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

Autor: Tatsuji Yasuda, Masataka Kuwana, H. Itabe, T. Ueno, Akito Tsutsumi, Eiji Matsuura, Kazuko Kobayashi, K. Tada, P. H. Liu, P. G. De Groot, Y Shoenfeld
Rok vydání: 2007
Předmět:
Zdroj: Lupus. 16:929-938
ISSN: 1477-0962
0961-2033
DOI: 10.1177/0961203307084170
Popis: 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 × 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. Lupus (2007) 16, 929—938.
Databáze: OpenAIRE