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Advanced glycation end products (AGEs) are a heterogenous group of glycation adducts on amino acids produced with sugars or dicarbonyls. Intracellular inflammation triggered by binding of AGEs to receptor for AGEs (RAGE) is linked to some chronic diseases. Here, we established a competitive assay format to comprehensively quantify AGEs which bound to RAGE. RAGE-binding activities of sugar- and dicarbonyl-derived AGEs were correlated with oxidative stress in cultured cells generated by the respective AGEs, suggesting that this would be a promising method for evaluating AGEs which could affect cellular functions despite limited information on individual glycation adducts.

Lectin-like oxidized low-density lipoprotein (LDL) receptor-1 (LOX-1) is an endothelial scavenger receptor that is important for oxidized low-density lipoprotein uptake. LOX-1 functions as an oligomer; however, little is known about the oligomeric complex and ligand processing after recognition by LOX-1. Here, we found that LOX-1 recognized and internalized ligands through the caveolae/raft-dependent endocytosis pathway in human coronary artery endothelial cells. Furthermore, we demonstrated that LOX-1 was palmitoylated and that both cysteine 36 and cysteine 46 were necessary for the recruitment of LOX-1 into raft microdomains and for its ligand uptake ability.