کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2052965 | 1074249 | 2006 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Heat-shock protein 27 is a major methylglyoxal-modified protein in endothelial cells Heat-shock protein 27 is a major methylglyoxal-modified protein in endothelial cells](/preview/png/2052965.png)
In endothelial cells cultured under high glucose conditions, methylglyoxal is the major intracellular precursor in the formation of advanced glycation endproducts. We found that endothelial cells incubated with 30 mM d-glucose produced approximately 2-fold higher levels of methylglyoxal but not 3-deoxyglucosone and glyoxal, as compared to 5 mM d-glucose. Under hyperglycaemic conditions, the methylglyoxal-arginine adduct argpyrimidine as detected with a specific antibody, but not Ne-(carboxymethyl)lysine and Ne-(carboxyethyl)lysine, was significantly elevated. The glyoxylase I inhibitor HCCG and the PPARγ ligand troglitazone also increased argpyrimidine levels. Increased levels of argpyrimidine by glucose, HCCG and troglitazone are accompanied by a decrease in proliferation of endothelial cells. A 27 kDa protein was detected as a major argpyrimidine-modified protein. With in-gel digestion and mass spectrometric analysis, we identified this major protein as heat-shock protein 27 (Hsp27). This argpyrimidine modification of Hsp27 may contribute to changes in endothelial cell function associated to diabetes.
Journal: FEBS Letters - Volume 580, Issue 6, 6 March 2006, Pages 1565–1570