Inactivation of tissue inhibitor of metalloproteinases by neutrophil elastase and other serine proteinases

FEBS Letters

Nakanishi, Isao¹  Okada, Yasunod¹  Travis, James³  Hayakawa, Taro⁵  Watanabe, Shoji⁴  Kishi, Jun-ichi⁵  Nagase, Hideaki²  Watorek, Wieslaw³ 

[1] Department of Pathology and School of Medicine, Kanazawa University, 13-1 Takara-machi, Kanazawa 920, Japan;Department of Biochemistry, University of Kansas Medical Center, Kansas City, KS 66103, USA;Department of Biochemistry, University of Georgia, Athens, GA 30602, USA;Orthopedic Surgery, School of Medicine, Kanazawa University, 13-1 Takara-machi, Kanazawa 920, Japan;Department of Biochemistry, School of Dentistry, Aichi-Gakuin University, Suemori-dori, Chikusaku, Nagoya 464, Japan

关键词: Tissue inhibitor of metalloproteinases;    Neutrophil elastase;    Metalloproteinase;    Extracellular matrix;   

DOI  :  10.1016/0014-5793(88)80817-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown