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J Biol Chem, Vol. 273, Issue 40, 25573-25580, October 2, 1998
and 
Induces Apoptosis of Human Monocyte-derived Macrophages
,,,,,, and
From Peroxisome proliferator-activated receptors
(PPARs) have been implicated in metabolic diseases, such as obesity,
diabetes, and atherosclerosis, due to their activity in liver and
adipose tissue on genes involved in lipid and glucose homeostasis.
Here, we show that the PPAR U.325 INSERM, Département
d'Athérosclérose, Institut Pasteur, 1 Rue Calmette, 59019 Lille, France, the Faculté de Pharmacie, Université de
Lille II, 59006 Lille, France, and ¶ U.321 INSERM, Hôpital
de la Pitié, 83 Boulevard de l'Hôpital, F-75651 Paris,
Cedex 13, France
and PPAR
forms are expressed in
differentiated human monocyte-derived macrophages, which participate in
inflammation control and atherosclerotic plaque formation. Whereas
PPAR is already present in undifferentiated monocytes, PPAR
expression is induced upon differentiation into macrophages.
Immunocytochemistry analysis demonstrates that PPAR resides
constitutively in the cytoplasm, whereas PPAR is predominantly
nuclear localized. Transient transfection experiments indicate
that PPAR and PPAR are transcriptionally active after ligand
stimulation. Ligand activation of PPAR, but not of PPAR, results
in apoptosis induction of unactivated differentiated macrophages as
measured by the TUNEL assay and the appearance of the active
proteolytic subunits of the cell death protease caspase-3. However,
both PPAR and PPAR ligands induce apoptosis of macrophages
activated with tumor necrosis factor /interferon . Finally,
PPAR inhibits the transcriptional activity of the NF
B p65/RelA
subunit, suggesting that PPAR activators induce macrophage
apoptosis by negatively interfering with the anti-apoptotic NFB signaling pathway. These data demonstrate a novel
function of PPAR in human macrophages with likely consequences
in inflammation and atherosclerosis.
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