Calvo C, Talussot C, Ponsin G, Berthézène F
INSERM U 197, Laboratoire de Métabolisme des Lipides, Hôpital de l'Antiquaille, Lyon, France.
Biochem Biophys Res Commun. 1988 Jun 30;153(3):1060-7. doi: 10.1016/s0006-291x(88)81336-6.
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.
在糖尿病患者中，高血糖会导致包括载脂蛋白A-I在内的许多蛋白质发生非酶糖基化。我们纯化了糖基化的载脂蛋白A-I，并将其脂质结合特性与正常载脂蛋白A-I的脂质结合特性进行了比较。对色氨酸荧光光谱以及在碘存在下的荧光猝灭分析表明，载脂蛋白A-I的糖基化会导致脂质-载脂蛋白相互作用稳定性以及载脂蛋白自缔合稳定性降低。对含有放射性碘化载脂蛋白A-I或糖基化载脂蛋白A-I的高密度脂蛋白（HDL）样品进行反复超速离心后发现，载脂蛋白的糖基化促进了其与HDL的解离。这些结果表明，载脂蛋白A-I的非酶糖基化可能会影响HDL颗粒的结构凝聚力。
