Abstract
Tumor progression is a complex, multistage process by which a normal cell undergoes genetic changes that result in phenotypic alterations and acquisition of the ability to spread and colonization to distant sites in the human body. Understanding the molecular mechanisms of metastasis is crucial for developing novel therapeutic strategies to combat metastatic cancers. Early studies established the importance of the extracellular matrix on tumor cell growth and differentiation. With time, the role of the extracellular matrix and matrix metalloproteinases (MMPs), a family of degradative enzymes, in the regulation of tumor invasion, metastasis, and angiogenesis was recognized. Initially, it was believed that the major role of MMPs in metastasis was to facilitate the breakdown of physical barriers to metastasis, thus promoting invasion and entry into and out of blood or lymphatic vessels (intravasation, extravasation). However, recent evidence suggests that MMPs may have a more complex and divergent role in metastasis as well as in cancer stem cell maintenance. In the present review, the role of MMPs and their functional contribution in metastasis have been revisited and discussed. Upcoming approaches target MMPs and their inhibitors, e.g., tissue inhibitors of metalloproteinases (TIMPs), genetically or pharmacologically, suggesting that MMPs are key regulators of growth of tumors, both at primary and metastatic sites. These evidences present MMPs as the important candidates in creating and maintaining an environment that supports the initiation and maintenance of growth of primary and metastatic tumors. Future endeavors to target matrix metalloproteinases would be important in the development of novel therapeutic strategies against metastatic cancers.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Renee T (2005) Cancer Surpasses Heart Disease as Leading Cause of Death for All But the Very Elderly. J Natl Cancer Inst 97: 330-331
Joyce JA, Jeffrey W (2009) Pollard Microenvironmental regulation of metastasis. Nat Rev Cancer 9: 239-252
Saha B, Adhikary A, Ray P et al (2012) Restoration of tumor suppressor p53 by differentially regulating pro and anti p53 networks in HPV 18 infected cervical cancer cells. Oncogene 31: 178–186
Mazumdar M, Adhikary A, Chakraborty S et al (2013) Targeting RET to induce medullary thyroid cancer cell apoptosis in antagonistic interplay between PI3K/Akt and P38MAPK/caspase 8 pathways. Apoptosis 18: 587-604
Sen GS, Mohanty S, Bhattacharyya S et al (2011) Curcumin enhances the efficacy of chemotherapy by tailoring p65NFkB-p300 cross-talk in favor of p53-p300 in breast cancer. J Biol Chem 286: 42232–42247
Das T, Sa G, Saha B et al (2010) Multifocal signal modulation therapy of cancer: Ancient weapon, modern targets. Mol Cell Biochem 336: 85–95
Lahiry L, Saha B, Chakraborty J et al (2010) Theaflavin targets Fas/Caspase 8 and Akt/pBad pathways to induce apoptosis in p53 mutated human breast cancer cells. Carcinogenesis 31: 259-268
Lahiry L, Saha B, Chakraborty J et al (2008) Contribution of p53 mediated Bax transactivation in theaflavin induced mammary epithelial carcinoma cell apoptosis. Apoptosis 13: 771-781
Kinzler K W, Vogelstein B. The genetic basis of human cancer, 2nd edition, New York: McGraw-Hill, Medical Pub, 3-7, 2002
