Immunochemical evidence for increased formation of advanced glycation end products and inhibition by aminoguanidine in diabetic rat lenses.
Water-soluble and urea-soluble protein fractions from control and streptozotocin-diabetic rats were analyzed for AGEs with a CML-specific monoclonal anti-AGE antibody and a polyclonal anti-AGE antibody. AGEs, CML in particular, were significantly increased in the diabetic rats whereas aminoguandine treatment resulted in significant decrease in AGEs. The data also confirm that CML, a glycoxidation product, is a major epitope of AGE structures in lenses.
Matsumoto
K
K
Department of Biochemistry, Kumamoto University School of Medicine, Japan.
Ikeda
K
K
Horiuchi
S
S
Zhao
H
H
Abraham
E C
EC
D000818:Animals; D000918:Antibody Specificity; D003921:Diabetes Mellitus, Experimental / Q000378:metabolism*; D004797:Enzyme-Linked Immunosorbent Assay; D017127:Glycation End Products, Advanced / Q000037:antagonists & inhibitors* / Q000276:immunology; D006146:Guanidines / Q000494:pharmacology*; D007908:Lens, Crystalline / Q000378:metabolism*; D051381:Rats; D017207:Rats, Sprague-Dawley; D013311:Streptozocin
D017127:Glycation End Products, Advanced; D006146:Guanidines; D013311:Streptozocin; C004479:pimagedine