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Papers In Press, published online ahead of print January 16, 2003
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Department of Cell Chemistry, Okayama University Graduate School of Medicine and Dentistry, Okayama, Okayama 700-8558
Corresponding Author: eijimatu{at}md.okayama-u.ac.jp
Revised on December 27, 2002
Accepted on January 14, 2003
Circulating oxidized LDL forms complexes with
2-glycoprotein I: implication as an atherogenic autoantigen
2-Glycoprotein I (2-GPI) is a major antigen for antiphospholipid antibodies (Abs, aPL) present in patients with antiphospholipid syndrome (APS). We recently reported (J. Lipid Res., 42: 697, 2001; J. Lipid Res., 43: 1486, 2002) that 2-GPI specifically binds to Cu2+-oxidized low density lipoprotein (oxLDL) and that the 2-GPI ligands are 
-carboxylated 7-ketocholesteryl esters. In the present study, we demonstrate that oxLDL forms stable and non-dissociable complexes with 2-GPI in serum, and that high serum levels of the complexes are associated with arterial thrombosis in APS. A conjugated ketone function at the 7-position of cholesterol as well as the -carboxyl function of the 2-GPI ligands was necessary for 2-GPI binding. The ligand-mediated non-covalent interaction of 2-GPI and oxLDL undergoes a temperature and time dependent conversion to much more stable but readily dissociable complexes in vitro at neutral pH. In contrast, stable and non-dissociable 2-GPI-oxLDL complexes were frequently detected in sera from patients with APS and/or SLE. Both the presence of 2-GPI-oxLDL complexes and IgG Abs recognizing these complexes were strongly associated with arterial thrombosis. Further, these same Abs correlated with IgG immune complexes containing 2-GPI or LDL. Thus, the 2-GPI-oxLDL complexes acting as an auto-Ag are closely associated with autoimmune-mediated atherogenesis.
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