Aging, and crosslinking in mammlian collagen.
The amount and type of borohydride-reducible crosslinks in collagen have been examined as a function of animal age. In a variety of bovine, canine and human tissues the level of redicible crosslinks decreases with time and the ratios of individual compounds change. There is both tissue and species specificity in the extent of these changes. A decrease in the level of reducible crosslinks correlates with the cessation of growth. Loss of reducible crosslinks does not imply a small total number of crosslinks since physical changes with age imply the opposite. We conclude that reducible crosslinks are converted to a stable nonreducible state and the persistence of low levels of reducible crosslinks may be indicative of a low level of turnover in the tissue. Changes in ratios of reducible crosslinks are of doubtful functioal significance and may simply reflect variation in post-translational modification of lysine residues.
D000293:Adolescent; D000328:Adult; D000368:Aged; D000375:Aging; D000818:Animals; D001132:Arm; D002417:Cattle; D002648:Child; D002675:Child, Preschool; D003094:Collagen / Q000378:metabolism*; D003315:Cornea; D004151:Dipeptides; D004285:Dogs; D004388:Dura Mater; D004591:Electrophoresis, Polyacrylamide Gel; D005333:Fetus; D005528:Foot; D005552:Forelimb; D006801:Humans; D006901:Hydroxylysine / Q000031:analogs & derivatives; D007223:Infant; D007231:Infant, Newborn; D008875:Middle Aged; D010084:Oxidation-Reduction; D013710:Tendons
D004151:Dipeptides; D006901:Hydroxylysine; D003094:Collagen