Non enzymatic glycation of apolipoprotein A-I. Effects on its self-association and lipid binding properties |
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Authors: | C Calvo C Talussot G Ponsin F Berthézène |
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Affiliation: | INSERM U 197, Laboratoire de Métabolisme des Lipides, H?pital de l'Antiquaille, Lyon, France. |
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Abstract: | In diabetic patients, hyperglycaemia results in the non enzymatic glycation of many proteins including apolipoprotein A-I. We purified glycated apo A-I and compared its lipid binding properties to those of normal apo A-I. Analysis of tryptophan fluorescence spectra and of fluorescence quenching in the presence of iodine showed that glycation of apo A-I induces a decrease in the stability of the lipid-apoprotein interaction and in that of the apoprotein self-association. Repetitive ultracentrifugations of High Density Lipoprotein (HDL) samples containing radioiodinated apo A-I or glycated apo A-I revealed that glycation of the apoprotein facilitates its dissociation from HDL. These results suggest that the non enzymatic glycation of apo A-I may affect the structural cohesion of HDL particles. |
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