Matrix metalloproteinases and tumor progression

Advances in Experimental Medicine and Biology

Volumn 532, Issue , 2003, Pages 91-107

  Freije, José M P ^a   Balbín, Milagros ^a   Pendás, Alberto M ^a   Sánchez, Luis M ^a   Puente, Xose S ^a   López Otín, Carlos ^a  

^a UNIVERSITY OF OVIEDO   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE INHIBITOR;

CANCER INVASION; CELL PROLIFERATION; CLINICAL TRIAL; CONFERENCE PAPER; ENZYME ACTIVITY; HUMAN; METASTASIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; TUMOR CELL; TUMOR GROWTH;

EID: 0141757365     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4615-0081-0_9     Document Type: Conference Paper

References (115)

1. Chambers, A. F., Groom, A.C., and MacDonald, I.C. Dissemination and growth of cancer cells in metastatic sites. Nature Rev Cancer 2, 563-572 (2002)
2. López-Otín, C. and Overall, C. M. Protease degradomics, a challenge for proteomics. Nature Rev. Mol. Cell Biol. 3, 509-519 (2002)
3. Brinckerhoff, C. E. and Matrisian, L. M. Matrix metalloproteinases: a tail of a frog that became a prince. Nature Rev. Mol. Cell Biol. 3, 207-214 (2002).
4. Egeblad, M. and Werb, Z. New functions for the matrix metalloproteinases in cancer progression. Nature Rev. Cancer 2, 163-175 (2002).
5. Overall, C. M. and López-Otín, C Strategies for MMP inhibition in cancer: innovations for the post-trial era. Nature Rev. Cancer. 2, 657-672 (2002)
6. Uría, J. A. and López-Otín, C. Matrilysin-2, a new matrix metalloproteinase expressed in human tumors and showing the minimal domain organization required for secretion, latency, and activity. Cancer Res. 60, 4745-4751 (2000).
7. Velasco, G. et al. Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family members. J. Biol. Chem. 274, 4570-4576 (1999).
8. Sternlicht, M. D. et al. The stromal proteinase MMP3/stromelysin-1 promotes mammary carcinogenesis. Cell 98, 137-146 (1999).
9. Sternlicht, M. D. and Werb, Z. How matrix metalloproteinases regulate cell behavior. Annu. Rev. Cell Dev. Biol. 17, 463-516 (2001)
10. Rifkin, D. B., Mazzieri, R., Munger, J. S., Noguera, I. and Sung, J. Proteolytic control of growth factor availability. APMIS 107, 80-85 (1999).
11. Mañes, S. et al. The matrix metalloproteinase-9 regulates the insulin-like growth factor-triggered autocrine response in DU-145 carcinoma cells. J. Biol. Chem. 274, 6935-6945 (1999).
12. Noe, V. et al. Release of an invasion promoter E-cadherin fragment by matrilysin and stromelysin-1. J. Cell Sci. 114, 111-118 (2001).
13. Lochter, A. et al. Matrix metalloproteinase stromelysin-1 triggers a cascade of molecular alterations that leads to stable epithelial-to-mesenchymal conversion and a premalignant phenotype in mammary epithelial cells. J. Cell Biol. 139, 1861-1872 (1997).
14. Ho, A. T., Voura, E. B., Soloway, P. D., Watson, K. L. and Khokha, R. MMP inhibitors augment fibroblast adhesion through stabilization of focal adhesion contacts and up-regulation of cadherin function. J. Biol. Chem. 276, 40215-40224 (2001).
15. McQuibban, G. A. et al. Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3. Science 289, 1202-1206 (2000).
16. Fingleton, B., Vargo-Gogola, T., Crawford, H. C. and Matrisian, L. M. Matrilysin (MMP-7) expression selects for cells with reduced sensitivity to apoptosis. Neoplasia 3, 459-468 (2001).
17. Yu, Q. and Stamenkovic, I. Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-β and promotes tumor invasion and angiogenesis. Genes Dev. 14, 163-176 (2000).
18. Stetler-Stevenson, W. G. Matrix metalloproteinases in angiogenesis: a moving target for therapeutic intervention. J. Clin. Invest. 103, 1237-1241 (1999).
