Biology, 10, 1470–1476.PubMedPubMedCentralCrossRef
162.
Grange, C., Tapparo, M., Collino, F., Vitillo, L., Damasco, C., Deregibus, M. C., Tetta, C., Bussolati, B., & Camussi, G. (2011). Microvesicles released from human renal cancer stem cells stimulate angiogenesis and formation of lung premetastatic niche. Cancer Research, 71, 5346–5356.PubMedCrossRef
163.
Ghossoub, R., Lembo, F., Rubio, A., Gaillard, C. B., Bouchet, J., Vitale, N., Slavík, J., Machala, M., & Zimmermann, P. (2014). Syntenin-ALIX exosome biogenesis and budding into multivesicular bodies are controlled by ARF6 and PLD2. Nature Communications, 5, 3477.PubMedCrossRef
164.
Laulagnier, K., Grand, D., Dujardin, A., Hamdi, S., Vincent-Schneider, H., Lankar, D., Salles, J.-P., Bonnerot, C., Perret, B., & Record, M. (2004). PLD2 is enriched on exosomes and its activity is correlated to the release of exosomes. FEBS Letters, 572, 11–14.PubMedCrossRef
165.
Muralidharan-Chari, V., Clancy, J., Plou, C., Romao, M., Chavrier, P., Raposo, G., & D’Souza-Schorey, C. (2009). ARF6-regulated shedding of tumor cell-derived plasma membrane microvesicles. Current Biology: CB, 19, 1875–1885.PubMedCrossRef
166.
Clayton, A., Mitchell, J. P., Court, J., Mason, M. D., & Tabi, Z. (2007). Human tumor-derived exosomes selectively impair lymphocyte responses to interleukin-2. Cancer Research, 67, 7458–7466.PubMedCrossRef
167.
Mrizak, D., Martin, N., Barjon, C., Jimenez-Pailhes, A. S., Mustapha, R., Niki, T., Guigay, J., Pancre, V., de Launoit, Y., Busson, P., Morales, O., & Delhem, N. (2015). Effect of nasopharyngeal carcinoma-derived exosomes on human regulatory T cells. Journal of the National Cancer Institute, 107, 363.PubMedCrossRef
168.
Ye, S. B., Li, Z. L., Luo, D. H., Huang, B. J., Chen, Y. S., Zhang, X. S., Cui, J., Zeng, Y. X., & Li, J. (2014). Tumor-derived exosomes promote tumor progression and T-cell dysfunction through the regulation of enriched exosomal microRNAs in human nasopharyngeal carcinoma. Oncotarget, 5, 5439–5452.PubMedPubMedCentralCrossRef
169.
Peinado, H., Aleckovic, M., Lavotshkin, S., Matei, I., Costa-Silva, B., Moreno-Bueno, G., Hergueta-Redondo, M., Williams, C., Garcia-Santos, G., Ghajar, C., Nitadori-Hoshino, A., Hoffman, C., Badal, K., Garcia, B. A., Callahan, M. K., Yuan, J., Martins, V. R., Skog, J., Kaplan, R. N., Brady, M. S., Wolchok, J. D., Chapman, P. B., Kang, Y., Bromberg, J., & Lyden, D. (2012). Melanoma exosomes educate bone marrow progenitor cells toward a pro-metastatic phenotype through MET. Nature Medicine, 18, 883–891.PubMedPubMedCentralCrossRef
170.
Nwabo Kamdje, A. H., Seke Etet, P. F., Vecchio, L., Tagne, R. S., Amvene, J. M., Muller, J. M., Krampera, M., & Lukong, K. E. (2014). New targeted therapies for breast cancer: a focus on tumor microenvironmental signals and chemoresistant breast cancers. World Journal of Clinical Cases, 2, 769–786.PubMedCrossRef
171.
172.
