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. 1997 Dec 1;328(Pt 2):665–668. doi: 10.1042/bj3280665

Oligomeric forms of the 148 kDa cartilage matrix protein.

R Zeineldin 1, S Ekborg 1, J Baker 1
PMCID: PMC1218969  PMID: 9371729

Abstract

The 148 kDa cartilage matrix protein (CMP), composed of three disulphide-bonded subunits, is a cartilage-specific glycoprotein found in association with fibrils of type II collagen and possibly with aggrecan. It is probable that CMP serves a structural role. As cartilage ages, an increasing proportion of the CMP becomes insoluble and resistant to extraction. In the present study, the isolation of CMP has been improved by inclusion of a hydrophobic chromatography step, thereby removing the remaining traces of collagen and proteoglycan. Evidence of self-association of CMP is presented. Higher-molecular-mass forms of CMP, ranging in apparent molecular mass from 270 to 510 kDa and separated by SDS/PAGE, were located using a specific anti-CMP monoclonal antibody. Both CMP and its oligomeric forms are reducible to 52 kDa subunits, and only trace amounts of other proteins. The formation of oligomers, which may constitute 23% of the total cartilage matrix protein, could occur as a byproduct of the normal biosynthetic trimerization of subunits. Alternatively, the oligomers may represent a step toward the age-related cross-linking and insolubilization of CMP.

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Selected References

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