Katherine N, Weilbaecher T A, McCauley K. (2011) “Cancer to Bone” A fatal attraction. Nat Rev Cancer 11: 411-425
Frantz C, Stewart KM, Weaver VM (2010) The extracellular matrix at a glance. J Cell Sci 123: 4195-4200
Stetler-Stevenson WG, Aznavoorian S, Liotta LA (1993) Tumor cell interactions with the extracellular matrix during invasion and metastasis. Annu Rev Cell Biol 9: 541-573
Wolf K, Wu YI, Liu Y et al (2007) Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion. Nat Cell Biol 9: 893-904
Kenneth A Iczkowski (2011) Cell adhesion molecule CD44: its functional roles in prostate cancer Am J Transl Res 3: 1-7
Rundhaug JE (2003) Matrix Metalloproteinases, Angiogenesis, and Cancer. Clin Cancer Res 9 (2): 551-554
Cavallo-Medved D, Rudy D, Blum G et al (2009) Live-cell imaging demonstrates extracellular matrix degradation in association with active cathepsin B in caveolae of endothelial cells during tube formation. Exp Cell Res 315: 1234-1246
Chua KN, Poon KL, Lim J et al (2011) Target cell movement in tumor and cardiovascular diseases based on the epithelial–mesenchymal transition concept. Adv Drug Deliv Rev 63: 558-567
Kimura YN, Watari K, Fotovati A, et al (2007) Inflammatory stimuli from macrophages and cancer cells synergistically promote tumor growth and angiogenesis. Cancer Sci 98: 2009-2018
Albert R. Davalos, Jean-Philippe Coppe, Judith Campisi (2010) Senescent cells as a source of inflammatory factors for tumor progression. Cancer Meta Rev 29: 273-283
Ram M, Sherer Y, Shoenfeld Y (2006) Matrix metalloproteinase-9 and autoimmune diseases. J Clin Immunol 26: 299-307
Adhikary A, Mohanty S, Lahiry L et al (2009) Theaflavins retards human breast cancer cell migration by inhibiting NFƙB via p53-ROS crosstalk. FEBS L 584: 7-14
Sewon N, Jung Joon J, Jung M et al (2012) Body fluid MMP-2 as a putative biomarker in metastatic breast cancer. Onco Lett 3: 699-703
Opdenakker G, Philippe E. Van den Steen et al (2001) Gelatinase B functions as regulator and effector in leukocyte biology. J Leuko Biol 69: 851-859
Vu TH, Werb Z (2000) Matrix metalloproteinases: effectors of development and normal physiology. Genes & Dev 14: 2123-2133
Audic Y, Hartley RS (2004) Post-transcriptional regulation in cancer. Biol Cell 96: 479-498
Lochter A, Srebrow A, Sympson CJ et al (1997) Misregulation of Stromelysin-1 Expression in Mouse Mammary Tumor Cells Accompanies Acquisition of Stromelysin-1-dependent Invasive Properties. J Biol Chem 272: 5007-5015
Wysocki AB, Staiano-Coico L, Grinnell F (1993) Wound Fluid from Chronic Leg Ulcers Contains Elevated Levels of Metalloproteinases MMP-2 and MMP-9. J Invest Dermatol 101: 64-68
Malemud CJ (2006) Matrix metalloproteinases (MMPs) in health and disease: an overview. Front in Biosc 11: 1696-1701
Fingleton B (2007) Matrix Metalloproteinases as Valid Clinical Targets. Curr Pharmac Des 13: 333-346
Gomis-Rüth FX (2003) Structural aspects of the metzincin clan of metalloendopeptidases. Mol Biotech 24:157-202
Gomis-Rüth FX (2009) Catalytic Domain Architecture of Metzincin Metalloproteases. J Biol Chem 284: 15353-15357
Overall CM, López-Otín C (2002) Strategies for MMP inhibition in cancer: innovations for the post-trial era. Nat Rev Cancer 2: 657-672
Eisen A, Jeffrey J, Gross J (1968) Human skin collagenase. Isolation and mechanism of attack on the collagen molecule. Biochim Biophys Acta 151: 637–645
