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A more recent version of this article appeared on May 1, 2005

Papers In Press, published online ahead of print February 1, 2005
J. Lipid Res., doi:10.1194/jlr.M400496-JLR200
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Submitted on December 16, 2004
Revised on January 27, 2005
Accepted on January 31, 2005

Phosphocholine as a pattern recognition ligand for CD36

Agnes Boullier, Peter Friedman, Richard Harkewicz, Karsten Hartvigsen, Simone R Green, Felicidad Almazan, Edward A Dennis, Daniel Steinberg, Joseph L Witztum, and Oswald Quehenberger

Medicine, University of California, San Diego, La Jolla, CA 92093

Corresponding Author: oquehenberger{at}ucsd.edu

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 (OxPL) crosslinked 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 crosslinked 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.


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