Levels of metalloproteases and tissue inhibitor of metalloproteases in human osteoarthritic cartilage

D. D. Dean, W. Azzo, J. Martel-Pelletier, J. P. Pelletier, J. F. Woessner

Research output: Contribution to journalArticle

46 Scopus citations

Abstract

Human articular cartilage contains 2 distinct metalloproteases which degrade proteoglycan. One protease acts optimally at pH 5.3 and the other at pH 7.2. In addition, cartilage contains a tissue inhibitor of metalloproteases (TIMP) that inhibites both proteases. Methods have been developed for the estimation of metalloproteases and TIMP in extracts of cartilage prepared in buffered 2 M guanidine-HCl. In osteoarthritic cartilage, levels of the 2 metalloproteases increase 3-fold or more, while the levels of TIMP remains constant. It is postulated that a balance is maintained between inhibitor and metalloprotease levels in normal cartilage and that in osteoarthritis increased secretion of proteases upsets this balance and results in degradation of the extracellular matrix.

Original languageEnglish (US)
Pages (from-to)43-44
Number of pages2
JournalJournal of Rheumatology
Volume14
Issue numberSPEC. NO.
StatePublished - Jan 1 1987

ASJC Scopus subject areas

  • Rheumatology
  • Immunology and Allergy
  • Immunology

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    Dean, D. D., Azzo, W., Martel-Pelletier, J., Pelletier, J. P., & Woessner, J. F. (1987). Levels of metalloproteases and tissue inhibitor of metalloproteases in human osteoarthritic cartilage. Journal of Rheumatology, 14(SPEC. NO.), 43-44.