Native cross-links in collagen fibrils induce resistance to human synovial collagenase.
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.
D000629:Aminopropionitrile / Q000494:pharmacology; D000818:Animals; D001172:Arthritis, Rheumatoid / Q000201:enzymology; D001842:Bone and Bones / Q000378:metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D002645:Chickens; D003094:Collagen / Q000378:metabolism*; D003432:Cross-Linking Reagents; D006801:Humans; D003012:Microbial Collagenase / Q000378:metabolism*; D008954:Models, Biological; D008249:Protein-Lysine 6-Oxidase; D013582:Synovial Fluid / Q000201:enzymology
D003432:Cross-Linking Reagents; D000629:Aminopropionitrile; D003094:Collagen; D008249:Protein-Lysine 6-Oxidase; D003012:Microbial Collagenase