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    Metalloproteinase inhibitors from bovine cartilage and body fluids.

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    Authors
    Bunning, R
    Murphy, G
    Kumar, Shant
    Phillips, P
    Reynolds, J
    Affiliation
    Cell Physiology Department, Strangeways Research Laboratory, Cambridge
    Issue Date
    1984-02-15
    
    Metadata
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    Abstract
    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 Biochem
    Journal
    European Journal of Biochemistry
    URI
    http://hdl.handle.net/10541/123967
    DOI
    10.1111/j.1432-1033.1984.tb07978.x
    PubMed ID
    6321174
    Type
    Article
    Language
    en
    ISSN
    0014-2956
    ae974a485f413a2113503eed53cd6c53
    10.1111/j.1432-1033.1984.tb07978.x
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