Metalloproteinase inhibitors from bovine cartilage and body fluids.
Affiliation
Cell Physiology Department, Strangeways Research Laboratory, CambridgeIssue Date
1984-02-15
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Inhibitors of the mammalian metalloproteinases, collagenase, proteoglycanase and gelatinase were isolated from bovine cartilage (extracts and culture medium) and bovine amniotic fluid and serum. These inhibitors either bind or do not bind to concanavalin-A--Sepharose, with Mr (gel filtration) of about 30 000 and 20 000, respectively. Cartilage and chondrocyte culture media contained only concanavalin-A-binding inhibitors whereas cartilage extracts contained only a non-binding inhibitor: serum and amniotic fluid contained both forms of inhibitory activities. In moist biochemical respects, particularly in their abilities to inhibit metalloproteinases, all of the inhibitors were found to be similar. It is concluded that the forms of the inhibitors that differ in Mr may be closely related to the tissue inhibitor of metalloproteinases (TIMP) previously purified from rabbit and human sources. These findings help to clarify other studies on collagenase inhibitors and support the concept that TIMP-like inhibitors may be important in the control of connective tissue degradation.Citation
Metalloproteinase inhibitors from bovine cartilage and body fluids. 1984, 139 (1):75-80 Eur J BiochemJournal
European Journal of BiochemistryDOI
10.1111/j.1432-1033.1984.tb07978.xPubMed ID
6321174Type
ArticleLanguage
enISSN
0014-2956ae974a485f413a2113503eed53cd6c53
10.1111/j.1432-1033.1984.tb07978.x