Chemistry of the collagen cross-links. Nature of the cross-links in the polymorphic forms of dermal collagen during development.
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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001894:Borohydrides; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D003094:Collagen / Q000032:analysis / Q000302:isolation & purification; D006901:Hydroxylysine / Q000031:analogs & derivatives / Q000032:analysis; D008297:Male; D009646:Norleucine / Q000031:analogs & derivatives / Q000032:analysis; D010504:Periodic Acid; D012867:Skin / Q000032:analysis* / Q000196:embryology / Q000254:growth & development
D000596:Amino Acids; D001894:Borohydrides; D010504:Periodic Acid; D006901:Hydroxylysine; D009646:Norleucine; D003094:Collagen