The role of mass spectrometry in the study of non-enzymatic protein glycation in diabetes: an update

Mass Spectrometry Reviews
A LapollaP Traldi

Abstract

Recent studies on non-enzymatic protein glycation are reviewed, and results are critically discussed. Advanced glycation end products (AGE) levels in the body reflect a balance between their formation and catabolism. AGE proteolysis leads to the formation of low-molecular-weight AGE (AGE peptides) that are normally excreted in urine. In the case of diabetic disease and/or renal failure, AGE peptides accumulate in plasma. Because of their high reactivity, these compounds have been thought to play a role in the progression of chronic complications. The structural identification of these compounds is particularly important, and a strategy has been designed for their possible definition. A series of experiments has been devoted to the study of the enzymatic degradation products of in vitro glycated human serum albumin (HSA). This approach, based on different MS methods (LC/ESI/MS, LC/ESI/FTMS, MALDI), led to the detection of the glycated peptides generated by digestion of HSA. A further study was devoted to the possible identification of the peptides identified in the glycated HSA digestion products in the plasma of diabetic and nephropatic subjects. No glycated HSA digestion products were found in plasma samples of the subjects un...Continue Reading

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