Zhang, X. M., Claerhout, S., Prat, A., Dobrolecki, L. E., Petrovic, I., Lai, Q., Landis, M. D., Wiechmann, L., Schiff, R., Giuliano, M., Wong, H. L., Fuqua, S. W., Contreras, A., Gutierrez, C., Huang, J., Mao, S. F., Pavlick, A. C., Froehlich, A. M., Wu, M. F., Tsimelzon, A., Hilsenbeck, S. G., Chen, E. S., Zuloaga, P., Shaw, C. A., Rimawi, M. F., Perou, C. M., Mills, G. B., Chang, J. C., & Lewis, M. T. (2013). A renewable tissue resource of phenotypically stable, biologically and ethnically diverse, patient-derived human breast cancer xenograft models. Cancer Research, 73, 4885–4897.PubMedPubMedCentralCrossRef
173.
Ahn, S. G., Jeong, J., Hong, S., & Jung, W. H. (2015). Current issues and clinical evidence in tumor-infiltrating lymphocytes in breast cancer. Journal of Pathology and Translational Medicine, 49, 355–363.PubMedPubMedCentralCrossRef
174.
175.
Temme, C., Simonelig, M., & Wahle, E. (2014). Deadenylation of mRNA by the CCR4-NOT complex in Drosophila: molecular and developmental aspects. Frontiers in Genetics, 5.
176.
Martinez, J., Ren, Y. G., Thuresson, A. C., Hellman, U., Astrom, J., & Virtanen, A. (2000). A 54-kDa fragment of the poly(A)-specific ribonuclease is an oligomeric, processive, and cap-interacting poly(A)-specific 3′ exonuclease. The Journal of Biological Chemistry, 275, 24222–24230.PubMedCrossRef
177.
Godwin, A. R., Kojima, S., Green, C. B., & Wilusz, J. (2013). Kiss your tail goodbye: the role of PARN, Nocturnin, and Angel deadenylases in mRNA biology. Biochimica et Biophysica Acta, 1829, 571–579.PubMedCrossRef
178.
Martinez, J., Ren, Y. G., Thuresson, A. C., Hellmann, U., Astrom, J., & Virtanen, A. (2000). A 54-kDa fragment of the poly(A)-specific ribonuclease is an oligomeric, processive, and cap-interacting poly(A)-specific 3′ exonuclease. Journal of Biological Chemistry, 275, 24222–24230.PubMedCrossRef
179.
Wilson, T., & Treisman, R. (1988). Removal of poly(A) and consequent degradation of c-fos mRNA facilitated by 3′ AU-rich sequences. Nature, 336, 396–399.PubMedCrossRef
180.
Mitchell, P., & Tollervey, D. (2000). mRNA stability in eukaryotes. Current Opinion in Genetics & Development, 10, 193–198.CrossRef
181.
Shyu, A. B., Belasco, J. G., & Greenberg, M. E. (1991). Two distinct destabilizing elements in the c-fos message trigger deadenylation as a first step in rapid mRNA decay. Genes & Development, 5, 221–231.CrossRef
182.
183.
Nousch, M., Techritz, N., Hampel, D., Millonigg, S., & Eckmann, C. R. (2013). The Ccr4-Not deadenylase complex constitutes the main poly(A) removal activity in C. elegans. Journal of Cell Science, 126, 4274–4285.PubMedCrossRef
184.
Funakoshi, Y., Doi, Y., Hosoda, N., Uchida, N., Osawa, M., Shimada, I., Tsujimoto, M., Suzuki, T., Katada, T., & Hoshino, S. (2007). Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases. Genes & Development, 21, 3135–3148.CrossRef
185.
Mazan-Mamczarz, K., Galban, S., Lopez de Silanes, I., Martindale, J. L., Atasoy, U., Keene, J. D., & Gorospe, M. (2003). RNA-binding protein HuR enhances p53 translation in response to ultraviolet light irradiation. Proceedings of the National Academy of Sciences of the United States of America, 100, 8354–8359.PubMedPubMedCentralCrossRef
