The endothelial cell binding site for advanced glycation end products consists of a complex: an integral membrane protein and a lactoferrin-like polypeptide.

摘要: Advanced glycation end products (AGEs), formed as the result of extended interaction proteins with ketoses, modulate central properties endothelial cells and mononuclear phagocytes by interacting a cell surface binding site comprised novel integral membrane protein (receptor for AGE = RAGE) lactoferrin-like polypeptide (LF-L), latter having sequence identity to lactoferrin (LF). To further understand this cellular site, RAGE LF-L LF was characterized. By ligand blotting solid state competitive assay, 125I-LF-L 125I-LF bound immobilized on nitrocellulose membranes or polypropylene tubes in time-dependent reversible manner, demonstrating high affinity component Kd approximately 100 pM. The independent iron competed addition an excess unlabeled carboxyl-terminal portion LF. Cross-linking studies purified RAGE, presence disuccinimidyl suberate, showed new, slowly migrating band, corresponding complex LF-L, cross-linking mouse aortic two new bands immunoblotting visualized both anti-RAGE IgG anti-LF-L IgG. These data lead us propose that AGEs consists noncovalently anchored membrane.