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J. Lipid Res.
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A more recent version of this article appeared on March 1, 2007 Originally published In Press as doi:10.1194/jlr.M600266-JLR200 on January 2, 2007

Papers In Press, published online ahead of print December 4, 2006
J. Lipid Res., doi:10.1194/jlr.M600266-JLR200
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Submitted on June 19, 2006
Revised on November 10, 2006
Accepted on December 4, 2006

Anti-bis(monoacylglycero)phosphate antibody induces the accumulation of acetylated-low density lipoprotein-derived cholesterol in cultured macrophages

Isabelle Delton-Vandenbroucke, Jerome Bouvier, Asami Makino, Nelly Besson, Jean-Fracoise Pageaux, Michel Lagarde, and Toshihide Kobayashi

Lipid Biology Laboratory, RIKEN, Wako, Saitama 351-0198

Corresponding Author: kobayasi{at}riken.jp

Bis(monoacylglycero)phosphate (BMP), also called as lysobisphosphatidic acid (LBPA), is a phospholipid highly enriched in the internal membranes of multivesicular late endosomes, in which it forms specialized lipid domains. It has been suggested that BMP-rich membranes regulate cholesterol transport. Here we examine the effect of an anti-BMP antibody on cholesterol metabolism and transport in two macrophage cell lines, RAW 264.7 and THP-1, during loading with acetylated LDL (acLDL). Anti-BMP antibody was internalized and accumulated in both macrophage cell types. Cholesterol staining with filipin and mass measurements indicate that acLDL-stimulated accumulation of free cholesterol was enhanced in macrophages that have accumulated the antibody. Unlike the hydrophobic amine U18666A, esterification of acLDL-derived cholesterol by ACAT was not modified after anti-BMP treatment. AcLDL loading led to an increase of free cholesterol in the plasma membrane. This increase was further enhanced in anti-BMP treated macrophages. However, cholesterol efflux to high density lipoproteins (HDL) was reduced in antibody-treated cells. The present results suggest that the accumulation of anti-BMP antibody alters cholesterol homeostasis in acLDL-loaded macrophages.


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