Distinguished effects of antiphospholipid antibodies and anti-oxidized LDL antibodies on oxidized LDL uptake by macrophages

K. Kobayashi, K. Tada, H. Itabe, T. Ueno, P. H. Liu, A. Tsutsumi, M. Kuwana, T. Yasuda, Y. Shoenfeld, P. G. De Groot, Eiji Matsuura*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Several interpretations have been made regarding the specificity of antiphospholipid antibodies and antibodies against oxidized low-density lipoprotein (oxLDL), but these are still controversial. In the present study, we delineated specificity of these two types of antibodies and analyzed their regulatory effect on oxLDL and/or β2-glycoprotein I (β2GPI) binding to macrophages. Scavenger receptor-mediated binding of oxLDL (or its β2GPI complexes) to macrophages was observed and the binding was partly prevented by β2GPI. The IgG monoclonal anti-β2GPI antibody (WB-CAL-1), which was derived from NZW X BXSB F1 mouse (a model of antiphospholipid syndrome), significantly increased the oxLDL/β2GPI binding to macrophages. In contrast, IgM anti-oxLDL natural antibody, EO6 (derived from apoe-/- mouse), prevented the binding. Different antigenic specificity of these antibodies to oxLDL and its β2GPI complexes was also confirmed in TLC-ligand blot and ELISA. Thus, IgG anti-β2GPI autoantibodies contribute to lipid metabolism (housekeeping of oxLDL by macrophages) whereas IgM natural anti-oxLDL antibodies may protect against atherogenesis. In addition, in vitro data suggest that relatively high dose of intravenous immunoglobulin preparations (mainly contain IgG anti-oxLDL antibodies) might also prevent atherogenesis by inhibiting the oxLDL binding to macrophages.

Original languageEnglish
Pages (from-to)929-938
Number of pages10
Issue number12
StatePublished - 2007


  • Anticardiolipin antibody
  • Antiphospholipid syndrome
  • Atherosclerosis
  • Oxidized low-density lipoprotein
  • β-glycoprotein I


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