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. 1979 Sep 1;181(3):639–645. doi: 10.1042/bj1810639

Native cross-links in collagen fibrils induce resistance to human synovial collagenase.

C A Vater, E D Harris Jr, R C Siegel
PMCID: PMC1161203  PMID: 42386

Abstract

A model system consisting of highly purified lysyl oxidase and reconstituted lathyritic chick bone collagen fibrils was used to study the effect of collagen cross-linking on collagen degradation by mammalian collagenase. The results indicate that synthesis of approx. 0.1 Schiff-base cross-link per collagen molecule results in a 2--3-fold resistance to human synovial collagenase when compared with un-cross-linked controls or samples incubated in the presence of beta-aminopropionitrile to inhibit cross-linking. These results confirm previous studies utilizing artificially cross-linked collagens, or collagens isolated as insoluble material after cross-linking in vivo, and suggest that increased resistance to collagenase may be one of the earliest effects of cross-linking in vivo. The extent of intermolecular cross-linking among collagen fibrils may provide a mechanism for regulating the rate of collagen catabolism relative to synthesis in normal and pathological conditions.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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