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A more recent version of this article appeared on May 3, 2002
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M200475200v1
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Papers In Press, published online ahead of print March 1, 2002
J. Biol. Chem, 10.1074/jbc.M200475200
Submitted on January 16, 2002
Revised on March 1, 2002
Accepted on March 1, 2002

PPAR gamma coactivator-1 recruitment regulates PPAR subtype specificity

Hannes Oberkofler, Harald Esterbauer, Veronika Linnemayr, A. Donny Strosberg, Franz Krempler, and Wolfgang Patsch

Laboratory Medicine, Landeskliniken Salzburg, Salzburg, Salzburg A-5020

Corresponding Author: w.patsch{at}lks.at

The peroxisome proliferator activated receptors (PPAR) alpha and gamma play key roles in the transcriptional control of contrasting metabolic pathways such as adipogenesis and fatty acid beta -oxidation. Both ligand activated nuclear receptors bind to common target gene response elements and interact with distinct domains of the transcriptional coactivator PGC-1 to attain their full transcriptional potency. Thus, PPAR subtype specificity may be determined by ligand availability and transcription factor or coactivator expression levels. To identify other, perhaps more precise mechanisms contributing to PPAR subtype specificity, we studied PGC-1 recruitment by PPARs using a previously described hormone response element in the human UCP1 promoter and a human brown adipocyte cell line as our model system. Like in rodents, PGC-1 is involved in the transcriptional regulation of the UCP1 gene in humans and mediates the effects of PPARalpha and PPARgamma agonists and retinoic acid. Interestingly, a previously postulated PGC-1 repressor selectively affects the PPARalpha meditated activation of UCP1 gene expression. Furthermore, inhibition of p38 MAPK signaling, known to regulate the PGC-1/repressor interaction, decreases the stimulatory effect of PPARalpha agonist treatment without reducing the response to thiazolidinedione or retinoic acid. These data support a model whereby PPAR subtype specificity is regulated by recruitment of PGC-1.


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