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Abstract
We have previously shown that CD36 recognizes oxidation products of phospholipids on oxidized LDL (OxLDL) such as 1-palmitoyl-2-(5'-oxovaleroyl)-sn-glycero-3-phosphocholine (POVPC). The current study was designed to examine whether the phosphocholine (PC) headgroup in POVPC constitutes an obligatory binding target for CD36. To examine the contribution of PC in the binding of POVPC to CD36, we used well-defined synthetic oxidized phospholipids (OxPLs) cross-linked to BSA or to a hexapeptide. The OxPL adducts were then tested for their ability to bind to CD36-transfected cells and for their ability to inhibit OxLDL binding to CD36. Both POVPC-BSA and POVPC-peptide adducts were high-affinity ligands for CD36 and potent inhibitors of OxLDL binding. Enzymatic removal of the entire PC moiety of the POVPC-peptide, or of the choline headgroup alone, as well as substitution of the choline headgroup by ethanolamine abrogated the inhibitory activity of POVPC. Interestingly, PC by itself or cross-linked to BSA did not show any intrinsic competition activity. In conclusion, our data demonstrate that the PC headgroup of OxPL alone is sufficient for binding to CD36, but only if presented in the correct conformation as in OxPL of OxLDL or as in POVPC-peptide adducts.
Highlights
We have previously shown that CD36 recognizes oxidation products of phospholipids on oxidized LDL (OxLDL) such as 1-palmitoyl-2-(5-oxovaleroyl)-sn-glycero-3-phosphocholine (POVPC)
Binding and uptake studies demonstrated that scavenger receptor A and CD36 were the principal macrophage receptors responsible for the binding of OxLDL and the accumulation of cholesteryl ester derived from modified lipoproteins
To examine the potential contribution of the PC moiety in the binding of oxidized phospholipid (OxPL) to CD36, we first characterized the binding of the POVPC-BSA adduct to CD36
Summary
We have previously shown that CD36 recognizes oxidation products of phospholipids on oxidized LDL (OxLDL) such as 1-palmitoyl-2-(5-oxovaleroyl)-sn-glycero-3-phosphocholine (POVPC). CD36 is a heavily glycosylated protein with broad ligand specificity, a characteristic of pattern recognition receptors It binds long-chain fatty acids [2], anionic phospholipids [3], -amyloid [4], advanced glycation end products [5], and OxLDL [1]. It functions in the recognition and removal of Plasmodium falciparum-infected erythrocytes [6] and apoptotic cells [7]. Binding and uptake studies demonstrated that scavenger receptor A and CD36 were the principal macrophage receptors responsible for the binding of OxLDL and the accumulation of cholesteryl ester derived from modified lipoproteins.
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