Matrix vesicles contain metalloproteinases that degrade proteoglycans

David D. Dean, Z. V.I. Schwartz, Ofelia E. Muniz, Ruben Gomez, Larry D. Swain, David S. Howell, Barbara D. Boyan

Research output: Contribution to journalArticle

23 Scopus citations

Abstract

This study explored whether extracellular matrix processing enzymes are present in matrix vesicles produced by rat costochondral resting zone and growth zone chondrocytes in culture. It was found that there was a differential distribution of enzyme activities related to the cartilage zone from which the cells were isolated. There was a 3-fold enrichment of total and active acid metalloproteinase in growth zone chondrocyte (GC) matrix vesicles whereas no enrichment in enzyme activity was observed in resting zone chondrocyte (RC) matrix vesicles. Total and active neutral metalloproteinase were similarly enriched 2-fold in GC matrix vesicles. TIMP, plasminogen activator and β-glucuronidase activities were highest in the plasma membranes of both cell types. No collagenase, lysozyme, or hyaluronidase activity was found. The data indicate that matrix vesicles are selectively enriched in enzymes that degrade proteoglycans. The highest concentrations of these enzymes are found in matrix vesicles produced by growth zone chondrocytes, suggesting that this may be a mechanism by which the more differentiated cell modulates the matrix for calcification.

Original languageEnglish (US)
Pages (from-to)172-176
Number of pages5
JournalBone and Mineral
Volume17
Issue number2
DOIs
StatePublished - May 1992

Keywords

  • Matrix vesicles
  • Metalloproteinases
  • TIMP

ASJC Scopus subject areas

  • Surgery
  • Biochemistry
  • Endocrinology

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