Inhibitor of human collagenase from cultures of human tendon

A potent inhibitor of human collagenases, released from human tendon explants in culture, has been purified and partially characterized. The tendon inhibitor has an estimated molecular weight of 25,000. It is relatively heat-stable but undergoes loss of activity following exposure to trypsin. It inh...

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Bibliographic Details
Published inThe Journal of biological chemistry Vol. 254; no. 8; pp. 3045 - 3053
Main Authors Vater, C.A., Mainardi, C.L., Harris, E.D.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 25.04.1979
American Society for Biochemistry and Molecular Biology
Subjects
Cells, Cultured
Clostridium - enzymology
Humans
Kinetics
Microbial Collagenase - antagonists & inhibitors
Molecular Weight
Pancreatic Elastase - analysis
Protease Inhibitors - isolation & purification
Protease Inhibitors - physiology
Species Specificity
Tendons - physiology
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Summary:A potent inhibitor of human collagenases, released from human tendon explants in culture, has been purified and partially characterized. The tendon inhibitor has an estimated molecular weight of 25,000. It is relatively heat-stable but undergoes loss of activity following exposure to trypsin. It inhibits trypsin-activated rheumatoid synovial collagenase as well as the enzyme obtained from polymorphonuclear leukocytes. No inhibition of collagenase from Clostridium histolyticum (clostridiopeptidase A, EC 3.4.24.3) was noted. This collagenase inhibitor may be a factor in the regulation of extracellular connective tissue catabolism.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(17)30180-1