186.
Jalkanen, A. L., Coleman, S. J., & Wilusz, J. (2014). Determinants and implications of mRNA poly(A) tail size—does this protein make my tail look big? Seminars in Cell & Developmental Biology, 34, 24–32.CrossRef
187.
Zhang, X., Devany, E., Murphy, M. R., Glazman, G., Persaud, M., & Kleiman, F. E. (2015). PARN deadenylase is involved in miRNA-dependent degradation of TP53 mRNA in mammalian cells. Nucleic Acids Research, 43, 10925–10938.PubMedPubMedCentralCrossRef
188.
Png, K. J., Halberg, N., Yoshida, M., & Tavazoie, S. F. (2012). A microRNA regulon that mediates endothelial recruitment and metastasis by cancer cells. Nature, 481, 190–194.CrossRef
189.
Cevher, M. A., Zhang, X., Fernandez, S., Kim, S., Baquero, J., Nilsson, P., Lee, S., Virtanen, A., & Kleiman, F. E. (2010). Nuclear deadenylation/polyadenylation factors regulate 3′ processing in response to DNA damage. The EMBO Journal, 29, 1674–1687.PubMedPubMedCentralCrossRef
190.
Devany, E., Zhang, X., Park, J. Y., Tian, B., & Kleiman, F. E. (2013). Positive and negative feedback loops in the p53 and mRNA 3′ processing pathways. Proceedings of the National Academy of Sciences of the United States of America, 110, 3351–3356.PubMedPubMedCentralCrossRef
191.
Maragozidis, P., Karangeli, M., Labrou, M., Dimoulou, G., Papaspyrou, K., Salataj, E., Pournaras, S., Matsouka, P., Gourgoulianis, K. I., & Balatsos, N. A. (2012). Alterations of deadenylase expression in acute leukemias: evidence for poly(A)-specific ribonuclease as a potential biomarker. Acta Haematologica, 128, 39–46.PubMedCrossRef
192.
193.
Maragozidis, P., Papanastasi, E., Scutelnic, D., Totomi, A., Kokkori, I., Zarogiannis, S. G., Kerenidi, T., Gourgoulianis, K. I., & Balatsos, N. A. (2015). Poly(A)-specific ribonuclease and Nocturnin in squamous cell lung cancer: prognostic value and impact on gene expression. Molecular Cancer, 14, 187.PubMedPubMedCentralCrossRef
194.
Rhodes, D. R., Yu, J., Shanker, K., Deshpande, N., Varambally, R., Ghosh, D., Barrette, T., Pandey, A., & Chinnaiyan, A. M. (2004). ONCOMINE: a cancer microarray database and integrated data-mining platform. Neoplasia, 6, 1–6.PubMedPubMedCentralCrossRef
195.
Finak, G., Bertos, N., Pepin, F., Sadekova, S., Souleimanova, M., Zhao, H., Chen, H., Omeroglu, G., Meterissian, S., Omeroglu, A., Hallett, M., & Park, M. (2008). Stromal gene expression predicts clinical outcome in breast cancer. Nature Medicine, 14, 518–527.PubMedCrossRef
196.
Mittal, S., Aslam, A., Doidge, R., Medica, R., & Winkler, G. S. (2011). The Ccr4a (CNOT6) and Ccr4b (CNOT6L) deadenylase subunits of the human Ccr4-Not complex contribute to the prevention of cell death and senescence. Molecular Biology of the Cell, 22, 748–758.PubMedPubMedCentralCrossRef
197.
Marx, V. (2018). Meet some code-breakers of noncoding RNAs. Nature Publishing Group.
198.
Telonis, A. G., Magee, R., Loher, P., Chervoneva, I., Londin, E., & Rigoutsos, I. (2017). Knowledge about the presence or absence of miRNA isoforms (isomiRs) can successfully discriminate amongst 32 TCGA cancer types. Nucleic Acids Research, 45, 2973–2985.PubMedPubMedCentralCrossRef
