Open AccessThe complex between a tissue inhibitor of metalloproteinases (TIMP‐2) and 72‐kDa progelatinase is a metalloproteinase inhibitor
Author(s) -
KOLKENBROCK Hansjörg,
ORGEL Dagmar,
HECKERKIA Adelheid,
NOACK Wolfgang,
ULBRICH Norbert
Publication year - 1991
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1991.tb16080.x
Subject(s) - matrix metalloproteinase , gelatinase , tissue inhibitor of metalloproteinase , collagenase , chemistry , gelatinase a , interstitial collagenase , metalloproteinase , enzyme , biochemistry
Human rheumatoid synovial cells in culture secrete both 72‐kDa progelatinase and a complex consisting of 72‐kDa progelatinase and a 24‐kDa inhibitor of metalloproteinases, TIMP‐2. In addition, the culture medium contains TIMP‐1, the classical inhibitor of metalloproteinases, with a molecular mass of 30 kDa. TIMP‐1 does not form a complex with free 72‐kDa progelatinase. Free progelatinase and progelatinase complexed with TIMP‐2 can be activated with the organomercury compound p ‐aminophenylmercury acetate. The activated complex shows less than 10% the enzyme activity of activated free gelatinase. The progelatinase – TIMP‐2 complex could be shown to be an inhibitor for other metalloproteinases, such as gelatinase and collagenase secreted by human rheumatoid synovia fibroblasts, as well as for the corresponding enzymes from human neutrophils.