Fontana V, Coll TA, Sobarzo CM et al (2012) Matrix metalloproteinase expression and activity in trophoblast-decidual tissues at organogenesis in CF-1 mouse. J Mol Histol 43(5): 487-496
Parks WC, Wilson CL, López-Boado YS (2004) Matrix metalloproteinases as modulators of inflammation and innate immunity. Nat Rev Immunol 4: 617-629
Fridman R (2006) Metalloproteinases and cancer. Cancer Metastasis Rev 25: 7-8
Van Wart H, Birkedal-Hansen H (1990) The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc Natl Acad Sci USA 87: 5578–5582
Egeblad M, Werb Z (2002) New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2: 161-174
Pei D, Kang T, Qi H (2000) Cysteine array matrix metalloproteinase (CA-MMP)/MMP-23 is a type II transmembrane matrix metalloproteinase regulated by a single cleavage for both secretion and activation. J Biol Chem 275: 33988–33997
Morgunova E, Tuuttila A, Bergmann U et al (1999) Structure of Human Pro-Matrix Metalloproteinase-2: activation mechanism revealed. Sci 284: 1667-1670
Bode W (1995) A helping hand for collagenases: the haemopexin-like domain. Struct 3(6): 527–30
Kojima K, Ogawa H, Matsumoto I, Yoneda A (1998) Characterization of the ligand binding activities of vitronectin: interaction of vitronectin with lipids and identification of the binding domains for various ligands using recombinant domains. Biochem 37: 6351–6360
Massova I, Kotra LP, Fridman R, Mobashery S (1998) Matrix metalloproteinases: structures, evolution, and diversification. FASEB J 12: 1075–1095
Kojima S, Itoh Y, Matsumoto S (2000) Membrane-type 6 matrix metalloproteinase (MT6-MMP, MMP-25) is the second glycosyl-phosphatidyl inositol (GPI)-anchored MMP. FEBS Letter 480: 142-146
Monea S, Lehti K, Keski-Oja J, Mignatti P et al (2002) Plasmin activates pro-matrix metalloproteinase-2 with a membrane-type 1 matrix metalloproteinase-dependent mechanism. J Cell Physiol 192: 160-170
Park BC, Thapa D, Lee YS et al (2007)1-furan-2-yl-3-pyridin-2-yl-propenone inhibits the invasion and migration of HT1080 human fibrosarcoma cells through the inhibition of proMMP-2 activation and down regulation of MMP-9 and MT1-MMP. Eur J Pharmacol. 587: 193-197
Brooke C. Henderson, Suresh C. Tyagi (2006) Oxidative mechanism and homeostasis of proteinase/antiproteinase in congestive heart failure. J Mol and Cell Cardiol 41: 959-962
Fu X, Kassim SY, Parks WC (2003) Hypochlorous Acid Generated by Myeloperoxidase Modifies Adjacent Tryptophan and Glycine Residues in the Catalytic Domain of Matrix Metalloproteinase-7: An Oxidative: Mechanism for Restraining Proteolytic Activity during Inflammation. J Biol Chem 278: 28403-28409
Visse R, Nagase H (2003) Matrix Metalloproteinases and Tissue Inhibitors of Metalloproteinases :Structure, Function, and Biochemistry. Circul Res 92: 827-839
Rupp PA, Visconti RP, Czirók A et al (2008) Matrix Metalloproteinase 2-Integrin αvβ3 Binding Is Required for Mesenchymal Cell Invasive Activity but Not Epithelial Locomotion: A Computational Time-Lapse Study. Mol Biol Cell 19: 5529–5540
Zarrabi K, Dufour A, Li J, Kuscu C et al (2011)Inhibition of matrix metalloproteinase 14 (MMP-14)-mediated cancer cell migration. J Biol Chem. 286: 33167-33177
Levental KR, Yu H, Kass L et al (2009) Matrix Crosslinking Forces Tumor Progression by Enhancing Integrin Signaling. Cell: 891–906