199.
200.
201.
202.
Ling, H., Fabbri, M., & Calin, G. A. (2013). MicroRNAs and other non-coding RNAs as targets for anticancer drug development. Nature Reviews. Drug Discovery, 12, 847–865.PubMedPubMedCentralCrossRef
203.
204.
Bartel, D. P. (2004). MicroRNAs: genomics, biogenesis, mechanism, and function. Cell, 116, 281–297.PubMedCrossRef
205.
Kim, V. N. (2005). MicroRNA biogenesis: coordinated cropping and dicing. Nature Reviews. Molecular Cell Biology, 6, 376–385.PubMedCrossRef
206.
Han, J., Lee, Y., Yeom, K. H., Kim, Y. K., Jin, H., & Kim, V. N. (2004). The Drosha-DGCR8 complex in primary microRNA processing. Genes & Development, 18, 3016–3027.CrossRef
207.
Hwang, H. W., Wentzel, E. A., & Mendell, J. T. (2007). A hexanucleotide element directs microRNA nuclear import. Science, 315, 97–100.PubMedCrossRef
208.
Eiring, A. M., Harb, J. G., Neviani, P., Garton, C., Oaks, J. J., Spizzo, R., Liu, S., Schwind, S., Santhanam, R., Hickey, C. J., Becker, H., Chandler, J. C., Andino, R., Cortes, J., Hokland, P., Huettner, C. S., Bhatia, R., Roy, D. C., Liebhaber, S. A., Caligiuri, M. A., Marcucci, G., Garzon, R., Croce, C. M., Calin, G. A., & Perrotti, D. (2010). miR-328 functions as an RNA decoy to modulate hnRNP E2 regulation of mRNA translation in leukemic blasts. Cell, 140, 652–665.PubMedPubMedCentralCrossRef
209.
Jopling, C. L., Yi, M., Lancaster, A. M., Lemon, S. M., & Sarnow, P. (2005). Modulation of hepatitis C virus RNA abundance by a liver-specific MicroRNA. Science, 309, 1577–1581.PubMedCrossRef
210.
Calin, G. A., Liu, C. G., Ferracin, M., Hyslop, T., Spizzo, R., Sevignani, C., Fabbri, M., Cimmino, A., Lee, E. J., Wojcik, S. E., Shimizu, M., Tili, E., Rossi, S., Taccioli, C., Pichiorri, F., Liu, X., Zupo, S., Herlea, V., Gramantieri, L., Lanza, G., Alder, H., Rassenti, L., Volinia, S., Schmittgen, T. D., Kipps, T. J., Negrini, M., & Croce, C. M. (2007). Ultraconserved regions encoding ncRNAs are altered in human leukemias and carcinomas. Cancer Cell, 12, 215–229.PubMedCrossRef
211.
Vasudevan, S., Tong, Y., & Steitz, J. A. (2007). Switching from repression to activation: microRNAs can up-regulate translation. Science, 318, 1931–1934.PubMedCrossRef
212.
Fabbri, M., Paone, A., Calore, F., Galli, R., Gaudio, E., Santhanam, R., Lovat, F., Fadda, P., Mao, C., Nuovo, G. J., Zanesi, N., Crawford, M., Ozer, G. H., Wernicke, D., Alder, H., Caligiuri, M. A., Nana-Sinkam, P., Perrotti, D., & Croce, C. M. (2012). MicroRNAs bind to Toll-like receptors to induce prometastatic inflammatory response. Proceedings of the National Academy of Sciences of the United States of America, 109, E2110–E2116.PubMedPubMedCentralCrossRef
213.
Lehmann, S. M., Kruger, C., Park, B., Derkow, K., Rosenberger, K., Baumgart, J., Trimbuch, T., Eom, G., Hinz, M., Kaul, D., Habbel, P., Kalin, R., Franzoni, E., Rybak, A., Nguyen, D., Veh, R., Ninnemann, O., Peters, O., Nitsch, R., Heppner, F. L., Golenbock, D., Schott, E., Ploegh, H. L., Wulczyn, F. G., & Lehnardt, S. (2012). An unconventional role for miRNA: let-7 activates Toll-like receptor 7 and causes neurodegeneration. Nature Neuroscience, 15, 827–835.PubMedCrossRef
