Non-enzymatic interactions of glyoxylate with lysine, arginine, and glucosamine: A study of advanced non-enzymatic glycation like compounds

Glyoxylate is a 2 carbon aldo acid that is formed in hepatic tissue from glycolate. Once formed, the molecule can be converted to glycine by alanine–glyoxylate aminotransferase (AGAT). In defects of AGAT, glyoxylate is transformed to oxalate, resulting in high levels of oxalate in the body. The objective of this study was 2-fold. First, it was to determine, if akin to d-glucose, d-fructose or dl-glyceraldehyde, glyoxylate was susceptible to non-enzymatic attack by amino containing molecules such as lysine, arginine or glucosamine. Second, if by virtue of its molecular structure and size, glyoxylate was as reactive a reagent in non-enzymatic reactions as dl-glyceraldehyde; i.e., a glycose that we previously demonstrated to be a more effective glycating agent than d-glucose or d-fructose. Using capillary electrophoresis (CE), high performance liquid chromatography and UV and fluorescence spectroscopy, glyoxylate was found to be a highly reactive precursor of advanced glycation like end products (AGLEs) and a more effective promoter of non-enzymatic end products than d-glucose, d-fructose or dl-glyceraldehyde.

Advanced glycation end products (AGEs) are a complex and heterogenous group of compounds formed by the non-enzymatic reaction of reducing sugars/certain carbonyl containing compounds with amino acids and proteins.Figure optionsDownload as PowerPoint slide