Smith ML, Gourdon D, Little WC, Kubow KE, Eguiluz RA et al (2007) Force-Induced Unfolding of Fibronectin in the Extracellular Matrix of Living Cells. PLoS Biol 5: e268
Wirtz D, Konstantopoulos K, Searson PC (2011) The physics of cancer: the role of physical interactions and mechanical forces in metastasis. Nat Rev Cancer 11: 512-522
Würtz SØ , Schrohl AS, Sørensen NM (2005) Tissue inhibitor of metalloproteinases-1 in breast cancer. Endocr Relat Cancer 12: 215-227
Ogata Y, Itoh Y, Nagase H (1995) Steps Involved in Activation of the Pro-matrix Metalloproteinase 9 (Progelatinase B)-Tissue Inhibitor of Metalloproteinases-1 Complex by 4-Aminophenylmercuric Acetate and Proteinases. J Biol Chem 270: 18506-18511
Seo DW, Li H, Guedez L et al (2003) TIMP-2 Mediated Inhibition of Angiogenesis: An MMP-Independent Mechanism. Cell 114: 171-180
Basu R, Fan D, Kandalam V et al (2012) Loss of Timp3 leads to abdominal aortic aneurysm formation in response to angiotensin II. J Biol Chem 287: 44083-44096
Tummalapalli CM, Heath BJ, Tyagi SC (2001) Tissue inhibitor of metalloproteinase-4 instigates apoptosis in transformed cardiac fibroblasts. J Cell Biochem 80: 512-521
DeBerardinis RJ. (2012) Good neighbours in the tumour stroma reduce oxidative stress. Nat Cell Biol 14: 235-236
Mishra P, Banerjee D, Baruch AB (2011) Chemokines at the crossroads of tumor-fibroblast interactions that promote malignancy. J Leukoc Biol 89: 31-39
Bekes EM, Schweighofer B, Kupriyanova TA (2011) Tumor-recruited neutrophils and neutrophil TIMP-free MMP-9 regulate coordinately the levels of tumor angiogenesis and efficiency of malignant cell intravasation. Am J Pathol 179: 1455-1470
Schmalfeldt B, Prechtel D, Härting K et al (2001) Increased Expression of Matrix Metalloproteinases (MMP)-2, MMP-9, and the Urokinase-Type Plasminogen Activator Is Associated with Progression from Benign to Advanced Ovarian Cancer. Clin Cancer Res 7: 2396-2404
Kuittinen O, Apaja-Sarkkinen M, Turpeenniemi-Hujanen T (2003) Gelatinases (MMP-2 and MMP-9), TIMP-1 expression and the extent of neovascularization in aggressive non-Hodgkin’s lymphomas. Eur J Haematol 71: 91-109
Koshiba T, Hosotani R, Wada M (1998) Involvement of matrix metalloproteinase-2 activity in invasion and metastasis of pancreatic carcinoma. Cancer 82: 642-650
Choi JY, Jang YS, Min SY (2011) Overexpression of MMP-9 and HIF-1α in Breast Cancer Cells under Hypoxic Conditions. J Breast Cancer 14: 88–95
Kedrin D, Gligorijevic B, Wyckoff J et al (2008) Intravital imaging of metastatic behavior through a mammary imaging window. Nat Meth 5: 1019-1021
Koop S, Khokha R, Schmidt EE et al (1994) Overexpression of metalloproteinase inhibitor in B16F10 cells does not affect extravasation but reduces tumor growth. Cancer Res 54: 4791-4797
Royer C, Lu X (2011) Epithelial cell polarity: a major gatekeeper against cancer? Cell Death Differ 18:1470-1477
Vernon AE, LaBonne C et al (2004)Tumor Metastasis: A New Twist on Epithelial–Mesenchymal Transitions. Current Biol 14: 719-721
Brabletz T, Herrmann K, Jung A et al (2000)Expression of Nuclear β-Catenin and c-myc Is Correlated with Tumor Size but Not with Proliferative Activity of Colorectal Adenomas. Am J Pathol 156: 865–870
Lynch CC, Vargo-Gogola T, Matrisian LM et al (2010) Cleavage of E-Cadherin by Matrix Metalloproteinase-7 Promotes Cellular Proliferation in Nontransformed Cell Lines via Activation of RhoA. J of Oncol 2010: 530745