19. Dong, Z., Kumar, R., Yang, X. and Fidler, I. J. Macrophage-derived metalloelastase is responsible for the generation of angiostatin in Lewis lung carcinoma. Cell 88, 801-810 (1997).
20. Cornelius, L. A. et al. Matrix metalloproteinases generate angiostatin: effects on neovascularization. J. Immunol. 161, 6845-6852 (1998).
21. Ferreras, M., Felbor, U., Lenhard, T., Olsen, B. R. and Delaisse, J. Generation and degradation of human endostatin proteins by various proteinases. FEBS Lett. 486, 247-251 (2000).
22. Kheradmand, F., Werner, E., Tremble, P., Symons, M. and Werb, Z. Role of Racl and oxygen radicals in collagenase-1 expression induced by cell shape change. Science 280, 898-902 (1998).
23. Overall, C. M., Wrana, J. L. and Sodek, J. Independent regulation of collagenase, 72-kDa progelatinase, and metalloendoproteinase inhibitor expression in human fibroblasts by transforming growth factor-β. J. Biol. Chem. 264, 1860-1869 (1989).
24. Guérin, E., Ludwig, M. G., Basset, P. and Anglard, P. Stromelysin-3 induction and interstitial collagenase repression by retinoic acid: therapeutical implication of receptor-selective retinoids dissociating transactivation and AP-1-mediated transrepression. J. Biol. Chem. 272, 11088-11095 (1997).
25. Uría, J. A., Jiménez, M. G., Balbín, M., Freije, J. M. P. and López-Otín, C. Differential effects of transforming growth factor-β on the expression of collagenase-1 and collagenase-3 in human fibroblasts. J. Biol. Chem. 273, 9769-9777 (1998).
26. Jiménez, M. J. et al. A regulatory cascade involving retinoic acid, Cbfal, and matrix metalloproteinases is coupled to the development of a process of perichondrial invasion and osteogenic differentiation during bone formation. J. Cell Biol. 155, 1333-1344 (2001).
27. Simon, C., Goepfert, H. and Boyd, D. Inhibition of the p38 mitogen-activated protein kinase by SB 203580 blocks PMA-induced Mr 92,000 type IV collagenase secretion and in vitro invasion. Cancer Res. 58, 1135-1139 (1998).
28. Johansson, N. et al. Expression of collagenase-3 (MMP-13) and collagenase-1 (MMP-1) by transformed keratinocytes is dependent on the activity of p38 mitogen-activated protein kinase. J. Cell Sci. 113, 227-235 (2000).
29. Pendás, A. M., Balbin, M., Llano, E., Jimenez, M. G. and López-Otín, C. Structural analysis and promoter characterization of the human collagenase-3 gene (MMP13). Genomics 40, 222-233 (1997).
30. Gutman, A. and Wasylyk, B. The collagenase gene promoter contains a TPA and oncogene-responsive unit encompassing the PEA3 and AP-1 binding sites. EMBO J. 9, 2241-2246 (1990).
31. Bond, M., Fabunmi, R. P., Baker, A. H. and Newby, A. C. Synergistic upregulation of metalloproteinase-9 by growth factors and inflammatory cytokines: an absolute requirement for transcription factor NF-kappa B. FEBS Lett. 435, 29-34 (1998).
32. Rutter, J. L. et al. A single nucleotide polymorphism in the matrix metalloproteinase-1 promoter creates an Ets binding site and augments transcription. Cancer Res. 58, 5321-5325 (1998).
33. Biondi, M. L. et al. MMP1 and MMP3 polymorphisms in promoter regions and cancer. Clin. Chem. 46, 2023-2024 (2000).
34. Springman, E. B., Angleton, E. L., Birkedal-Hansen, H. and Van Wart, H.E. Multiple modes of activation of latent human fibroblast collagenase: evidence for the role of a Cys73 active-site zinc complex in latency and a "cysteine switch" mechanism for activation. Proc. Natl. Acad. Sci. USA 87, 364-368 (1990).
35. Bannikov, G. A., Karelina, T. V., Collier, I. E., Marmer, B. L. and Goldberg, G. I. Substrate binding of gelatinase B induces its enzymatic activity in the presence of intact propeptide. J. Biol. Chem. 277, 16022-16027 (2002).
36. Knauper, V. et al. Cellular mechanisms for human collagenase-3 (MMP-13) activation: evidence that MT1-MMP (MMP-14) and gelatinase A (MMP-2) are able to generate active enzyme. J. Biol. Chem. 271, 17124-17131 (1996).
