Background
Protein damage induced by retained uremic solutes may be an important component in the pathophysiology of advanced renal disease. Albumin isolated from hemodialysis patients was recently shown to block high-density lipoprotein (HDL) receptor-mediated cholesterol uptake. However, post-translational modifications that render albumin a scavenger receptor class B type I (SR-BI) ligand are not known. We hypothesized that the elimination of positive charge through oxidation of albumin-lysine residues is required to generate recognition motifs for SR-BI. Since carbamylation and carboxymethylation are major lysine modifications in vivo, we aimed at investigating their influence on the binding properties of HD-albumin to SR-BI.