グリケーションと老化(<特集>老化とアフェレシス)

概要

論文の詳細を見る
Accumulation of advanced glycation end-produds(AGE) of the Maillard reaction in tissue proteins increases with the pathogenesis of diabetic complications and atherosclerosis. This strongly suggests an association of AGE for the development of age-related disorders. Since this reaction proceeds non-enzymatically (almost all of the proteins are in accordance with reducing sugar concentration and the half-life of each protein), it is different from enzymatic post-translational modification such as phosphorylation and acetylation of some specific proteins. Although the formation of Amadori products, relatively stable intermediates of the reaction, is reversible, the formation of AGE is on irreversible reaction, indicating that AGE-formation causes the irreversible denature of proteins in vivo. The AGE research originally began in the field of food chemistry and has expanded to in vivo study since 1990 because of the development of polydonaland monoclonal antibodies against AGE-modified proteins. These immunochemical approaches have greatly contributed to understanding the biological significance of AGE in the pathogenesis of age-enhanced diseases. Furthermore, several AGE inhibitors have shown promise in model systems for inhibiting both the Maillard reaction and the development of diabetic complications.
日本アフェレシス学会の論文
2004-05-31