The endothelial cell binding site for advanced glycation end products consists of a complex: an integral membrane protein and a lactoferrin-like polypeptide
AM Schmidt, R Mora, R Cao, SD Yan, J Brett… - Journal of Biological …, 1994 - ASBMB
Advanced glycation end products (AGEs), formed as the result of the extended interaction of
proteins with ketoses, modulate central properties of endothelial cells and mononuclear
phagocytes by interacting with a cell surface binding site comprised of a novel integral
membrane protein (receptor for AGE= RAGE) and a lactoferrin-like polypeptide (LF-L), the
latter having sequence identity to lactoferrin (LF). To further understand this cellular binding
site, the interaction of RAGE with LF-L and LF was characterized. By ligand blotting and a …
proteins with ketoses, modulate central properties of endothelial cells and mononuclear
phagocytes by interacting with a cell surface binding site comprised of a novel integral
membrane protein (receptor for AGE= RAGE) and a lactoferrin-like polypeptide (LF-L), the
latter having sequence identity to lactoferrin (LF). To further understand this cellular binding
site, the interaction of RAGE with LF-L and LF was characterized. By ligand blotting and a …