Effect of age on collagen fibril formation.
The rates of collagen fibril formation are, under otherwise identical conditions, a function of the age of the acid-soluble rat tail tendon collagen utilized. The rate is most rapid with young adult (165 day) collagen, which exhibits no induction period before collagen multimerization begins. In contrast, 21-day collagen exhibits both a 30% slower rate and an induction period. Collagens from older animals also have age-dependent fibril formation rates going from a maximum at 165 days to 80% of that for 1,100-day-old material. These age-related differences in collagen fibril formation kinetics appear to be related to the degree of cross-linking of the collagen involved.
D000375:Aging; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D003094:Collagen / Q000096:biosynthesis*; D066298:In Vitro Techniques; D007700:Kinetics; D051381:Rats; D012995:Solubility
D000596:Amino Acids; D003094:Collagen