Immunochemical detection of advanced glycosylation end products in vivo.

摘要: Reducing sugars react with protein amino groups to form a diverse group of protein-bound moieties fluorescent and cross-linking properties. These compounds, called advanced glycosylation end products (AGEs), have been implicated in the structural functional alterations proteins that occur during aging long-term diabetes. Although several AGEs identified on basis de novo synthesis tissue isolation procedures, measurement AGE compounds vivo has remained difficult. As an approach study formation vivo, we prepared polyclonal antiserum epitope(s) which forms vitro after incubation glucose ribonuclease (RNase). This proved suitable for detection vivo. Both diabetic serum known contain elevated levels readily competed antibody binding. Cross-reactivity studies revealed presence common glucose. Cross-reactive epitopes also formed 6-phosphate or fructose. data suggest appear immunological epitope cross-reacts vitro, supporting concept immunologically similar structures from different (Horiuchi, S., Araki, N., Morino, Y. (1991) J. Biol. Chem. 266, 7329-7332). None AGEs, such as 4-furanyl-2-furoyl-1H-imidazole, 1-alkyl-2-formyl-3,4-diglycosylpyrrole, pyrraline, carboxymethyllysine, pentosidine, were found compete binding anti-AGE antibody. further dominant reaction under native conditions is distinct structurally defined described date.