Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 1992 Apr;50(4):342-9.
doi: 10.1007/BF00301632.

Matrix vesicles are enriched in metalloproteinases that degrade proteoglycans

D D Dean  1 , Z Schwartz, O E Muniz, R Gomez, L D Swain, D S Howell, B D Boyan
Affiliations

Matrix vesicles are enriched in metalloproteinases that degrade proteoglycans

D D Dean et al. Calcif Tissue Int. 1992 Apr.

Abstract

This study examined the presence of extracellular matrix processing enzymes in matrix vesicles produced by rat costochondral resting zone and growth zone chondrocytes in culture. Optimum procedures for the extraction of each enzyme activity were determined. Enzyme activity associated with chondrocyte plasma membrane microsomes was used for comparison. There was a differential distribution of the enzyme activities related to the cartilage zone from which the cells were isolated. Acid and neutral metalloproteinase (TIMP), plasminogen activator, and beta-glucuronidase were highest in the growth zone chondrocyte (GC) membrane fractions when compared with matrix vesicles and plasma membranes isolated from resting zone chondrocyte (RC) cultures. There was a threefold enrichment of total and active acid metalloproteinase in GC matrix vesicles, whereas no enrichment in enzyme activity was observed in RC matrix vesicles. Total and active neutral metalloproteinase were similarly enriched twofold in GC matrix vesicles. TIMP, plasminogen activator, and beta-glucuronidase activities were highest in the plasma membranes of both cell types. No collagenase, lysozyme, or hyaluronidase activity was found in any of the membrane fractions. The data indicate that matrix vesicles are selectively enriched in enzymes which 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.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Lab Invest. 1989 Mar;60(3):320-30 - PubMed
    1. Biochim Biophys Acta. 1990 Sep 7;1027(3):278-86 - PubMed
    1. Clin Orthop Relat Res. 1973 Jan-Feb;(90):191-200 - PubMed
    1. J Orthop Res. 1987;5(1):128-32 - PubMed
    1. Endocrinology. 1988 Jun;122(6):2851-60 - PubMed

Publication types

LinkOut - more resources