Susceptibility of tenascin to degradation by matrix metalloproteinases and serine proteinases

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

Research output: Contribution to journalArticlepeer-review

70 Citations (Scopus)


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 Sept 26
Externally publishedYes


  • Matrix metalloproteinase
  • Serine proteinase
  • Tenascin

ASJC Scopus subject areas

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


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