Strategies for MMP inhibition in cancer: Innovations for the post-trial era

Nature Reviews Cancer

Volumn 2, Issue 9, 2002, Pages 657-672

  Overall, Christopher Mark ^a   López Otín, Carlos ^b  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^b UNIVERSITY OF OVIEDO   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITOR; MATRIX METALLOPROTEINASE; 4 DEDIMETHYLAMINOSANCYCLINE; AE 941; CGS 27023A; INTERLEUKIN 1; MARIMASTAT; MATRIX METALLOPROTEINASE INHIBITOR; MITOGEN ACTIVATED PROTEIN KINASE; MM 1270; NUCLEAR FACTOR; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PRINOMASTAT; PROTEASOME INHIBITOR; REBIMASTAT; TANOMASTAT; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

ANIMAL; BINDING SITE; CHEMISTRY; CLINICAL TRIAL; DRUG ANTAGONISM; ENZYME SPECIFICITY; ENZYMOLOGY; GENE EXPRESSION REGULATION; GENETICS; HUMAN; METABOLISM; NEOPLASM; REVIEW; STRUCTURE ACTIVITY RELATION; ANTINEOPLASTIC ACTIVITY; BASEMENT MEMBRANE; CANCER; CANCER SURVIVAL; CELL SURFACE; CYTOKINE PRODUCTION; DRUG MECHANISM; DRUG TARGETING; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME INHIBITION; EXTRACELLULAR MATRIX; GENE OVEREXPRESSION; METASTASIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN MOTIF; REGULATORY MECHANISM; SIGNAL TRANSDUCTION; SINGLE NUCLEOTIDE POLYMORPHISM; STOMACH CANCER; TUMOR GROWTH;

ANIMALS; BINDING SITES; CLINICAL TRIALS; ENZYME INHIBITORS; GENE EXPRESSION REGULATION, ENZYMOLOGIC; HUMANS; MATRIX METALLOPROTEINASES; NEOPLASMS; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 0036716282     PISSN: 1474175X     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrc884     Document Type: Review

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127. 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).
128. Gomis-Ruth, F. X. et al. Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1. Nature 389, 77-81 (1997).
129. Bode, W. et al. Structural properties of matrix metalloproteinases. Cell Mol. Life Sci. 55, 639-652 (1999).
130. Turk, B. E., Huang, L. L., Piro, E. T. and Cantley, L. C. Determination of protease cleavage site motifs using mixture-based oriented peptide libraries. Nature Biotechnol. 19, 661-667 (2001).
131. Koivunen, E. et al. Tumor targeting with a selective gelatinase inhibitor. Nature Biotechnol. 17, 768-774 (1999).
132. 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).
133. Garbisa, S. et al. Tumor gelatinases and invasion inhibited by the green tea flavonol epigallocatechin-3-gallate. Cancer 91, 822-832 (2001).
134. 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).
135. Baker, A. H., George, S. J., Zaltsman, A. B., Murphy, G. and Newby, A. C. Inhibition of invasion and induction of apoptotic cell death of cancer cell lines by overexpression of TIMP-3. Br. J. Cancer. 79, 1347-1355 (1999).
136. Bello, L. et al. Simultaneous inhibition of glioma angiogenesis, cell proliferation, and invasion by a naturally occurring fragment of human metalloproteinase-2. Cancer Res. 61, 8730-8736 (2001). Analysis of possibilities of disrupting non-catalytic activities of MMPs.
137. Du, L. et al. cDNA cloning of the murine Pex gene implicated in X-linked hypophosphatemia and evidence for expression in bone. Genomics 36, 22-28 (1996).
138. Pfeifer, A., Kessler, T., Silletti, S., Cheresh, D. A. and Verma, I. M. Suppression of angiogenesis by lentiviral delivery of PEX, a noncatalytic fragment of matrix metalloproteinase 2 Proc. Natl Acad. Sci. USA 97, 12227-12232 (2000).
139. 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).
140. Tam, E., Wu, Y. I., Butler, G. S., Stack, S. M. and Overall, C. M. Collagen binding properties of the MT1-MMP hemopexin C domain: the ectodomain of the 44-kDa autocatalytic fragment of MT1-MMP inhibits cell invasion by disrupting native type I collagen cleavage. J. Biol. Chem. 25 Jul 2002 [epub ahead of print].
141. Peng, K. W., Vile, R., Cosset, F. L. and Russell, S. Selective transduction of protease-rich tumors by matrix-metalloproteinase-targeted retroviral vectors. Gene Ther. 6, 1552-1557 (1999). Together with references 142 and 143, this paper is an example of novel strategies for cancer therapy that is based on exploiting MMP function.
142. 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).
143. Hayashi, M., Tomita, M. and Yoshizato, K. Interleukin-2-collagen chimeric protein which liberates interleukin-2 upon collagenolysis. Protein Eng. 15, 429-436 (2002).
144. Lippman, S. M. and Matrisian, L. M. Protease inhibitors in oral carcinogenesis and chemoprevention. Clin. Cancer Res. 6, 4599-4603 (2000).
145. Balbin, M. et al. Identification and enzymatic characterization of two diverging murine counterparts of human interstitial collagenase (MMP-1) expressed at sites of embryo implantation. J. Biol. Chem. 276, 10253-10262 (2001).
146. Weissleder, R. Scaling down imaging: molecular mapping of cancer in mice. Nature Rev. Cancer 2, 11-18 (2002). Excellent discussion of potential solutions to the problem of assessment of in vivo inhibition of MMPs.
147. Schatzkin, A. and Gail, M. The promise and peril of surrogate end points in cancer research. Nature Rev. Cancer 2, 19-27 (2002).
148. Gross, J. and Lapiere C. M. Collagenolytic activity in amphibian tissues: A tissue culture assay. Proc. Natl Acad. Sci. USA 48, 1014-1022 (1962). The first demonstration of an animal collagenase that is active at neutral pH, normal temperature and isotonicity: the starting point of studies on MMPs.
149. Hirohata, S. et al. Punctin, a novel ADAMTS-like molecule, ADAMTSL-1, in extracellular matrix. J. Biol. Chem. 277, 12182-12189 (2002).
150. Lewitt, N. C. et al. Phase I and pharmacological study of the oral matrix metalloproteinase inhibitor, MMI270 (CGS27023A), in patients with advanced solid cancer. Clin. Cancer Res. 7, 1912-1922 (2001).