Liu P, Yang J, Pei J, Pei D, Wilson MJ (2010) Regulation of MT1-MMP activity by β-catenin in MDCK non-cancer and HT1080 cancer cells. J Cell Physiol 225: 810-821
Frittoli E, Palamidessi A, Disanza A (2012) Secretory and endo/exocytic trafficking in invadopodia formation: the MT1-MMP paradigm. Eur J Cell Biol 90(2-3): 108-114
Nascimento CF, Gama-De-Souza LN, Freitas VM (2010) Role of MMP9 on invadopodia formation in cells from adenoid cystic carcinoma. Study by laser scanning confocal microscopy. Microsc Res Tech 73: 99-108
Mizutani K, Kofuji K, Shirouzu K (2000) The significance of MMP-1 and MMP-2 in peritoneal disseminated metastasis of gastric cancer. Surg Today 30: 614-621
Yang EV, Sood AK, Chen M (2006 ) Norepinephrine Up-regulates the Expression of Vascular Endothelial Growth Factor, Matrix Metalloproteinase (MMP)-2, and MMP-9 in Nasopharyngeal Carcinoma Tumor Cells. Cancer Res 66: 10357-10364
Szabova L, Chrysovergis K, Yamada S (2008) MT1-MMP is required for efficient tumor dissemination in experimental metastatic disease. Oncogene 27: 3274-3281
Davies B, Miles DW, Happerfield LC (1993) Activity of type IV collagenases in benign and malignant breast disease. Br J Cancer 67: 1126-1131
DeClerck YA, Imren S (1994) Protease inhibitors: role and potential therapeutic use in human cancer. Eur J Cancer 30A: 2170-2180
Lu XQ, Levy M, Weinstein IB et al (1991) Immunological quantitation of levels of tissue inhibitor of metalloproteinase-1 in human colon cancer. Cancer Res 51: 6231-6235
L Guedez, W G Stetler-Stevenson, L Wolff et al (1998) In vitro suppression of programmed cell death of B cells by tissue inhibitor of metalloproteinases-1. J Clin Invest 102: 2002–2010
Zucker S, Lysik RM, Malik M et al (1992) Secretion of Gelatinases and Tissue Inhibitors of Metalloproteinases by Human Lung-Cancer Cell-Lines and Revertant Cell-Lines - Not an Invariant Correlation with Metastasis. Int J Cancer 52: 366-371
Parks WC (1999) Matrix metalloproteinases in repair. Wound Rep Regen 7: 423-432
Packard BZ, Artym VV, Komoriya A, Yamada KM (2009) Direct visualization of protease activity on cells migrating in three-dimensions. Matrix Biol 28: 3-10
Giannelli G, Pozzi A, Stetler-Stevenson WG et al (1999)Expression of matrix metalloprotease-2-cleaved laminin-5 in breast remodeling stimulated by sex steroids. Am J Pathol 154: 1193-1201
Xu J, Rodriguez D, Petitclerc E et al (2001) Proteolytic exposure of a cryptic site within collagen type IV is required for angiogenesis and tumor growth in vivo. J Cell Biol 154: 1069-1080
Okamoto I, Tsuiki H, Kenyon CL et al (2002) Proteolytic Cleavage of the CD44 Adhesion Molecule in Multiple Human Tumors. Am J Pathol 160: 441-447
Jaime G. de la Garza-Salazar, Abelardo Meneses García, Claudia Arce-Salinas. Inflammatory Breast Cancer, 1st edition, Springer, 29-50, 2012
Paiva De CS, Yoon KC, Pangelinan BS (2009) Cleavage of functional IL-2 receptor alpha chain (CD25) from murine corneal and conjunctival epithelia by MMP-9. J Inflamm 6: 31-42
Becker C, Fantini MC, Neurath MF (2006) TGF-beta as a T cell regulator in colitis and colon cancer. Cytokine and growth factor reviews 17: 97-106
Kataoka H, Uchino H, Iwamura T (1999) Enhanced Tumor Growth and Invasiveness in Vivo by a Carboxyl-Terminal Fragment of α1-Proteinase Inhibitor Generated by Matrix Metalloproteinases. Am J Pathol 154: 457–468