37. Sato, H. et al. A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature 370, 61-65 (1994).
38. Strongin, A. Y. et al. Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease. J. Biol. Chem. 270, 5331-5338 (1995).
39. Overall, C. M. et al. Identification of the tissue inhibitor of metalloproteinases-2 (TIMP-2) binding site on the hemopexin carboxyl domain of human gelatinase A by site-directed mutagenesis. The hierarchical role in binding TIMP-2 of the unique cationic clusters of hemopexin modules III and IV. J. Biol. Chem. 274, 4421-4429 (1999).
40. Pei, D. and Weiss, S. J. Furin-dependent intracellular activation of the human stromelysin-3 zymogen. Nature 375, 244-247 (1995).
41. Yana, I. and Weiss, S. J. Regulation of membrane type-1 matrix metalloproteinase activation by proprotein convertases. Mol. Biol. Cell 11, 2387-2401 (2000).
42. Lohi, J., Wilson, C. L., Roby, J. D. and Parks, W. C. Epilysin, a novel human matrix metalloproteinase (MMP-28) expressed in testis and keratinocytes and in response to injury. J. Biol. Chem. 276, 10134-10144 (2001).
43. Velasco, G. et al. Human MT6-matrix metalloproteinase: identification, progelatinase A activation, and expression in brain tumors. Cancer Res. 60, 877-882 (2000).
44. Nagase, H., Itoh, Y. and Binner, S. Interaction of alpha 2-macroglobulin with matrix metalloproteinases and its use for identification of their active forms. Ann. N. Y. Acad. Sci. 732, 294-302 (1994).
45. Brew, K., Dinakarpandian, D. and Nagase, H. Tissue inhibitors of metalloproteinases: evolution, structure and function. Biochim Biophys Acta 1477, 267-283 (2000).
46. Amour, A. et al. The in vitro activity of ADAM-10 is inhibited by TIMP-1 and TIMP-3. FEBS Lett. 473, 275-279 (2000).
47. Kashiwagi, M., Tortorella, M., Nagase, H. and Brew, K. TIMP-3 is a potent inhibitor of aggrecanase 1 (ADAM-TS4) and aggrecanase 2 (ADAM-TS5). J. Biol. Chem. 276, 12501-12504 (2001).
48. Khokha, R. et al. Antisense RNA-induced reduction in murine TIMP levels confers oncogenicity on Swiss 3T3 cells. Science 243, 947-950 (1989).
49. Corcoran, M. L. and Stetler-Stevenson, W. G. Tissue inhibitor of metalloproteinase-2 stimulates fibroblast proliferation via a cAMP-dependent mechanism. J. Biol. Chem. 270, 13453-13459 (1995).
50. Jiang, Y., Goldberg, I. D. and Shi, Y. E. Complex roles of tissue inhibitors of metalloproteinases in cancer. Oncogene 21, 2245-2252 (2002).
51. Oh, J. et al. The membrane-anchored MMP inhibitor RECK is a key regulator of extracellular matrix integrity and angiogenesis. Cell 107, 789-800 (2001).
52. Herman, M. P. et al. Tissue factor pathway inhibitor-2 is a novel inhibitor of matrix metalloproteinases with implications for atherosclerosis. J. Clin. Invest. 107, 1117-1126 (2001).
53. Mott, J. D. et al. Post-translational proteolytic processing of procollagen C-terminal proteinase enhancer releases a metalloproteinase inhibitor. J. Biol. Chem. 275, 1384-1390 (2000).
54. Petitclerc, E. et al. New functions for non-collagenous domains of human collagen type IV. Novel integrin ligands inhibiting angiogenesis and tumor growth in vivo. J. Biol. Chem. 275, 8051-8061 (2000).
55. Stetefeld, J. et al. The laminin-binding domain of agrin is structurally related to N-TIMP-1. Nat. Struct. Biol. 8, 705-709 (2001).
56. Westermarck, J. and Kähäri, V. M. Regulation of matrix metalloproteinase expression in tumor invasion. FASEB J. 13, 781-792 (1999).
57. Hua, J. and Muschel, R. J. Inhibition of matrix metalloproteinase 9 expression by a ribozyme blocks metastasis in a rat sarcoma model system. Cancer Res. 56, 5279-5284 (1996).
