Ageing promotes the increase of early glycation Amadori product as assessed by epsilon-N-(2-furoylmethyl)-L-lysine (furosine) levels in rodent skin collagen. The relationship to dietary restriction and glycoxidation.

Glucose has been implicated in the aging process by its ability to react nonenzymatically with long-lived proteins like collagen to produce advanced glycosylated end-products (AGEs). In the initial phase of this reaction, referred to as glycation, glucose reacts with the free amino group of proteins resulting in Schiff base formation followed by rearrangement to an Amadori product. Since the Amadori product is transient due to its conversion to other products as well as its reversibility to the initial products, glycation as an age-related marker in collagen has questionable significance. In human studies, glycation of collagen has been found to increase modestly with age. In rodent studies, results are conflicting due to differences in methodology. Thus, it has been concluded that collagen glycation either does not vary or increases modestly with age. In the present study, a C8 HPLC column was used to measure Amadori product formation as the acid-hydrolyzed breakdown product furosine in the skin of rats and mice. Surprisingly, levels were found to increase at a rapid rate during aging of rodents. Impurity of the furosine peak from the use of crude acid-hydrolyzed skin samples was ruled-out because reductive properties and spectroscopic profiles matched those previously described for furosine. In the present study, glycemia was found important in furosine formation as shown by the glycation lowering effects of dietary restriction on collagen. Decreased collagen turnover probably plays a substantial role in explaining the age-related increase in furosine levels in rodent skin collagen.