J. Lipid Res.
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Originally published In Press as doi:10.1194/jlr.M600266-JLR200 on January 2, 2007 Originally published In Press as doi:10.1194/jlr.M600266-JLR200 on December 4, 2006

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Journal of Lipid Research, Vol. 48, 543-552, March 2007
Copyright © 2007 by American Society for Biochemistry and Molecular Biology

Anti-bis(monoacylglycero)phosphate antibody accumulates acetylated LDL-derived cholesterol in cultured macrophages

Isabelle Delton-Vandenbroucke1,*, Jerome Bouvier*, Asami Makino{dagger}, Nelly Besson*, Jean-François Pageaux*, Michel Lagarde* and Toshihide Kobayashi1,*,{dagger}

* Institut National de la Santé et de la Recherche Médicale U585, Institut National des Sciences Appliquees-Lyon, Institut Multidisciplinaire de Biochimie des Lipides, 69621 Villeurbanne, France
{dagger} RIKEN (Institute of Physical and Chemical Research), 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan

Published, JLR Papers in Press, December 4, 2006.

1 To whom correspondence should be addressed. e-mail: kobayashi{at}riken.jp (T.K.); isabelle.vandenbroucke{at}insa-lyon.fr (I.D.V.)

Bis(monoacylglycero)phosphate (BMP), also called lysobisphosphatidic acid, 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 effects 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 low density lipoprotein (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 (FC) was enhanced in macrophages that had accumulated the antibody. Unlike the hydrophobic amine U18666A (3-ß-[2-(diethylamino)ethoxy]androst-5-en-17-one), esterification of AcLDL-derived cholesterol by ACAT was not modified after anti-BMP treatment. AcLDL loading led to an increase of FC in the plasma membrane. This increase was further enhanced in anti-BMP-treated macrophages. However, cholesterol efflux to HDL was reduced in antibody-treated cells. These results suggest that the accumulation of anti-BMP antibody alters cholesterol homeostasis in AcLDL-loaded macrophages.

Supplementary key words endocytosis • late endosome • lipid domain • cholesterol efflux • low density lipoprotein

Abbreviations: AcLDL, acetylated low density lipoprotein; BMP, bis(monoacylglycero)phosphate; CE, cholesteryl ester; FC, free cholesterol; [3H-CO]LDL, low density lipoprotein labeled with [3H]cholesteryl oleate; LBPA, lysobisphosphatidic acid; MßCD, methyl-ß-cyclodextrin; MTT, 3-(4,5-dimethyl thiazol-2-yl)-2,5-diphenyl tetrazolium bromide; PMA, phorbol myristate acetate


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F. Hullin-Matsuda, K. Kawasaki, I. Delton-Vandenbroucke, Y. Xu, M. Nishijima, M. Lagarde, M. Schlame, and T. Kobayashi
De novo biosynthesis of the late endosome lipid, bis(monoacylglycero)phosphate
J. Lipid Res., September 1, 2007; 48(9): 1997 - 2008.
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