58. Kondraganti, S. et al. Selective suppression of matrix metalloproteinase-9 in human glioblastoma cells by antisense gene transfer impairs glioblastoma cell invasion. Cancer Res. 60, 6851-6855 (2000).
59. Nagavarapu, U., Relloma, K. and Herron, G. S. Membrane type 1 matrix metalloproteinase regulates cellular invasiveness and survival in cutaneous epidermal cells. J. Invest. Dermatol. 118, 573-581 (2002).
60. Slaton, J. W. et al. Treatment with low-dose interferon-alpha restores the balance between matrix metalloproteinase-9 and E-cadherin expression in human transitional cell carcinoma of the bladder. Clin. Cancer Res. 7, 2840-2853 (2001).
61. Ala-aho, R. et al. Inhibition of collagenase-3 (MMP-13) expression in transformed human keratinocytes by interferon-gamma is associated with activation of extracellular signal-regulated kinase-2,2 and STAT1. Oncogene. 19, 248-257 (2000).
62. Ma, Z., Qin, H. and Benveniste, E. N. Transcriptional suppression of matrix metalloproteinase-9 gene expression by IFN-γ and IFN-β: critical role of STAT-1α. J. Immunol. 167, 5150-5159 (2001).
63. Mengshol, J. A., Mix, K. S. and Brinckerhoff, C. E. Matrix metalloproteinases as therapeutic targets in arthritic diseases: bull's-eye or missing the mark? Arthritis Rheum. 46, 13-20 (2002).
64. Futamura, M. et al. Malolactomycin D, a potent inhibitor of transcription controlled by the Ras responsive element, inhibit Ras-mediated transformation activity with suppression of MMP-1 and MMP-9 in NIH3T3 cells. Oncogene 20, 6724-6730 (2001).
65. Zhang, Y. et al. Hyaluronan-CD44s signaling regulates matrix metalloproteinase-2 secretion in a human lung carcinoma cell line QG90. Cancer Res. 62, 3962-3965 (2002).
66. McGaha, T. L., Phelps, R. G., Spiera, H. and Bona, C. Halofuginone, an inhibitor of type-I collagen synthesis and skin sclerosis, blocks transforming-growth-factor-beta-mediated Smad3 activation in fibroblasts. J. Invest. Dermatol. 118, 461-470 (2002).
67. Elkin M, Reich R, Nagler A, Aingorn E, Pines M, de-Groot N, Hochberg A, Vlodavsky I. Inhibition of matrix metalloproteinase-2 expression and bladder carcinoma metastasis by halofuginone. Clin. Cancer Res. 5, 1982-1988 (1999).
68. Karin, M. and Chang, L. AP-1-glucocorticoid receptor crosstalk taken to a higher level. J. Endocrinol. 169, 447-451 (2001).
69. Sato, T. et al. Inhibition of activator protein-1 binding activity and phosphatidylinositol 3-kinase pathway by nobiletin, a polymethoxy flavonoid, results in augmentation of tissue inhibitor of metalloproteinases-1 production and suppression of production of matrix metalloproteinases-1 and -9 in human fibrosarcoma HT-1080 cells. Cancer Res. 62, 1025-1029 (2002).
70. Mohan, R. et al. Curcuminoids inhibit the angiogenic response stimulated by fibroblast growth factor-2, including expression of matrix metalloproteinase gelatinase B. J. Biol. Chem. 275, 10405-10412 (2000).
71. Adams, J. et al. Proteasome inhibitors: a novel class of potent and effective antitumor agents. Cancer Res. 59, 2615-2622 (1999).
72. Tan, C. and Waldmann, T. A. Proteasome inhibitor PS-341, a potential therapeutic agent for adult T-cell leukemia. Cancer Res. 62, 1083-1086 (2002).
73. Barille, S. et al. Metalloproteinases in multiple myeloma: production of matrix metalloproteinase-9 (MMP-9), activation of proMMP-2, and induction of MMP-1 by myeloma cells. Blood 90, 1649-1655 (1997).
74. Jimenez, M. J. et al. Collagenase 3 is a target of Cbfal, a transcription factor of the runt gene family involved in bone formation. Mol. Cell Biol. 19, 4431-4442 (1999).
