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 2023 EHA Congress 2023 ASCO Annual Meeting
Clinical Collections
Advances in Alzheimer’s

Keynote webinar | Spotlight on sleep in brain health

LIVE: Thursday 2nd May 2024, 18:00-19:30 (CEST)

Quality sleep is essential for health. But what happens to our brains when sleep patterns are disturbed? Join our experts to explore the interplay between sleep disruption and neurological diseases, and the questions that you need to be asking your patients to help you prevent the harmful effects of sleep deprivation.
ADVANCED SEARCH
Log in
Top
Breast Cancer Research
Published in: Breast Cancer Research 4/2000

01-08-2000 | Review

Metalloproteinases: role in breast carcinogenesis, invasion and metastasis

Authors: Michael J Duffy, Teresa M Maguire, Arnold Hill, Enda McDermott, Niall O'Higgins

Published in: Breast Cancer Research | Issue 4/2000

Login to get access

Abstract

The matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases. Their primary function is degradation of proteins in the extracellular matrix. Currently, at least 19 members of this family are known to exist. Based on substrate specificity and domain organization, the MMPs can be loosely divided into four main groups: the interstitial collagenases, gelatinases, stromelysins and membrane-type MMPs. Recent data from model systems suggest that MMPs are involved in breast cancer initiation, invasion and metastasis. Consistent with their role in breast cancer progression, high levels of at least two MMPs (MMP-2 and stromelysin-3) have been found to correlate with poor prognosis in patients with breast cancer. Because MMPs are apparently involved in breast cancer initiation and dissemination, inhibition of these proteinases may be of value both in preventing breast cancer and in blocking metastasis of established tumours
Literature
1.
Chambers AF, Matrisian LM: Changing views of the role of matrix metalloproteinases in metastasis. J Natl Cancer Inst. 1997, 89: 1260-1270. 10.1093/jnci/89.17.1260. This is a comprehensive overview on the multiple roles of MMPs in cancer initiation and progression.CrossRefPubMed
2.
Duffy MJ, McCarthy K: Matrix metalloproteinases in cancer: prognostic markers and targets for therapy. Int J Oncol. 1998, 12: 1343-1348. This paper examines the prognostic and therapeutic potential of MMPs in cancer.PubMed
3.
Balbin M, Pendas AM, Uria JA, et al: Expression and regulation of collagenase-3 (MMP-13) in human malignant tumors. APMIS. 1999, 107: 45-53.CrossRefPubMed
4.
Levi E, Fridman R, Miao H-Q, et al: Matrix metalloproteinase releases active soluble ectodomain of fibroblast growth factor 1. Proc Natl Acad Sci USA. 1996, 93: 7069-7074. 10.1073/pnas.93.14.7069.CrossRefPubMedPubMedCentral
5.
Rei D, Majmudar G, Weiss SJ: Hydrolytic inactivation of a breast carcinoma cell-derived serpin by human stromelysin-3. J Biol Chem . 1994, 269: 25849-25855.
6.
Murphy G, Segain JP, O'Shea M, et al: The 28 kD N-terminal domain of mouse stromelysin-3 has the general properties of a weak stromelysin-like metalloproteinase. J Biol Chem. 1993, 268: 15435-15441.PubMed
7.
Pei D, Weiss S: Furin-dependent intracellular activation of the human stromelysin-3 zymogen. Nature. 1995, 375: 244-247. 10.1038/375244a0.CrossRefPubMed
8.
Seki M: Membrane-type matrix metalloproteinases. Review article. APMIS. 1999, 107: 137-143.CrossRef
9.
Ohuchi E, Imai K, Fujii Y, et al: Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. J Biol Chem. 1997, 272: 2446-2451. 10.1074/jbc.272.4.2446.CrossRefPubMed
10.
Hiraoka N, Allen E, Apel IJ, et al: Matrix metalloproteinases regulate neovascularization by acting as pericellular fibrinolysins. Cell. 1998, 95: 365-377.CrossRefPubMed
11.
Stone AL, Kroeger M, Amy Sang QX: Structure-function analysis of the ADAM family of disintegrin-like and metalloproteinase-containing proteins [review]. J Prot Chem. 1999, 18: 447-465. 10.1023/A:1020692710029. A comprehensive and up-to-date review on ADAMs is provided.CrossRef
12.