Webster NL, Crowe SM (2006) Matrix metalloproteinases, their production by monocytes and macrophages and their potential role in HIV-related diseases. J Leukoc Biol 80: 1052-1066
Stephanie J. Mail G, Kurschat N, Drenckhan A (2012) Involvement of CXCR4 Chemokine Receptor in Metastastic HER2-Positive Esophageal Cancer. PLOS One 7: e47287
Davalos AR, Coppe JP, Campisi J et al (2010)Senescent cells as a source of inflammatory factors for tumor progression. Cancer Metast Rev 29: 273-283
Pengfei L, Weaver MV, Werb Z (2012) The extracellular matrix: A dynamic niche in cancer progression. J Cell Biol 196: 395-406
Huang Y, Song N, Ding Y et al (2009) Pulmonary vascular destabilization in the premetastatic phase facilitates lung metastasis. Cancer Res 69: 7529-7537
Song N, Sung H, Choi JY et al (2012) Preoperative serum levels of matrix metalloproteinase-2 (MMP-2) and survival of breast cancer among Korean women. Cancer Epidemiol Biomarkers Prev 21(8):1371-1380
Demeter A, Sziller I, Csapo Z et al (2005) Molecular Prognostic Markers in Recurrent and in Non-recurrent Epithelial Ovarian Cancer. Antican Res 25: 2885-2890
Kuniyasu H, Lee ME, Douglas B et al (1999) Relative Expression of E-Cadherin and Type IV Collagenase Genes Predicts Disease Outcome in Patients with Resectable Pancreatic Carcinoma. Clin Cancer Res 5: 25-33
Yamamoto H, Itoh F, Shouhei I et al (2001) Expression of Matrix Metalloproteinases and Tissue Inhibitors of Metalloproteinases in Human Pancreatic Adenocarcinomas: Clinicopathologic and Prognostic Significance of Matrilysin Expression. J Clin Oncol 19: 1118-1127
Moser PL, Kieback DG, Hefler L et al (1999)Immunohistochemical detection of matrix metalloproteinases (MMP) 1 and 2 and tissue inhibitor of metalloproteinase 2 (TIMP 2) in stage IB cervical cancer. Anticancer Res.19: 4391–4393
Inoue T, Yashiro M, Nishimura S et al (1999) Matrix metalloproteinase-1 expression is a prognostic factor for patients with advanced gastric cancer. Int J Mol Med 4: 73-80
Yoshizaki T, Maruyama Y, Sato H et al (2001) Expression of tissue inhibitor of matrix metalloproteinase-2 correlates with activation of matrix metalloproteinase-2 and predicts poor prognosis in tongue squamous cell carcinoma. Int J Cancer 95: 44–50
Zeng ZS, Huang Y, Cohen AM et al (1996) Prediction of colorectal cancer relapse and survival via tissue RNA levels of matrix metalloproteinase-9. J Clin Oncol 14: 3133–3140
Gokaslan ZL, Chintala SK, York JE et al (1998) Expression and role of matrix metalloproteinases MMP-2 and MMP-9 in human spinal column tumours. Clin Exp Metastasis 16: 721-728
Gojhi K, Fujimoto N, Hara I (1998) Serum matrix metalloproteinase-2 and its density in men with prostate cancer as a new predictor of disease extension. Int J Cancer 79: 96-101
Slaton JW, Inoue K, Perrotte P et al (2001) Expression levels of genes that regulate metastasis and angiogenesis correlate with advanced pathological stage of renal cell carcinoma. Am J Pathol 158: 735–743
Verline J, Regala RP, Tseng CI (2012)Matrix Metalloproteinase-10 Is Required for Lung Cancer Stem Cell Maintenance, Tumor Initiation and Metastatic Potential. PLoS one 7: e35040
Coussens LM, Fingleton B, Matrisian LM (2012) Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Sci. 295: 2387–2392
