Degradation of vitronectin by matrix metalloproteinases-1, -2, -3, -7 and -9

Kazushi Imai, Hideo Shikata, Yasunori Okada

Research output: Contribution to journalArticlepeer-review

59 Citations (Scopus)


The susceptibility of vitronectin (Vn) purified from human plasma to digestion by matrix metalloproteinases (MMPs) was examined. MMP-2, -3, -7 and -9 except for MMP-1 degraded Vn into multiple fragments. MMP-7 showed the highest activity to the substrate among these MMPs, digesting 8-, 30- and 44-fold more preferentially than MMP-2, -3 and -9, respectively. These data suggest that MMP-2, -3, -7 and -9 may be responsible for the pathological degradation and/or normal turnover of Vn.

Original languageEnglish
Pages (from-to)249-251
Number of pages3
JournalFEBS Letters
Issue number2-3
Publication statusPublished - 1995 Aug 7


  • Degradation
  • Kinetics
  • Matrix metalloproteinase
  • Vitronectin

ASJC Scopus subject areas

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


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