| Autor: |
Breitling-Utzmann, Carmen M., Unger, Anke, Friedl, D. Alexander, Lederer, Markus O. |
| Zdroj: |
Archives of Biochemistry and Biophysics; July 15, 2001, Vol. 391 Issue: 2 p245-254, 10p |
| Abstrakt: |
While the Maillard reaction of amino acids and proteins as well as its consequences in vivo has been thoroughly investigated, little attention has so far been paid to the glycation of aminophospholipids such as phosphatidylethanolamine (PE) or phosphatidylserine (PS), which are essential for structure and functionality of biological membranes. PE-derived glucosylamines (Schiff-PEs) and aminoketoses (Amadori-PEs) have now for the first time been simultaneously identified and quantified in erythrocytes from diabetics and healthy individuals by liquid chromatography–electrospray mass spectrometry (LC-(ESI)MS). The amounts of glycated PE (gPE) were significantly higher in diabetics (0.18–34.2 mol% Schiff-PE and 0.047–0.375 mol% Amadori-PE) than in controls (0.12–3.99 mol% Schiff-PE and 0.018–0.055 mol% Amadori-PE). A positive correlation between fructosylated hemoglobin (HbA1c) and the gPE levels was established. No advanced glycation endproducts (AGEs) like 5-hydroxymethylpyrrole-2-carbaldehyde (pyrrole-PE), carboxymethyl (CM-PE), or carboxyethyl (CE-PE) derivatives were detected. To investigate the influence of gPE on lipid peroxidation of biological membranes, liposomes consisting of soy-PE and synthetically prepared Amadori-PE (16:0–16:0) were incubated for several days and the formation of oxidation products was monitored. It could be shown that Amadori-PE extensively promotes lipid peroxidation even in the absence of transition metal ions like Cu2+ and Fe3+. Oxidative damage to membrane lipids therefore is supposed to be at least partially caused by the glycation of aminophospholipids. |
| Databáze: |
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