N.epsilon.-(Carboxymethyl)lysine Is a Dominant Advanced Glycation End Product (AGE) Antigen in Tissue Proteins

Citations Over TimeTop 1% of 1995 papers

Abstract

Advanced glycation end products (AGEs) and glycoxidation products are formed during Maillard or browning reactions between sugars and proteins and are implicated in the pathophysiology of aging and the complications of diabetes. To determine the structure of AGEs, antibodies were prepared to protein browned by incubation with glucose and used in ELISA assays to measure AGEs formed in model reactions between bovine serum albumin (BSA) or N alpha-acetyllysine and glucose, fructose, or glyoxal. AGEs were formed from glucose and fructose only under oxidative conditions, but from glyoxal under both oxidative and antioxidative conditions. Gel permeation chromatographic analysis indicated that a similar AGE was formed in reactions of N alpha-acetyllysine with glucose, fructose, and glyoxal and that this AGE co-eluted with authentic N alpha-acetyl-N epsilon-(carboxymethyl)lysine. Amino acid analysis of AGE proteins revealed a significant content of N epsilon-(carboxymethyl)lysine (CML). In ELISA assays using polyclonal antibodies against AGE proteins, CML-BSA (approximately 25 mol of CML/mol of BSA), prepared by chemical modification of BSA, was a potent inhibitor of the recognition of AGE proteins and of AGEs in human lens proteins. We conclude that AGEs are largely glycoxidation products and that CML is a major AGE recognized in tissue proteins by polyclonal antibodies to AGE proteins.

Related Papers

• Advanced glycation end product (AGE) modified proteins in tears of diabetic patients.(2010)
• → Inihbition of Protein Glycation with Varying Concentrations of Lysine(2008)4 cited
• → Lysine proximity significantly affects glycation of lysine-containing collagen model peptides(2011)4 cited
• Glycation of lysozyme in a restricted water environment.(1991)
• → LEVELS OF FRUCTOSYLLYSINE IN COLLAGEN ARE LOW COMPARED WITH THE LOSS OF LYSINE IN DIABETIC RATS: INVOLVEMENT OF OXIDATION IN INCREASED CROSS‐LINKING(1997)