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.
@article{Vater_1979, title={Native cross-links in collagen fibrils induce resistance to human synovial collagenase}, volume={181}, ISSN={0264-6021}, url={http://dx.doi.org/10.1042/bj1810639}, DOI={10.1042/bj1810639}, number={3}, journal={Biochemical Journal}, publisher={Portland Press Ltd.}, author={Vater, C A and Harris, E D and Siegel, R C}, year={1979}, month=sep, pages={639–645} }