214.
Mitchell, P. S., Parkin, R. K., Kroh, E. M., Fritz, B. R., Wyman, S. K., Pogosova-Agadjanyan, E. L., Peterson, A., Noteboom, J., O'Briant, K. C., Allen, A., Lin, D. W., Urban, N., Drescher, C. W., Knudsen, B. S., Stirewalt, D. L., Gentleman, R., Vessella, R. L., Nelson, P. S., Martin, D. B., & Tewari, M. (2008). Circulating microRNAs as stable blood-based markers for cancer detection. Proceedings of the National Academy of Sciences of the United States of America, 105, 10513–10518.PubMedPubMedCentralCrossRef
215.
Cortez, M. A., Bueso-Ramos, C., Ferdin, J., Lopez-Berestein, G., Sood, A. K., & Calin, G. A. (2011). MicroRNAs in body fluids—the mix of hormones and biomarkers. Nature Reviews. Clinical Oncology, 8, 467–477.PubMedPubMedCentralCrossRef
216.
Redis, R. S., Calin, S., Yang, Y., You, M. J., & Calin, G. A. (2012). Cell-to-cell miRNA transfer: from body homeostasis to therapy. Pharmacology & Therapeutics, 136, 169–174.CrossRef
217.
218.
219.
Ma, L., Reinhardt, F., Pan, E., Soutschek, J., Bhat, B., Marcusson, E. G., Teruya-Feldstein, J., Bell, G. W., & Weinberg, R. A. (2010). Therapeutic silencing of miR-10b inhibits metastasis in a mouse mammary tumor model. Nature Biotechnology, 28, 341–347.PubMedPubMedCentralCrossRef
220.
Song, S. J., Poliseno, L., Song, M. S., Ala, U., Webster, K., Ng, C., Beringer, G., Brikbak, N. J., Yuan, X., Cantley, L. C., Richardson, A. L., & Pandolfi, P. P. (2013). MicroRNA-antagonism regulates breast cancer stemness and metastasis via TET-family-dependent chromatin remodeling. Cell, 154, 311–324.PubMedPubMedCentralCrossRef
221.
222.
Pineau, P., Volinia, S., McJunkin, K., Marchio, A., Battiston, C., Terris, B., Mazzaferro, V., Lowe, S. W., Croce, C. M., & Dejean, A. (2010). miR-221 overexpression contributes to liver tumorigenesis. Proceedings of the National Academy of Sciences of the United States of America, 107, 264–269.PubMedCrossRef
223.
Felli, N., Fontana, L., Pelosi, E., Botta, R., Bonci, D., Facchiano, F., Liuzzi, F., Lulli, V., Morsilli, O., Santoro, S., Valtieri, M., Calin, G. A., Liu, C. G., Sorrentino, A., Croce, C. M., & Peschle, C. (2005). MicroRNAs 221 and 222 inhibit normal erythropoiesis and erythroleukemic cell growth via kit receptor down-modulation. Proceedings of the National Academy of Sciences of the United States of America, 102, 18081–18086.PubMedPubMedCentralCrossRef
224.
Medina, P. P., Nolde, M., & Slack, F. J. (2010). OncomiR addiction in an in vivo model of microRNA-21-induced pre-B-cell lymphoma. Nature, 467, 86–90.PubMedCrossRef
225.
Costinean, S., Zanesi, N., Pekarsky, Y., Tili, E., Volinia, S., Heerema, N., & Croce, C. M. (2006). Pre-B cell proliferation and lymphoblastic leukemia/high-grade lymphoma in E(mu)-miR155 transgenic mice. Proceedings of the National Academy of Sciences of the United States of America, 103, 7024–7029.PubMedPubMedCentralCrossRef
