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Inactivation of tissue inhibitor of metalloproteinases by neutrophil elastase and other serine proteinases
Author(s) -
Okada Yasunod,
Watanabe Shoji,
Nakanishi Isao,
Kishi Jun-ichi,
Hayakawa Taro,
Watorek Wieslaw,
Travis James,
Nagase Hideaki
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80817-2
Subject(s) - cathepsin g , elastase , plasmin , matrix metalloproteinase , pancreatic elastase , chemistry , neutrophil elastase , trypsin , cathepsin , serine , biochemistry , serine proteinase inhibitors , in vivo , microbiology and biotechnology , serine protease , enzyme , biology , inflammation , immunology , protease
Tissue inhibitor of metalloproteinases (TIMP) from cultured bovine dental pulp inhibits human rheumatoid synovial matrix metalloproteinase 3 (MMP‐3) with a stoichiometry of 1:1 on a molar basis. Among the serine proteinases examined, human neutrophil elastase, trypsin and α‐chymotrypsin destroyed the inhibitory activity of TIMP against MMP‐3 by degrading the inhibitor molecule into small fragments. In contrast, the inhibitory activity of TIMP was not significantly reduced by the actions of cathepsin G, pancreatic elastase and plasmin. These data indicate that neutrophils which infiltrate tissues in various inflammatory conditions may play an important role in regulating TIMP activity in vivo through the action of neutrophil elastase.