Henriet P, Blavier L, DeClerck YA: Tissue inhibitors of metalloproteinases (TIMP) in invasion and proliferation. APMIS. 1999, 107: 111-119. This paper reviews the role of TIMPs in cancer proliferation and invasion.CrossRefPubMed
13.
Amour A, Slocombe PM, Webster A, et al: TNF-α converting enzyme (TACE) is inhibited by TIMP-3. FEBS Lett . 1998, 435: 39-41. 10.1016/S0014-5793(98)01031-X.CrossRefPubMed
14.
Guedez L, Stetler-Stevenson WG, Wolf L, et al: In vitro suppression of programmed cell death of B cells by tissue inhibitor of metalloproteinase-1. J Clin Invest. 1998, 102: 2002-2010.CrossRefPubMedPubMedCentral
15.
Valente P, Fassina G, Melchiori A, et al: TIMP-2 overexpression reduces invasion and angiogenesis and protects B16F10 melanoma cells from apoptosis. Int J Cancer. 1998, 75: 246-253. 10.1002/(SICI)1097-0215(19980119)75:2<246::AID-IJC13>3.0.CO;2-B.CrossRefPubMed
16.
Baker AH, George SJ, Zaltsman AB, et al: Inhibition of invasion and induction of apoptotic cell death of cancer cell lines by overexpression of TIMP-3. Br J Cancer. 1999, 79: 1347-1355. 10.1038/sj.bjc.6690217.CrossRefPubMedPubMedCentral
17.
Benz CC: Transcriptional factors and breast cancer. Endoc Rel Cancers. 1998, 5: 271-282. This paper examines the involvement of transcriptional factors in breast carcinogenesis.CrossRef
18.
Giunciuglio D, Culty M, Fassina G, et al: Invasive phenotype of MCF10A cells overexpressing c-Ha-ras and c-erbB-2 oncogenes. Int J Cancer. 1995, 63: 815-822.CrossRefPubMed
19.
Kaya M, Yoshida K, Higashino F, et al: A single ets-related transcription factor, E1AF, confers invasive phenotype on human cancer cells. Oncogene. 1996, 12: 221-227.PubMed
20.
Wiesen JF, Werb Z: The role of stromelysin-1 in stromal-epithelial interactions and cancer. Enzyme Protein. 1996, 49: 174-181.PubMed
21.
22.
Rio M-C, Lefebvre O, Santavicca M, et al: Stromelysin-3 in the biology of the normal and neoplastic mammary gland. J Mam Gland Neoplasia. 1996, 1: 231-240.CrossRef
23.
Masson R, Lefebvre R, Noel A, et al: In vivo evidence that the stromelysin-3 metalloproteinase contributes in a paracrine manner to epithelial cell malignancy. J Cell Biol. 1998, 140: 1535-1541. 10.1083/jcb.140.6.1535.CrossRefPubMedPubMedCentral
24.
Rudolph-Owen LA, Chan R, Muller WJ, et al: The matrix metalloproteinase matrilysin influences early stage mammary tumorigenesis. Cancer Res. 1988, 58: 5500-5506.
25.
Sledge GWJ, Qulali M, Goulet R, et al: Effect of matrix metalloproteinase inhibitor batimastat on breast cancer regrowth and metastasis in athymic mice. J Natl Cancer Inst. 1995, 87: 1546-1550.CrossRefPubMed
26.
Wang M, Liu YE, Greene J, et al: Inhibition of tumor growth and metastasis of human breast cancer cells transfected with tissue inhibitor of metalloproteinase. Oncogene. 1997, 14: 2767-2774. 10.1038/sj.onc.1201245.CrossRefPubMed
27.
Zetter B: Angiogenesis and tumor metastasis. Annu Rev Med. 1998, 49: 407-424. 10.1146/annurev.med.49.1.407. This is an comprehensive and up-to-date review on the role of angiogenesis in tumour metastasis.CrossRefPubMed
28.
Stetler-Stevenenson W: Matrix metalloproteinases in angiogenesis: a moving target for therapeutic intervention. J Clin Invest. 1999, 103: 1237-1241. A review of the role of MMPs in angiogenesis is presented.CrossRef
29.
Peschon JJ, Slack JL, Reddy P, et al: An essential role for ectodomain shedding in mammalian development. Science. 1998, 282: 1281-1284. 10.1126/science.282.5392.1281.CrossRefPubMed
30.
Dong J, Opresko LK, Dempsey PJ, et al: Metalloprotease-mediated ligand release regulates autocrine signalling through the epidermal growth factor receptor. Proc Natl Acad Sci USA. 1999, 96: 6235-6240. 10.1073/pnas.96.11.6235. This is a comprehensive review of the main steps and molecules involved in metastasis.CrossRefPubMedPubMedCentral
31.
Codony-Servat J, Albanell J, Lopez-Talavera JC, et al: Clevage of the HER-2 ectodomain is a pervanadate-activable process that is inhibited by the tissue-inhibitor of metalloprotease-1 in breast cancer cells. Cancer Res. 1999, 59: 1196-1201.PubMed
32.
