J. Lipid Res.
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A more recent version of this article appeared on December 1, 2005

Papers In Press, published online ahead of print September 14, 2005
J. Lipid Res., doi:10.1194/jlr.M500326-JLR200
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Submitted on July 27, 2005
Revised on September 1, 2005
Accepted on September 14, 2005

Peroxisome proliferator-activated receptoralpha controls cellular cholesterol trafficking in macrophages

Giulia Chinetti-Gbaguidi, Elena Rigamonti, Lionel Helin, Aino-Liisa Mutka, Marco Lepore, Jean Charles Fruchart, Véronique Clavey, Elina Ikonen, Sophie Lestavel, and Bart Staels

Inserm UR 545, Institut Pasteur de Lille, Lille

Corresponding Author: bart.staels{at}pasteur-lille.fr

The mobilization of cholesterol from intracellular pools to the plasma membrane is a determinant governing its availability for efflux to extra-cellular acceptors. NPC1 and NPC2 are proteins localized in the late endosome controlling cholesterol transport from the lysosome to the plasma membrane. Here, we report that NPC1 and NPC2 gene expression is induced by OxLDL in human macrophages. Since OxLDL contain natural activators of PPARalpha , a fatty acid-activated nuclear receptor, the regulation of NPC1 and NPC2 by PPARalpha and the consequences on cholesterol trafficking were further studied. NPC1 and NPC2 expression is induced by synthetic PPARalpha ligands in human macrophages. Furthermore, PPARalpha activation leads to an enrichment of cholesterol in the plasma membrane. By contrast, incubation with progesterone, which blocks post-lysosomal cholesterol trafficking, as well as NPC1 and NPC2 mRNA depletion using siRNA, abolished ABCA1-dependent cholesterol efflux induced by PPARalpha activators. These observations identify a novel regulatory role for PPARalpha in the control of cholesterol availability for efflux that, associated with its ability to inhibit cholesterol esterification and to stimulate ABCA1 and SR-BI expression, may contribute to the stimulation of reverse cholesterol transport.


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