Studies on the structure of glyceraldehyde-modified proteins and the mechanism underlying the pathogenesis of diabetes and ageing

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MG-H1, GLAP, argpyrimidine, and 2-(4-acetylamino-4-carboxybutylamino)-5-(5-acetylamino-5-carboxy-pentyl)-7-hydroxy-3, 4-dihydro-pyrido[3,2-d]pyri-midin-5-ium (P4) were identified as AGEs (advanced glycation end products) by the reaction of the N^α-acetyllysine, N^α-acetylarginine, and glyceraldehydes (GLA). Furthermore, glyceraldehyde, glusocone, 3-deoxyglucosone (3-DG), 3-deoxyxylosone, tetrosone, triosone, 3-deoxytetrosone, glyoxal and methylglyoxal were identified by the incubation of glucose or fructose. We found that 3-DG caused apoptosis through the endoplasmic reticulum stress for mouse macrophage cell line, and clarified the significance of the carbonyl stress on the mechanism underlying the pathogenesis of diabetes complication such as arteriosclerosis and ageing. GLAP, and analogs of MG-H1, argpyrimidine, and P4 were also generated from the reaction of GLA, creatine, and N^α-acetyllysine. On the other hand, we revealed that protein modified by GLA suppressed interferon β stimulated gene expression.