Extracts of human articular cartilage contain an inhibitor of tissue metalloproteinases

D. D. Dean, J. F. Woessner

Research output: Contribution to journalArticlepeer-review

73 Scopus citations

Abstract

When human articular cartilage is extracted with 2M-guanidinium hydroxychloride at pH 7.5, an inhibitor is obtained that blocks the activity of three metalloproteinases, including collagenase. Molecular-sieve chromatography of the inhibitor gives an M(r) value for the inhibitor of 28 500. The inhibitor is stable to heat (60°C, 1 h) and acid (pH2, 24°C, 10 min). It is destroyed by trypsin and by reduction and alkylation. It is slowly inactivated by aminophenylmercuric acetate. It binds to concanavalin A-Sepharose and it eluted with α-D-l-O-methyl glucopyranoside. Complexes of enzyme and inhibitor are not re-activated by aminophenylmercuric acetate and only partially so by high levels of trypsin. These properties indicate that this inhibitor is a member of the TIMP (tissue inhibitor of metalloproteinases) class. Such an inhibitor previously found in tissue culture and amniotic fluid, is now shown to be directly extractable from tissue.

Original languageEnglish (US)
Pages (from-to)277-280
Number of pages4
JournalBiochemical Journal
Volume218
Issue number1
DOIs
StatePublished - 1984

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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