Key result
Glycated human serum albumin derived from 20 mM glucose and shear stress independently enhanced RAGE expression on human umbilical vein endothelial cells.
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Glycated human serum albumin and shear stress synergistically modulate RAGE expression on endothelial cells, providing mechanistic insights into diabetic vascular complications.
Advanced glycation end products (AGEs) are known to be involved in the pathogenesis of several diseases, in particular diabetes, via signaling through their receptor. Numerous studies have been carried out on protein-sugar interactions at very high concentrations of the latter. The objective of this investigation was to determine the effects of nonenzymatic glycation induced by reducing sugars on the secondary structure of human serum albumin (HSA) under different physiological conditions and to correlate that with expression of RAGE (receptor for advanced glycation end products) on HUVECs (human umbilical vein endothelial cells) in a controlled hemodynamic environment. Our results indicate that RAGE expression is shear stress modulated and that glycated HSA enhances the expression further. The secondary structure of AGE-HSA derived from glucose at 20 mM contains higher α-helical content and elicits maximum expression of the receptor. The effect of shear stress at 10 dynes cm(-2) is independent of AGE-HSA.
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Bala et al. (2011) studied this question. Glycated human serum albumin (AGE-HSA) and shear stress was evaluated on RAGE expression on HUVECs and secondary structure of HSA. Glycated human serum albumin derived from 20 mM glucose and shear stress independently enhanced RAGE expression on human umbilical vein endothelial cells.
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