Activation of matrix metalloproteinase 3 (stromelysin) and matrix metalloproteinase 2 ('gelatinase') by human neutrophil elastase and cathepsin G

Yasunori Okada, Isao Nakanishi

Research output: Contribution to journalArticle

136 Citations (Scopus)

Abstract

The ability of human neutrophil elastase and cathepsin G to activate matrix metalloproteinase 3 (MMP-3 = stromelysin) and MMP-2 ('gelatinase') purified from human rheumatoid synovial fibroblasts in culture was examined. The zymogen of MMP-3 (proMMP-3) was activated to full activity with elastase and cathepsin G by limited proteolysis of the molecule into two active forms of Mr ∼ 45000 and Mr ∼ 25000. In contrast, proMMP-2 was not activated at all by these neutrophil serine proteinases, although it was degraded into small fragments. These data suggest that neutrophil elastase and cathepsin G may play an important role in the activation of proMMP-3 in vivo in various inflammatory conditions, but proMMP-2 may be activated in different ways.

Original languageEnglish
Pages (from-to)353-356
Number of pages4
JournalFEBS Letters
Volume249
Issue number2
DOIs
Publication statusPublished - 1989 Jun 5

Keywords

  • Activation
  • Cathepsin G
  • Elastase
  • Extracellular matrix
  • Metalloproteinase
  • Neutrophil enzyme

ASJC Scopus subject areas

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

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