The role of oxidative cross-link stabilization in increased collagen polymerization in food deprived rats.

It was demonstrated that 50% food restriction for a period of two years causes a considerable increase in gamma-chain polymers of rat skin collagen. The polymerization reaction occurs in both main skin collagen types, e.g. collagen type I and III. Concomitantly increased amounts of alpha-aminoadipic acid were found in preparations of food deprived rats as compared to the controls. It appears that this unusual amino acid arises from the oxidative stabilization of dehydro hydroxylysinonorleucine, the main intermolecular collagen cross-link present in the skin. It is suggested that the degree of polymerization of skin collagen in fasted animals is the result of reutilization of more soluble collagen forms.