226.
Klein, U., Lia, M., Crespo, M., Siegel, R., Shen, Q., Mo, T., Ambesi-Impiombato, A., Califano, A., Migliazza, A., Bhagat, G., & Dalla-Favera, R. (2010). The DLEU2/miR-15a/16-1 cluster controls B cell proliferation and its deletion leads to chronic lymphocytic leukemia. Cancer Cell, 17, 28–40.PubMedCrossRef
227.
Mavrakis, K. J., Van Der Meulen, J., Wolfe, A. L., Liu, X., Mets, E., Taghon, T., Khan, A. A., Setty, M., Rondou, P., Vandenberghe, P., Delabesse, E., Benoit, Y., Socci, N. B., Leslie, C. S., Van Vlierberghe, P., Speleman, F., & Wendel, H. G. (2011). A cooperative microRNA-tumor suppressor gene network in acute T-cell lymphoblastic leukemia (T-ALL). Nature Genetics, 43, 673–678.PubMedPubMedCentralCrossRef
228.
O'Donnell, K. A., Wentzel, E. A., Zeller, K. I., Dang, C. V., & Mendell, J. T. (2005). c-Myc-regulated microRNAs modulate E2F1 expression. Nature, 435, 839–843.PubMedCrossRef
229.
Hui, L., Zheng, Y., Yan, Y., Bargonetti, J., & Foster, D. A. (2006). Mutant p53 in MDA-MB-231 breast cancer cells is stabilized by elevated phospholipase D activity and contributes to survival signals generated by phospholipase D. Oncogene, 25, 7305–7310.PubMedCrossRef
230.
Shi, M., Zheng, Y., Garcia, A., Xu, L., & Foster, D. A. (2007). Phospholipase D provides a survival signal in human cancer cells with activated H-Ras or K-Ras. Cancer Letters, 258, 268–275.PubMedPubMedCentralCrossRef
231.
Jing, Q., Huang, S., Guth, S., Zarubin, T., Motoyama, A., Chen, J. M., Di Padova, F., Lin, S. C., Gram, H., & Han, J. H. (2005). Involvement of MicroRNA in AU-rich element-mediated mRNA instability. Cell, 120, 623–634.PubMedCrossRef
232.
Braun, J. E., Huntzinger, E., & Izaurralde, E. (2012). A molecular link between miRISCs and deadenylases provides new insight into the mechanism of gene silencing by microRNAs. Cold Spring Harbor Perspectives in Biology, 4.
233.
Lavieri, R., Scott, S. A., Lewis, J. A., Selvy, P. E., Armstrong, M. D., Brown, H. A., & Lindsley, C. W. (2009). Design and synthesis of isoform-selective phospholipase D (PLD) inhibitors. Part II. Identification of the 1,3,8-triazaspiro[4,5]decan-4-one privileged structure that engenders PLD2 selectivity. Bioorganic & Medicinal Chemistry Letters, 19, 2240–2243.CrossRef
234.
Lewis, J. A., Scott, S. A., Lavieri, R., Buck, J. R., Selvy, P. E., Stoops, S. L., Armstrong, M. D., Brown, H. A., & Lindsley, C. W. (2009). Design and synthesis of isoform-selective phospholipase D (PLD) inhibitors. Part I: impact of alternative halogenated privileged structures for PLD1 specificity. Bioorganic & Medicinal Chemistry Letters, 19, 1916–1920.CrossRef
235.
Scott, S. A., Selvy, P. E., Buck, J. R., Cho, H. P., Criswell, T. L., Thomas, A. L., Armstrong, M. D., Arteaga, C. L., Lindsley, C. W., & Brown, H. A. (2009). Design of isoform-selective phospholipase D inhibitors that modulate cancer cell invasiveness. Nature Chemical Biology, 5, 108–117.PubMedPubMedCentralCrossRef
236.
