333
Views
99
CrossRef citations to date
0
Altmetric
Original Article

Matrix metalloproteinases and their inhibitors

Pages 55-60 | Published online: 08 Jul 2009

References

  • Allan J A., Hembry R M., Angal S, Reynolds J J., Murphy G. Binding of latent and high Mr active forms of stromelysin to collagen is mediated by the C-terminal domain. J Cell Sci 1991; 99: 789–95
  • Allan J A., Docherty A J P, Barker P, Huskisson N P., Reynolds J J., Murphy G. The binding of gelatinases A and B to type 1 collagen and other matrix components. Biochem J 1995, in press
  • Apte S S., Mattei M-G, Olsen B R. Cloning of the cDNA encoding human tissue inhibitor of metalloproteinases-3 (TIMP-3) and mapping of the TIMP3 gene to chromosome 22. Genomics 1994a; 19: 86–90
  • Apte S S., Hayashi K, Seldin M F., Mattei M-G, Hayashi M, Olsen B R. Gene encoding a novel murine tissue inhibitor of metalloproteinases (TIMP), TIMP-3, is expressed in developing mouse epithelia, cartilage, and muscle, and is located on mouse chromosome 10. Dev Dyn 1994b; 200: 177–97
  • Brown C C., Hembry R M., Reynolds J J. Immunolocalization of metalloproteinases and their inhibitor in the rabbit growth plate. J Bone Joint Surg 1989; 71-A: 580–93
  • Buttle D J., Handley C J., Ilic M Z., Saklatvala J, Murata M, Barrett A J. Inhibition of cartilage proteoglycan release by a specific inactivator of cathepsin B and an inhibitor of matrix metalloproteinases. Evidence for two converging pathways of chondrocyte-mediated proteoglycan degradation. Arthritis Rheum 1993; 36: 1709–17
  • Clark I M., Powell L K., Ramsey S, Hazleman B L., Cawston T E. The measurement of collagenase, tissue inhibitor of metalloproteinases (TIMP), and collagenase-TIMP complex in synovial fluids from patients with osteoarthritis and rheumatoid arthritis. Arthritis Rheum 1993; 36: 372–79
  • Crabbe T, Ioannou C, Docherty A J P. Human progelatinase A can be activated by autolysis at a rate that is concentration-dependent and enhanced by heparin bound to the C-terminal domain. Eur J Biochem 1993; 218: 431–38
  • Dayer J-M, Krane S M., Russell R G G, Robinson D R. Production of collagenase and prostaglandins by isolated adherent rheumatoid synovial cells. Proc Natl Acad Sci USA 1976; 730: 945–9
  • Dean D D., Martel-Pelletier J, Pelletier J-P, Howell D S., Woessner J F. Evidence for metalloproteinase and metal-loproteinase inhibitor imbalance in human osteoarthritic cartilage. J Clin Invest 1989; 84: 678–85
  • Docherty A J P, Murphy G. The tissue metalloproteinase family and the inhibitor TIMP: a study using cDNAs and recombinant proteins. Ann. Rheum Dis 1990; 49: 469–79
  • Docherty A J P, O'Connell J, Crabbe T, Angal S, Murphy G. The matrix metalloproteinases and their natural inhibitors: prospects for treating degenerative tissue diseases. TIBTECH 1992; 10: 200–7
  • Flannery C R., Lark M W., Sandy J D. Identification of a stromelysin cleavage site within the interglobular domain of human aggrecan. Evidence for proteolysis at this site in vivo in human articular cartilage. J Biol Chem 1992; 267: 1008–14
  • Fosang A J., Neame P J., Hardingham T E., Murphy G, Hamilton J A. Cleavage of cartilage proteoglycan between G1 and G2 domains by stromelysins. J Biol Chem 1991; 266: 15579–82
  • Fosang A J., Neame P J., Last K, Hardingham T E., Murphy G, Hamilton J A. The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B. J Biol Chem 1992; 267: 19470–4
  • Fosang A J., Last K, Neame P J., Murphy G, Knauper V, Tschesche H, Hughes C E., Caterson B, Hardingham T E. Neutrophil collagenase (MMP-8) cleaves at the aggrecanase site E373-A374 in the interglobular domain of cartilage aggrecan. Biochem J 1994; 304: 347–51
