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Advanced Glycosylation of LDL: Role in Oxidative Modification and Diabetic Complications

Maillard Reactions in Chemistry, Food and Health, Page: 286-291
2005
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Book Chapter Description

We investigated the possibility that amine-containing phospholipids react directly with glucose to form advanced glycosylation endproducts (AGEs). Phospholipid-linked AGEs formed readily in vitro, mimicking the absorbance, fluorescence, and immunochemical properties of AGEs that result from the advanced glycosylation of proteins. Lipid-AGE formation was accompanied by fatty acid oxidation, which occurred in the absence of added, transition metal ions. In additional experiments, incubation of low-density lipoprotein (LDL) with glucose was found to produce AGE moieties that were attached to both the lipid and the apoprotein (ApoB) components. Oxidized-LDL formed concomitantly with AGE-modified LDL. AGE-specific ELISA analysis of LDL specimens isolated from diabetic individuals revealed increased levels of both apoprotein- and lipid-linked AGEs when compared to specimens obtained from normal, non-diabetic controls. Circulating levels of oxidized-LDL were elevated in diabetic patients, and correlated significantly with apoB-AGE and lipid-AGE levels. Lipid-advanced glycosylation may result from intra-molecular redox reactions that occur during advanced glycosylation and presents a facile mechanism to explain lipid oxidation in vivo, where free metals are present in too low a concentration to induce oxidative modification.

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