ISOLATION AND IDENTIFICATION OF GLYCATED AMINOPHOSPHOLIPIDS FROM RED-CELLS AND PLASMA OF DIABETIC BLOOD

Glycosylation is a major pathway for posttranslational modification of tissue protein and begins with nonenzymatic addition of carbohydrate to the primary amino groups. Excessive glycation of tissue protein has been implicated in the pathogenesis of diabetes and ageing, While gly cation of aminophospholipids has also been postulated, glycated aminop hospholipids have not been isolated. Using normal phase HPLC with on-l ine electrospray mass spectrometry we found glycated ethanolamine phos pholipids to make up 10-16% of the total phosphatidylethanolamine (PE) of the red blood cells and plasma of the diabetic subjects, The corre sponding values for glycated PE of control subjects were 1-2%.