THE ASSESSMENT OF PROTEIN GLYCATION IN HUMAN ATHEROSCLEROTIC PLAQUES BY AFFINITY-CHROMATOGRAPHY

Human atherosclerotic plaques are characterized by a massive depositio n of lipid within arterial walls, The lipids accumulated are partly ox idized, as assessed by gas chromatography of lipids and their oxidatio n products, Both advancing age and diabetes mellitus are associated wi th an increased prevalence and severity of atherosclerosis, In diabete s mellitus the development of secondary complications appear to be inc reased by poor glucose control, Indeed, the post-translational modific ation of protein by non-enzymatic glycation may provide the link betwe en abnormal glucose control and diabetic complications, For atheroscle rosis however, the relationship between glucose control and disease is unclear, with evidence available to support and discount such a link, To study protein glycation in a condition associated with a significa nt level of lipid oxidation products poses several methodological prob lems, most of which are associated with interference by lipid-derived aldehydes, Many chemical assays of protein glycation monitor aldehydic products common to the chemistry of both protein glycation and lipid oxidation, Studies of protein glycation in human atheroma, obtained at necropsy, are presented which make use of a commercially available bo ronic acid affinity-based chromatographic assay of glycated protein, T he commercially available affinity-based chromatographic assay of glyc ated protein appears to be free from such interference and may well pr ove useful in the study of other conditions in which the non-enzymatic glycation of protein is suspected.