Eccles SA, Box GM, Court WJ, et al: Control of lymphatic and hematogenous metastasis of a rat mammary carcinoma by the matrix metalloproteinase inhibitor batimistat (BB-94). Cancer Res . 1996, 56: 2815-2822.PubMed
33.
Lochter A, Srebrow A, Sympson CJ, et al: Misregulation of stromelysin-1 expression in mouse mammary tumor cells accompanies acquisition of stromelysin-1 dependent invasive properties. J Biol Chem. 1997, 272: 5007-5015. 10.1074/jbc.272.8.5007.CrossRefPubMed
34.
35.
Yoneda T, Sasaki A, Dunstan C, et al: Inhibition of osteolytic bone metastasis of breast cancer by combined treatment with the bis-phosphonate ibandronate and tissue inhibitor of the matrix metal-loproteinase-2. J Clin Invest. 1997, 99: 2509-2517.CrossRefPubMedPubMedCentral
36.
Barsky S, Togo S, Garbisa S, et al: Type IV collagenase immunoreactivity in invasive breast carcinoma. Lancet. 1983, i: 296-297.CrossRef
37.
Lochter A, Bissell MJ: An odyssey from breast to bone: multistep control of mammary metastases and osteolysis by matrix matalloproteinases. APMIS. 1999, 107: 128-136.CrossRefPubMedPubMedCentral
38.
Duffy MJ: The biochemistry of metastasis. Adv Clin Chem . 1996, 32: 136-166.
39.
Duffy MJ: Do proteases play a role in cancer invasion and metastasis?. Eur J Cancer Clin Oncol. 1987, 23: 583-589.CrossRefPubMed
40.
Talvensaari-Mattila A, Paakko P, Hoyhtya M, et al: Matrix metalloproteinase-2 immunoreactive protein: a marker of aggressiveness in breast carcinoma. Cancer. 1998, 83: 1153-1162. 10.1002/(SICI)1097-0142(19980915)83:6<1153::AID-CNCR14>3.3.CO;2-0.CrossRefPubMed
41.
McCarthy K, Maguire T, McGreal G, et al: High levels of tissue inhibitor of metalloproteinase-1 predict poor outcome in patients with breast cancer. Int J Cancer. 1999, 84: 44-48. 10.1002/(SICI)1097-0215(19990219)84:1<44::AID-IJC9>3.3.CO;2-G.CrossRefPubMed
42.
Remackle A, McCarthy K, Noel A, et al: High levels of TIMP-2 correlate with adverse prognosis in breast cancer. Int J Cancer. 2000, 89: 118-121. 10.1002/(SICI)1097-0215(20000320)89:2<118::AID-IJC3>3.0.CO;2-8.CrossRef
43.
Andreasen P, Kjoller L, Christensen L, et al: The urokinase-type plasminogen activator in cancer metastasis: a review. Int J Cancer. 1997, 72: 1-22. 10.1002/(SICI)1097-0215(19970703)72:1<1::AID-IJC1>3.0.CO;2-Z.CrossRefPubMed
44.
Talbot DC, Brown P: Experimental and clinical studies on the use of matrix metalloproteinases inhibitors for the treatment of cancer. Eur J Cancer. 1996, 32A: 2528-2533. 10.1016/S0959-8049(96)00398-X.CrossRefPubMed
45.
46.
Nemunaitis J, Poole C, Primrose J, et al: Combined analysis of studies of the effects of the matrix metalloproteinase inhibitor marimastat on serum tumor markers in advanced cancer. Selection of a biologically active and tolerable dose for longer-term studies. Clin Cancer Res. 1998, 4: 1101-1109.PubMed
47.
Dano K, Romer J, Nielsen BS, et al: Cancer invasion and tissue remodelling: cooperation of protease systems and cell types. APMIS. 1999, 107: 120-127.CrossRefPubMed
48.
Mitsiades N, Poulaki V, Leone A, et al: Fas-mediated apoptosis in Ewing's sarcoma cell lines by metalloproteinase inhibitors. J Natl Cancer Inst. 1999, 91: 1678-1684. 10.1093/jnci/91.19.1678.CrossRefPubMed
Metadata
Title
Metalloproteinases: role in breast carcinogenesis, invasion and metastasis
Authors
Michael J Duffy
Teresa M Maguire
Arnold Hill
Enda McDermott
Niall O'Higgins
Publication date
01-08-2000
Publisher
BioMed Central
Published in
Breast Cancer Research / Issue 4/2000
Electronic ISSN: 1465-542X
DOI
https://doi.org/10.1186/bcr65

Other articles of this Issue 4/2000

Breast Cancer Research 4/2000 Go to the issue

Review

Future possibilities in the prevention of breast cancer: Breast cancer prevention trials

Commentary

Acetyltransferases and tumour suppression

Research article

BRCA1 and BRCA2 mutations in central and southern Italian patients

Review

Future possibilities in the prevention of breast cancer: Luteinizing hormone-releasing hormone agonists

Review

Future possibilities in the prevention of breast cancer: Fat and fiber and breast cancer research

Commentary

Mammographic screening and mammographic patterns
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