Susceptibility of tenascin to degradation by matrix metalloproteinases and serine proteinases

Kazushi Imai, Moriaki Kusakabe, Teruyo Sakakura, Isao Nakanishi, Yasunori Okada

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The degradation of tenascin purified from human melanoma cells was examined by treatment with matrix metalloproteinases (MMPs) and serine proteinases. Among eight different types of proteinases examined, MMP-1, -3, and -7, cathepsin G and leukocyte elastase could digest tenascin, but MMP-2, MMP-9 and thrombin did not. This suggests that tenascin may be readily catabolized by extracellular matrix-degrading proteinases found in the pathophysiological conditions.

Original languageEnglish
Pages (from-to)216-218
Number of pages3
JournalFEBS Letters
Issue number2
Publication statusPublished - 1994 Sep 26



  • Matrix metalloproteinase
  • Serine proteinase
  • Tenascin

ASJC Scopus subject areas

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

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