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

Producción científica: Articlerevisión exhaustiva

31 Citas (Scopus)


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.

Idioma originalEnglish (US)
Páginas (desde-hasta)172-176
Número de páginas5
PublicaciónBone and Mineral
EstadoPublished - may 1992

ASJC Scopus subject areas

  • Endocrinology
  • Biochemistry
  • Surgery


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