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

Yasunod Okada, Shoji Watanabe, Isao Nakanishi, Jun ichi Kishi, Taro Hayakawa, Wieslaw Watorek, James Travis, Hideaki Nagase

Research output: Contribution to journalArticle

156 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)157-160
Number of pages4
JournalFEBS Letters
Volume229
Issue number1
DOIs
Publication statusPublished - 1988 Feb 29

Keywords

  • Extracellular matrix
  • Metalloproteinase
  • Neutrophil elastase
  • Tissue inhibitor of metalloproteinases

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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