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Advanced glycation endproduct formation in rat tissue proteins

The object of our study was to follow time-relationship of advanced glycation endproducts (AGE) formation on tissues related to the late complications of diabetes. Alloxan-induced diabetic rats (n=12) and age related controls (n=7) were analyzed after 1 and 5 months of disease duration. The tissue specimens: eye lens, aortic and tendon collagen were analyzed by fluorescence method (335/385 nm ex/em), competitive ELISA method and SDS-electrophoresis on homogeneous and gradient resolving gel. The fluorescence of alkali-soluble lens proteins was significantly higher in diabetics with 5-month disease duration compared to age-matched controls (3.251.02 vs 1.610.17 FU/mg, p<0.001). Lens from diabetic animals had 30% and lens from controls had 2.5% of high molecular weight polymers (HMW-protein). Aortic AGE-collagen was significantly different between diabetics and the controls (206.616.7 vs 127.35.5 U/mg, p<0.001). SDS-electrophoresis analysis of aortic and tendon collagen showed collagen fragments resistant to protease digestion. AGE-modification of eye lens proteins and proteins of vascular collagen is very intense and is of quantitative significance in diabetes. In nondiabetic controls these processes are of reduced intensity and the reaction does not have the same quantitative significance.

Advanced glycation product; collagen; diabetes

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