  • Gadher S J., Schmid T M., Heck L W., Woolley D E. Cleavage of collagen type X by human synovial collagenase and neutrophil elastase. Matrix 1989; 9: 109–15
  • Gadher S J., Eyre D R., Wotton S F., Schmid T M., Woolley D E. Degradation of cartilage collagens type II, IX, X and XI by enzymes derived from human articular chondrocytes. Matrix 1990; 10: 154–63
  • Hasty K A., Hibbs M S., Kang A H., Mainardi C L. Secreted forms of human neutrophil collagenase. J Biol Chem 1986; 261: 5645–50
  • Hembry R M., Murphy G, Cawston T E., Dingle J T., Reynolds J J. Characterization of a specific antiserum for mammalian collagenase from several species: immunolo-calization of collagenase in rabbit chondrocytes and uterus. J Cell Sci 1986; 81: 105–23
  • Hembry R M., Bagga M R., Reynolds J J., Hamblen D L. Immunolocalisation studies on six matrix metalloproteinases and their inhibitors, TIMP-1 and TIMP-2, in synovia from patients with osteo- and rheumatoid arthritis. Ann Rheum Dis 1995; 54: 25–32
  • Hughes C, Murphy G, Hardingham T E. Metalloproteinase digestion of cartilage proteoglycan. Pattern of cleavage by stromelysin and susceptibility to collagenase. Biochem J 1991; 279: 733–9
  • Ilic M Z., Handley C J., Robinson H C., Mok M T. Mechanism of catabolism of aggrecan by articular cartilage. Arch Biochem Biophys 1995; 292: 827–35
  • Lohmander L S., Hoerrner L A., Lark M W. Metallo-proteinases, tissue inhibitor, and proteoglycan fragments in knee synovial fluid in human osteoarthritis. Arthritis Rheum 1993; 36: 181–9
  • Loulakis P, Shrikhande A, Davis G, Maniglia C A. N-Terminal sequence of proteoglycan fragments isolated from medium of interleukin-1 treated articular-cartilage cultures. Biochem J 1992; 284: 589–93
  • Matrisian L M. The matrix-degrading metalloproteinases. BioEssays 1992; 14: 455–63
  • McCachren S S. Expression of metalloproteinases and met-alloproteinase inhibitor inhuman arthritic synovium. Arthritis Rheum 1991; 34: 1085–92
  • Murphy G, Allan J A., Willenbrock F, Cockett M I., O'Connell J P., Docherty A J P. The role of the C-terminal domain in collagenase and stromelysin specificity. J Biol Chem 1992a; 267: 9612–8
  • Murphy G, Atkinson S, Ward R, Gavrilovic J, Reynolds J J. The role of plasminogen activators in the regulation of connective tissue metalloproteinases. Ann NY Acad Sci 1992b; 667: 1–12
  • Murphy G, Willenbrock F, Ward R V., Cockett M I., Eaton D, Docherty A J P. The C-terminal domain of 72 kDa gelat-inase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases. Biochem J 1992c; 283: 637–41
  • Murphy G, Reynolds J J. Extracellular matrix degradation. Connective Tissue and its Heritable Disorders, P M. Royce, B Steinmann. Wiley-Liss, Inc, New York 1993; 287–316
  • Nagase H, Ogata Y, Suzuki K, Enghild J J., Salvesen G. Substrate specificities and activation mechanisms of matrix metalloproteinases. Biochem Soc Trans 1991; 19: 715–8
  • Okada Y, Gonoji Y, Nakanishi I, Nagase H, Hayakawa T. Immunohistochemical demonstration of collagenase and tissue inhibitor of metalloproteinases (TIMP) in synovial lining cells of rheumatoid synovium. Virchows Archiv B Cell Pathol 1990; 59: 305–312
  • Okada Y, Shinmei M, Tanaka O, Naka K, Kimura A, Nakanishi I, Bayliss M Y., Iwata K, Nagase H. Localization of matrix metalloproteinase 3 (stromelysin) in osteoarthritic cartilage and synovium. Lab Invest 1992; 66: 680–90
  • Pavloff N, Staskus P W., Kishnani N S., Hawkes S P. A new inhibitor of metalloproteinases from chicken: ChIMP-3 A third member of the TIMP family. J Biol Chem 1992; 267: 17321–6
