Bailey A J, Sims T J
Biochem J. 1976 Feb 1;153(2):211-5. doi: 10.1042/bj1530211.
Both the type I and type III collagens present in embryonic dermis are stabilized by the intermolecular cross-link, hydroxylysino-5-oxonorleucine, derived from hydroxylysine-aldehyde, although the type I collagen possesses a significant proportion of dehydrohydroxylysinonorleucine. However, concurrent with the change in the proportion of the two types of collagen during postnatal development there is a change-over with both type I and III collagens to the labile cross-link, dehydrohydroxylysinonorleucine, derived from lysine aldehyde. The results indicate that the change in the nature of the cross-link with development is determined primarily by the change in the extent of hydroxylation of the lysine residues in the terminal non-helical regions rather than being due to the change in the type of collagen.
胚胎真皮中存在的I型和III型胶原蛋白都通过源自羟赖氨酸醛的分子间交联——羟赖氨酰-5-氧代正亮氨酸得以稳定，尽管I型胶原蛋白含有相当比例的脱氢羟赖氨酰正亮氨酸。然而，在出生后发育过程中，随着两种胶原蛋白比例的变化，I型和III型胶原蛋白都转而形成源自赖氨酸醛的不稳定交联——脱氢羟赖氨酰正亮氨酸。结果表明，随着发育交联性质的变化主要由末端非螺旋区域赖氨酸残基羟基化程度的变化决定，而非胶原蛋白类型的变化。
