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Distinguished effects of antiphospholipid antibodies and anti-oxidized LDL antibodies on oxidized LDL uptake by macrophagesDepartment of Cell Chemistry, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama, Japan
Department of Cell Chemistry, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama, Japan
Department of Biological Chemistry, Showa University School of Pharmaceutical Sciences, Tokyo, Japan
Department of Cell Chemistry, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama, Japan
Department of Cell Chemistry, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama, Japan
Division of Clinical Immunology, Major of Advanced Biomedical Applications, Graduate School of Comprehensive Human Science, University of Tsukuba, Tsukuba, Japan
Division of Rheumatology, Department of Internal Medicine, Keio University School of Medicine, Tokyo, Japan
Department of Cell Chemistry, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama, Japan
Department of Medicine B and Center for Autoimmune Diseases, Sheba Medical Center, Tel-Hashomer, Isreal, Incumbent of the Laura Schwarz-Kipp Chair for Research for Autoimmune Diseases, Sackler Faculty of Medicine, Tel-Aviv University, Tel-Aviv, Israel
Thrombosis and Haemostasis Laboratory, Department of Clinical Chemistry and Haematology, University Medical Center, Utrecht, The Netherlands
Department of Cell Chemistry, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama, Japan, eijimatu{at}md.okayama-u.ac.jp 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 β 2-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 β 2GPI. 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-β2 GPI 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. Lupus (2007) 16, 929—938.
Key Words: anticardiolipin antibody antiphospholipid syndrome atherosclerosis β2-glycoprotein I oxidized low-density lipoprotein
Lupus, Vol. 16, No. 12,
929-938 (2007) This article has been cited by other articles:
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