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  • Title: Type X collagen isolated from the hypertrophic cartilage of embryonic chick tibiae contains both hydroxylysyl- and lysylpyridinoline cross-links.
    Author: Orth MW, Luchene LJ, Schmid TM.
    Journal: Biochem Biophys Res Commun; 1996 Feb 15; 219(2):301-5. PubMed ID: 8604981.
    Abstract:
    Hypertrophic cartilage from the tibiotarsus of Day 20 chick embryonic tibiae was found to contain an unusually high concentration of lysylpyridinoline (LP), a nonreducible collagen cross-link normally found only in bone and dentin but not in cartilage. Since type X collagen is abundant in this cartilage, research was conducted to see if type X was the primary source of LP. The 45-kDa pepsin-resistant form of type X was purified by immunoaffinity chromatography. It contained a high concentration of the LP cross-link while type II contained primarily hydroxylysylpyridinoline (HP), the predominant cross-link in cartilage. This, to our knowledge is the first time that type X has been shown directly to form nonreducible cross-links and that a collagen other than type I has a high level of LP. Also, it is interesting that the HP and LP cross-links are found in a collagen that is degraded so rapidly. Possible explanations for these findings are discussed.
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