75. Yang, J. et al. Prostate cancer cells induce osteoblast differentiation through a Cbfal-dependent pathway. Cancer Res. 61, 5652-5659 (2001).
76. Sun, Y. et al. Wild type and mutant p53 differentially regulate the gene expression of human collagenase-3 (hMMP-13). J. Biol. Chem. 275, 11327-11332 (2000).
77. Koul, D. et al. Suppression of matrix metalloproteinase-2 gene expression and invasion in human glioma cells by MMAC/PTEN. Oncogene 20, 6669-6678 (2001).
78. Fenrick, R. et al. TEL, a putative tumor suppressor, modulates cell growth and cell morphology of ras-transformed cells while repressing the transcription of stromelysin-1. Mol. Cell Biol. 20, 5828-5839 (2000).
79. Galvez, B. G., Matias-Roman, S., Albar, J. P., Sanchez-Madrid, F. and Arroyo, A. G. Membrane type 1-matrix metalloproteinase is activated during migration of human endothelial cells and modulates endothelial motility and matrix remodeling. J. Biol. Chem. 276, 37491-37500 (2001).
80. Annabi, B. et al. Green tea polyphenol (-)-epigallocatechin 3-gallate inhibits MMP-2 secretion and MT1-MMP-driven migration in glioblastoma cells. Biochim Biophys. Acta 1542, 209-220 (2002).
81. Bassi, D. E. et al. Furin inhibition results in absent or decreased invasiveness and tumorigenicity of human cancer cells. Proc. Natl. Acad. Sci. USA 98, 10326-10331 (2001).
82. Rodriguez-Manzaneque, J. C. et al. Thrombospondin-1 suppresses spontaneous tumor growth and inhibits activation of matrix metalloproteinase-9 and mobilization of vascular endothelial growth factor. Proc. Natl Acad. Sci. USA 98, 12485-12490 (2001).
83. Yang, Z., Strickland, D. K. and Bornstein, P. Extracellular matrix metalloproteinase 2 levels are regulated by the low density lipoprotein-related scavenger receptor and thrombospondin 2. J. Biol. Chem. 276, 8403-8408 (2001).
84. Kim, Y. M. et al. Endostatin inhibits endothelial and tumor cellular invasion by blocking the activation and catalytic activity of matrix metalloproteinase. Cancer Res. 60, 5410-5413 (2000).
85. Nakada, M. et al. Suppression of membrane-type 1 matrix metalloproteinase (MMP)-mediated MMP-2 activation and tumor invasion by testican 3 and its splicing variant gene product, N-tes. Cancer Res. 61, 8896-8902 (2001).
86. Sgadari, C. et al. HIV protease inhibitors are potent anti-angiogenic molecules and promote regression of Kaposi sarcoma. Nature Med. 8, 225-232 (2002).
87. Kruger, A., Fata, J. E. and Khokha, R. Altered tumor growth and metastasis of a T-cell lymphoma in Timp-1 transgenic mice. Blood 90, 1993-2000 (1997).
88. Martin, D. C. et al. Transgenic TIMP-1 inhibits simian virus 40 T antigen-induced hepatocarcinogenesis by impairment of hepatocellular proliferation and tumor angiogenesis. Lab. Invest. 79, 225-234 (1999).
89. Brown, P. D. Clinical studies with matrix metalloproteinase inhibitors. APMIS 107, 174-180 (1999).
90. Duivenvoorden, W, C. et al. Doxycycline decreases tumor burden in a bone metastasis model of human breast cancer. Cancer Res. 62, 1588-1591 (2002).
91. Cianfrocca, M. et al. Matrix metalloproteinase inhibitor COL-3 in the treatment of AIDS-related Kaposi's sarcoma: a phase I AIDS malignancy consortium study. J. Clin. Oncol. 20, 153-159 (2002).
92. Boissier, S. et al. Bisphosphonates inhibit breast and prostate carcinoma cell invasion, an early event in the formation of bone metastases. Cancer Res. 60, 2949-2954 (2000).
93. Coussens, L. M., Fingleton, B. and Matrisian, L. M. Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science 295, 2387-2392 (2002).
94. Bramhall, S.R. et al. Marimastat as maintenance therapy for patients with advanced gastric cancer: a randomised trial. Br. J. Cancer. 86, 1864-1870 (2002).