Sulzmaier, F. J., Valmiki, M. K. G., Nelson, D. A., Caliva, M. J., Geerts, D., Matter, M. L., White, E. P., & Ramos, J. W. (2012). PEA-15 potentiates H-Ras-mediated epithelial cell transformation through phospholipase D. Oncogene, 31, 3547–3560.PubMedCrossRef
237.
Bruntz, R. C., Taylor, H. E., Lindsley, C. W., & Brown, H. A. (2014). Phospholipase D2 mediates survival signaling through direct regulation of Akt in glioblastoma cells. Journal of Biological Chemistry, 289, 600–616.PubMedCrossRef
238.
Han, X., Yu, R., Zhen, D., Tao, S., Schmidt, M., & Han, L. (2011). β-1, 3-Glucan-induced host phospholipase D activation is involved in Aspergillus fumigatus internalization into type II human pneumocyte A549 cells. PloS One, 6, e21468.PubMedPubMedCentralCrossRef
239.
Basiouni, S., Fuhrmann, H., & Schumann, J. (2013). The influence of polyunsaturated fatty acids on the phospholipase D isoforms trafficking and activity in mast cells. International Journal of Molecular Sciences, 14, 9005–9017.PubMedPubMedCentralCrossRef
240.
Jiang, Y., Sverdlov, M. S., Toth, P. T., Huang, L. S., Du, G. W., Liu, Y. Y., Natarajan, V., & Minshall, R. D. (2016). Phosphatidic acid produced by RalA-activated PLD2 stimulates caveolae-mediated endocytosis and trafficking in endothelial cells. Journal of Biological Chemistry, 291, 20729–20738.PubMedCrossRef
241.
Lavieri, R. R., Scott, S. A., Selvy, P. E., Kim, K., Jadhav, S., Morrison, R. I., Daniels, J. S., Brown, H. A., & Lindsley, C. W. (2010). Design, synthesis, and biological evaluation of halogenated N-(2-(4-Oxo-1-phenyl-1,3,8-triazaspiro[4.5]decan-8-yl)ethyl)benzamides: discovery of an isoform-selective small molecule phospholipase D2 inhibitor. Journal of Medicinal Chemistry, 53, 6706–6719.PubMedPubMedCentralCrossRef
242.
Ganesan, R., Mahankali, M., Alter, G., & Gomez-Cambronero, J. (2015). Two sites of action for PLD2 inhibitors: the enzyme catalytic center and an allosteric, phosphoinositide biding pocket. Biochimica et Biophysica Acta, 1851, 261–272.PubMedCrossRef
243.
Henkels, K. M., Muppani, N. R., & Gomez-Cambronero, J. (2016). PLD-specific small-molecule inhibitors decrease tumor-associated macrophages and neutrophils infiltration in breast tumors and lung and liver metastases. PLoS One, 11, e0166553.PubMedPubMedCentralCrossRef
244.
Chaves-Moreira, D., de Moraes, F. R., Caruso, Í. P., Chaim, O. M., Senff-Ribeiro, A., Ullah, A., da Silva, L. S., Chahine, J., Arni, R. K., & Veiga, S. S. (2017). Potential implications for designing drugs against the brown spider venom phospholipase-D. Journal of Cellular Biochemistry, 118, 726–738.PubMedCrossRef
245.
Bonnefond, M.-L., Lambert, B., Giffard, F., Abeilard, E., Brotin, E., Louis, M.-H., Gueye, M. S., Gauduchon, P., Poulain, L., & N’Diaye, M. (2015). Calcium signals inhibition sensitizes ovarian carcinoma cells to anti-Bcl-xL strategies through Mcl-1 down-regulation. Apoptosis, 20, 535–550.PubMedPubMedCentralCrossRef
246.
Monovich, L., Mugrage, B., Quadros, E., Toscano, K., Tommasi, R., LaVoie, S., Liu, E., Du, Z., LaSala, D., Boyar, W., & Steed, P. (2007). Optimization of halopemide for phospholipase D2 inhibition. Bioorganic & Medicinal Chemistry Letters, 17, 2310–2311.CrossRef
