Association in vivo of glycated apolipoprotein A-I with high density lipoproteins.
In diabetic patients, hyperglycaemia results in the non-enzymatic glycation of apolipoprotein A-I, the major protein of human high density lipoproteins. The effect of the non-enzymatic glycation on the association of apolipoprotein A-I with high density lipoprotein in vivo has been studied in the rat. The distribution volume obtained after injection of glycated apolipoprotein A-I was 2- to 3-fold higher in kidneys and approximately 30% lower in adrenals and ovaries than that obtained with apolipoprotein A-I. Analysis by gel chromatography of serum from donor rats shows that glycation diminishes the interaction between apolipoprotein A-I and high density lipoprotein. The findings in this study suggest that non-enzymatic glycation of apolipoprotein A-I may contribute to the development of atherosclerosis in patients with diabetes mellitus.
Calvo
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Departamento de Bioquímica Aplicada, Facultad de Farmacia, Universidad de Concepción, Chile.
Verdugo
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C
D000311:Adrenal Glands / Q000378:metabolism; D000818:Animals; D016632:Apolipoprotein A-I / Q000378:metabolism*; D002850:Chromatography, Gel; D005260:Female; D006031:Glycosylation; D006801:Humans; D007668:Kidney / Q000378:metabolism; D008075:Lipoproteins, HDL / Q000097:blood / Q000378:metabolism*; D008099:Liver / Q000378:metabolism; D010053:Ovary / Q000378:metabolism; D051381:Rats
D016632:Apolipoprotein A-I; D008075:Lipoproteins, HDL