95. Bramhall, S. R., Rosemurgy, A., Brown, P. D., Bowry, C. and Buckels, J. A. Marimastat as first-line therapy for patients with unresectable pancreatic cancer: a randomized trial. J. Clin. Oncol. 19, 3447-3455 (2001).
96. Groves, M D. et al. Phase II trial of temozolomide plus the matrix metalloproteinase inhibitor, marimastat, in recurrent and progressive glioblastoma multiforme. J. Clin. Oncol. 20, 1383-1388 (2002).
97. Zucker, S., Cao, J. and Chen, W. T. Critical appraisal of the use of matrix metalloproteinase inhibitors in cancer treatment. Oncogene 19, 6642-6650 (2000).
98. Bergers, G., Javaherian, K., Lo, K. M., Folkman, J. and Hanahan, D. Effects of angiogenesis inhibitors on multistage carcinogenesis in mice. Science 284, 808-812 (1999).
99. Fingleton, B. M., Heppner Goss, K. J., Crawford, H. C. and Matrisian, L. M. Matrilysin in early stage intestinal tumorigenesis. APMIS 107, 102-110 (1999).
100. Pozzi, A. et al. Elevated matrix metalloprotease and angiostatin levels in integrin alpha I knockout mice cause reduced tumor vascularization. Proc. Natl Acad. Sci. USA 97, 2202-2207 (2000).
101. Pozzi, A., LeVine, W. F. and Gardner, H. A. Low plasma levels of matrix metalloproteinase 9 permit increased tumor angiogenesis. Oncogene 22, 272-281 (2002).
102. Vazquez, F. et al. METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity. J. Biol. Chem. 274, 23349-23357 (1999).
103. Cal, S. et al. Cloning, expression analysis, and structural characterization of seven novel human ADAMTSs, a family of metalloproteinases with disintegrin and thrombospondin-1 domains. Gene 283, 49-62 (2002)
104. Gomis-Ruth, F. X. et al. Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1. Nature 389, 77-81 (1997).
105. Bode, W. et al. Structural properties of matrix metalloproteinases. Cell Mol. Life Sci. 55, 639-652 (1999).
106. Morgunova, E., Tuuttila, A., Bergmann, U. and Tryggvason, K. Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2. Proc. Natl. Acad. Sci. USA. 99, 7414-7419 (2002).
107. Koivunen, E. et al. Tumor targeting with a selective gelatinase inhibitor. Nat. Biotechnol. 17, 768-774 (1999).
108. Bernardo, M. M., Brown. S., Li, Z. H., Fridman, R. and Mobashery, S. Design, synthesis, and characterization of potent, slow-binding inhibitors that are selective for gelatinases. J. Biol. Chem. 277, 11201-11207 (2002).
109. Garbisa, S. et al. Tumor gelatinases and invasion inhibited by the green tea flavanol epigallocatechin-3-gallate. Cancer 91, 822-832 (2001).
110. Falardeau. P., Champagne, P., Poyet, P., Hariton, C. and Dupont, E. Neovastat, a naturally occurring multifunctional antiangiogenic drug, in phase III clinical trials. Semin. Oncol. 28, 620-625 (2001).
111. Nielsen, B. S. et al. Collagenase-3 expression in breast myofibroblasts as a molecular marker of transition of ductal carcinoma in situ lesions to invasive ductal carcinomas. Cancer Res. 61, 7091-7100 (2001).
112. Bissell, M. J. and Radisky, D. Putting tumours in context. Nature Rev. Cancer 1, 46-54 (2001).
113. Silletti, S., Kessler, T., Goldberg, J., Boger, D. L. and Cheresh, D. A. Disruption of matrix metalloproteinase 2 binding to integrin αvβ3 by an organic molecule inhibits angiogenesis and tumor growth in vivo. Proc. Natl Acad. Sci. USA 98, 119-124 (2001).
114. Overall, C. M. Matrix metalloproteinase substrate binding domains, modules, and exosites: overview and experimental strategies. Methods Mol. Biol. 151, 73-114 (2001).
115. Liu, S., Netzel-Arnett, S., Birkedal-Hansen, H. and Leppla, S. H. Tumor cell-selective cytotoxicity of matrix metalloproteinase-activated anthrax toxin. Cancer Res. 60, 6061-6067 (2000).