247.
Stegner, D., Thielmann, I., Kraft, P., Frohman, M. A., Stoll, G., & Nieswandt, B. (2013). Pharmacological inhibition of phospholipase D protects mice from occlusive thrombus formation and ischemic stroke—brief report significance. Arteriosclerosis, Thrombosis, and Vascular Biology, 33, 2212–2217.PubMedCrossRef
248.
Su, W., Yeku, O., Olepu, S., Genna, A., Park, J.-S., Ren, H., Du, G., Gelb, M. H., Morris, A. J., & Frohman, M. A. (2009). 5-Fluoro-2-indolyl des-chlorohalopemide (FIPI), a phospholipase D pharmacological inhibitor that alters cell spreading and inhibits chemotaxis. Molecular Pharmacology, 75, 437–446.PubMedCrossRef
249.
O'connell, J., O’sullivan, G. C., Collins, J. K., & Shanahan, F. (1996). The Fas counterattack: Fas-mediated T cell killing by colon cancer cells expressing Fas ligand. Journal of Experimental Medicine, 184, 1075–1082.PubMedCrossRef
250.
Strand, S., Hofmann, W. J., Hug, H., Müller, M., Otto, G., Strand, D., Mariani, S. M., Stremmel, W., Krammer, P. H., & Galle, P. R. (1996). Lymphocyte apoptosis induced by CD95 (APO–1/Fas) ligand–expressing tumor cells—a mechanism of immune evasion? Nature Medicine, 2, 1361.PubMedCrossRef
251.
Foulkes, W. D., Smith, I. E., & Reis-Filho, J. S. (2010). Triple-negative breast cancer. New England Journal of Medicine, 363, 1938–1948.PubMedCrossRef
252.
Hudis, C. A., & Gianni, L. (2011). Triple-negative breast cancer: an unmet medical need. The Oncologist, 16, 1–11.PubMedCrossRef
Metadata
Title
Lack of effective translational regulation of PLD expression and exosome biogenesis in triple-negative breast cancer cells
Author
Julian Gomez-Cambronero
Publication date
01-09-2018
Publisher
Springer US
Published in
Cancer and Metastasis Reviews / Issue 2-3/2018
Print ISSN: 0167-7659
Electronic ISSN: 1573-7233
DOI
https://doi.org/10.1007/s10555-018-9753-x

Other articles of this Issue 2-3/2018

Cancer and Metastasis Reviews 2-3/2018 Go to the issue

Announcement

Biographies

OriginalPaper

Platelets and extracellular vesicles in cancer: diagnostic and therapeutic implications

OriginalPaper

Targeting the enzymes involved in arachidonic acid metabolism to improve radiotherapy

OriginalPaper

Angiogenesis and vascular stability in eicosanoids and cancer

OriginalPaper

The role of lipid signaling in the progression of malignant melanoma

OriginalPaper

Evaluation of oncogenic cysteinyl leukotriene receptor 2 as a therapeutic target for uveal melanoma
Webinar | 19-02-2024 | 17:30 (CET)

Keynote webinar | Spotlight on antibody–drug conjugates in cancer

Watch now

Antibody–drug conjugates (ADCs) are novel agents that have shown promise across multiple tumor types. Explore the current landscape of ADCs in breast and lung cancer with our experts, and gain insights into the mechanism of action, key clinical trials data, existing challenges, and future directions.

Dr. Véronique Diéras
Prof. Fabrice Barlesi
Developed by: Springer Medicine
Image Credits