Matrix metalloproteinases and their inhibitors in connective tissue remodeling

The FASEB JournalVolume 5, Issue 8 p. 2145-2154 ReviewsFree to Read Matrix metalloproteinases and their inhibitors in connective tissue remodeling J. Frederick Woessner Jr., Corresponding Author J. Frederick Woessner Jr. n/[email protected] Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, Miami, Florida, 33101 USATo whom correspondence should be sent, at: Department of Biochemistry and Molecular Biology, R-127, University of Miami School of Medicine, P.O. Box 016960, Miami, FL 33101, USA.Search for more papers by this author J. Frederick Woessner Jr., Corresponding Author J. Frederick Woessner Jr. n/[email protected] Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, Miami, Florida, 33101 USATo whom correspondence should be sent, at: Department of Biochemistry and Molecular Biology, R-127, University of Miami School of Medicine, P.O. Box 016960, Miami, FL 33101, USA.Search for more papers by this author First published: 01 May 1991 https://doi.org/10.1096/fasebj.5.8.1850705Citations: 2,379AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat Abstract Matrix metalloproteinases are an important group of zinc enzymes responsible for degradation of the extracellular matrix components such as collagen and proteoglycans in normal embryogenesis and remodeling and in many disease processes such as arthritis, cancer, periodontitis, and osteoporosis. A matrixin family is defined, comprising at least seven members that range in size from Mr 28000 to 92000 and are related in gene sequence to collagenase. All family members are secreted as zymogens that lose peptides of about 10,000 daltons upon activition. Latency is due to a conserved cysteine that binds to zinc at the active center. Latency is overcome by physical (chaotropic agents), chemical (HOCl, mercurials), and enzymatic (trypsin, plasmin) treatments that separate the cysteine residue from the zinc Expression of the metalloproteinases is switched on by a variety of agents acting through regulatory elements of the gene, particularly the AP-1 binding site. A family of protein inhibitors of Mr 28,500 or less binds strongly and stoichiometrically in noncovalent fashion to inhibit members of the family. The serum protein α2-macroglobulin and relatives are also strongly inhibitory.—Woessner, J. F., Jr. Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J. 5: 2145–2154; 1991. Citing Literature Volume5, Issue8May 1991Pages 2145-2154 RelatedInformation