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J. Biol. Chem., Vol. 276, Issue 15, 12440-12448, April 13, 2001
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From the We investigated whether peroxisome
proliferator-activated receptor
Peroxisome Proliferator-activated Receptor
Ligands Suppress
the Transcriptional Activation of Cyclooxygenase-2
EVIDENCE FOR INVOLVEMENT OF ACTIVATOR PROTEIN-1 AND CREB-BINDING
PROTEIN/p300*
§¶,
,, and§
Department of Medicine (Division of
Gastroenterology and Hepatology), New York Presbyterian Hospital and
Weill Medical College of Cornell University, the § Strang
Cancer Prevention Center, and the Department of Surgery (Head
and Neck Service), Memorial Sloan-Kettering Cancer Center,
New York, New York 10021
(PPAR) ligands
(ciglitazone, troglitazone, and 15-deoxy-
12,14
prostaglandin J2) inhibited cyclooxygenase-2 (COX-2)
induction in human epithelial cells. Ligands of PPAR inhibited
phorbol ester (phorbol 12-myristate 13-acetate, PMA)-mediated induction of COX-2 and prostaglandin E2 synthesis. Nuclear run-offs
revealed increased rates of COX-2 transcription after
treatment with PMA, an effect that was inhibited by PPAR ligands.
PMA-mediated induction of COX-2 promoter activity was
inhibited by PPAR ligands; this suppressive effect was prevented by
overexpressing a dominant negative form of PPAR or a PPAR response
element decoy oligonucleotide. The stimulatory effects of PMA were
mediated by a cyclic AMP response element in the COX-2
promoter. Treatment with PMA increased activator protein-1 (AP-1)
activity and the binding of c-Jun, c-Fos, and ATF-2 to the cyclic AMP
response element, effects that were blocked by PPAR ligands. These
findings raised questions about the mechanism underlying the anti-AP-1
effect of PPAR ligands. The induction of c-Jun by PMA was blocked by
PPAR ligands. Overexpression of either c-Jun or CREB-binding
protein/p300 partially relieved the suppressive effect of PPAR
ligands. When CREB-binding protein and c-Jun were overexpressed
together, the ability of PPAR ligands to suppress PMA-mediated
induction of COX-2 promoter activity was essentially
abrogated. Bisphenol A diglycidyl ether, a compound that binds to
PPAR but lacks the ability to activate transcription, also inhibited
PMA-mediated induction of AP-1 activity and COX-2. Taken together,
these findings are likely to be important for understanding the
anti-inflammatory and anti-cancer properties of PPAR ligands.
*
This work was supported in part by National Institutes of
Health Grants P01 CA29502, 1 R01 CA89578, and T32 CA09685, the Cancer Research Foundation of America, and the James E. Olson Foundation.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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