  • Saklatvala J, Sarsfield S. How do interleukin 1 and tumour necrosis factor induce degradation of proteoglycan in cartilage?. The Control of Tissue Damage, A M. Glauert. Elsevier, Amsterdam 1988; 97–106
  • Sandy J D., Neame P J., Boynton R E., Flannery C R. Catabolism of aggrecan in cartilage explants. Identification of a major cleavage site within the interglobular domain. J Biol Chem 1991; 266: 8683–5
  • Sato H, Takino T, Okada Y, Cao J, Shinagawa A, Yamamoto E, Seiki M. A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature 1994; 370: 61–5
  • Sirum K L., Brinckerhoff C E. Cloning of the genes for human stromelysin and stromelysin 2: different expression in rheumatoid synovial fibroblasts. Biochemistry 1989; 28: 8691–8
  • Staskus P W., Masiarz F R., Pallanck L J., Hawkes S P. The 21-kDa protein is a transformation-sensitive metalloproteinase inhibitor of chicken fibroblasts. J Biol Chem 1991; 266: 449–54
  • Tremble P, Chiquet-Ehrismann R, Werb Z. The extracellular matrix ligands fibronectin and tenascin collaborate in regulating collagenase gene expression in fibroblasts. Mol Biol Cell 1994; 5: 439–53
  • Vater C A., Mainardi C L., Harris E. D. Binding of latent rheumatoid synovial collagenase to collagen fibrils. Biochim Biophys Acta 1978; 539: 238–47
  • Walakovits L A., Moore V L., Bhardwaj N, Gallick G S., Lark M W. Detection of stromelysin and collagenase in synovial fluid from patients with rheumatoid arthritis and posttraumatic knee injury. Arthritis Rheum 1992; 35: 35–42
  • Ward R V., Hembry R M., Reynolds J J., Murphy G. The purification of tissue inhibitor of metaHoproteinases-2 from its 72 kDa progelatinase complex Demonstration of the biochemical similarities of tissue inhibitor of metallopro-teinases-2 and tissue inhibitor of metalloproteinases-1. Biochem J 1991a; 278: 179–87
  • Ward R V., Atkinson S J., Slocombe P M., Docherty A J P, Reynolds J J., Murphy G. Tissue inhibitor of metalloproteinases-2 inhibits the activation of 72 kDa progelatinase by fibroblast membranes. Biochim Biophys Acta 1991b; 1079: 242–6
  • Ward R V., Atkinson S J., Reynolds J J., Murphy G. Cell surface-mediated activation of progelatinase A: demonstration of the involvement of the C-terminal domain of progelatinase A in cell surface binding and activation of progelatinase A by primary fibroblasts. Biochem J 1994; 304: 263–9
  • Welgus H G., Jeffrey J J., Eisen A Z., Roswit W T., Stricklin G P. Human skin fibroblast collagenase: interaction with substrate and inhibitor. Collagen Rel Res 1985; 5: 167–79
  • Werb Z, Tremble P M., Behrendtsen O, Crowley E, Damsky C H. Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression. J Cell Biol 1989; 109: 877–89
  • Willenbrock F, Murphy G. Structure-function relationships in the tissue inhibitors of metalloproteinases. Am J Resp Crit Care Med 1994; 150: S156–70
  • Wolfe G C., MacNaul K L., Buechel F F., McDonnell J, Hoerrner L A., Lark M W., Moore V L., Hutchinson N I. Differential in vivo expression of collagenase messenger RNA in synovium and cartilage. Arthritis Rheum 1993; 36: 1540–7
  • Woolley D E., Crossley M J., Evanson J M. Collagenase at sites of cartilage erosion in the rheumatoid joint. Arthritis Rheum 1977; 20: 1231–9
  • Wu J-J, Lark M W., Chun L E., Eyre D R. Sites of stromelysin cleavage in collagen types II, IX, X, and XI of cartilage. J Biol Chem 1991; 266: 5625–8
  • Yocum S A., Lapresti-Morrow L L., Gabel C A., Milici A S., Mitchell P G. Bafilomycin A inhibits IL-1-stimulated proteoglycan degradation by chondrocytes without affecting stromelysin synthesis. Arch Biochem Biophys 1995; 316: 827–35

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.