Talbot DC, Brown P (1996) Experimental and clinical studies on the use of matrix metallo proteinases inhibitor for the treatment of cancer. Eur J Cancer 32A: 2528-2533
Nemunaitis J, Poole C, Primrose J et al (1998) 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 4: 1101-1109
Sparano JA, Bernardo P, Stephenson P et al (2004)Randomized phase III trial of marimastat versus placebo in patients with metastatic breast cancer who have responding or stable disease after first-line chemotherapy: Eastern Cooperative Oncology Group trial E2 196. J Clin Oncol 22: 4683–4690
Miller KD, Saphner TJ, Waterhouse DM et al (2004)A randomized phase II feasibility trial of BMS-275291 in patients with early stage breast cancer. Clin Cancer Res 10: 1971–1975
Overall CM, Kleifeld O (2006) Tumour microenvironment—opinion: validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy. Nat Rev Cancer 6: 227–239
Montel V, Kleeman J, Agarwal D et al (2004) Altered metastatic behavior of human breast cancer cells after experimental manipulation of matrix metalloproteinase 8 gene expression. Cancer Res 64: 1687–1694
Gutierrez-Fernandez A, Fueyo A, Folgueras AR et al (2008) Matrix metalloproteinase-8 functions as a metastasis suppressor through modulation of tumor cell adhesion and invasion. Cancer Res 68: 2755–2763
Sternlicht MD, Lochter A, Sympson CJ et al (1999) The stromal proteinase MMP3/stromelysin-1 promotes mammary carcinogenesis Cell 98: 137–146
Moy FJ, Chanda PK, Chen J et al (2002) Impact of mobility on structure-based drug design for the MMPs. J Am Chem Soc 124: 12658–12659
Jacobsen JA, Major Jourden JL, Miller MT et al (2010) To bind zinc or not to bind zinc: an examination of innovative approaches to improved metalloproteinase inhibition. Biochim Biophys Acta 1803: 72–94
Ikejiri M, Bernardo MM, Meroueh SO et al (2005) Design, synthesis, and evaluation of a mechanism-based inhibitor for gelatinase A. J Org Chem 70: 5709–5712
Sela-Passwell N, Rosenblum G, Shoham T, et al (2009) Structural and functional bases for allosteric control of MMP activities: Can it pave the path for selective inhibition? Biochim Biophys Acta 1803: 29-38
Williamson RA, Hutton M, Vogt G et al (2001) Tyrosine 36 plays a critical role in the interaction of the AB loop of tissue inhibitor of metalloproteinases-2 with matrix metalloproteinase-14. J Biol Chem 276: 32966–32970
Lee MH, Atkinson S, Rapti M et al (2009) The activity of a designer tissue inhibitor of metalloproteinases (TIMP)-1 against native membrane type 1 matrix metalloproteinase (MT1-MMP) in a cell-based environment. Cancer Lett 290: 114-122
Acknowledgment
Authors acknowledge the financial supports from CSIR and DST, Govt. of India.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2014 Springer Science+Business Media New York
About this chapter
Cite this chapter
Mukherjee, S., Manna, A., Mazumdar, M., Das, T. (2014). Matrix Metalloproteinases in Cancer Metastasis: An Unsolved Mystery. In: Dhalla, N., Chakraborti, S. (eds) Role of Proteases in Cellular Dysfunction. Advances in Biochemistry in Health and Disease, vol 8. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-9099-9_10
Download citation
DOI: https://doi.org/10.1007/978-1-4614-9099-9_10
Published:
Publisher Name: Springer, New York, NY
Print ISBN: 978-1-4614-9098-2
Online ISBN: 978-1-4614-9099-9
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)