Aging and cross-linking of skin collagen.
This report represents a clear demonstration of a cross-link in collagen whose abundance is related to chronological aging of an organism. Recently its structure was identified as histidinohydroxylysinonorleucine. Quantification of the cross-link in various aged samples of bovine and human skin indicate that it rapidly increases from birth through maturation. Subsequently, a steady increase occurs with aging, approaching 1 mole/mole of collagen. This compound seems to be related to the relative proportions of soluble to insoluble collagen from skin in neutral salt, dilute acid, and denaturing aqueous solvents (higher concentration in the insoluble portion). It is absent from other major collagenous tissues such as dentin, bone and tendon.
D000328:Adult; D000368:Aged; D000375:Aging; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D003094:Collagen / Q000502:physiology; D003432:Cross-Linking Reagents; D006639:Histidine / Q000502:physiology; D006801:Humans; D007223:Infant; D008239:Lysine / Q000502:physiology; D046911:Macromolecular Substances; D009646:Norleucine / Q000502:physiology; D012867:Skin / Q000032:analysis; D012879:Skin Physiological Phenomena
D000596:Amino Acids; D003432:Cross-Linking Reagents; D046911:Macromolecular Substances; D006639:Histidine; D009646:Norleucine; D003094:Collagen; D008239:Lysine