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A more recent version of this article appeared on August 1, 2007

Papers In Press, published online ahead of print May 7, 2007
J. Lipid Res., doi:10.1194/jlr.M700119-JLR200
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Submitted on March 8, 2007
Revised on May 4, 2007
Accepted on May 7, 2007

The acyl-CoA thioesterase I (Acot1) is regulated by the peroxisome proliferator-activated receptor alpha and hepatocyte nuclear factor 4 alpha via a distal response element in the promotor

Bikesh Dongol, Yatrik Shah, Insook Kim, Frank J. Gonzalez, and Mary C. Hunt

Department of Laboratory Medicine, Karolinska Institutet, Stockholm

Corresponding Author: mary.hunt{at}ki.se

The cytosolic acyl-CoA thioesterase I (Acot1) is an enzyme that hydrolyzes long-chain acyl-CoAs of C12-C20-CoA in chain-length, to the free fatty acid and coenzyme A. Acot1 was previously shown to be strongly upregulated at mRNA and protein level in rodents by fibrates. In this study, we show that Acot1 mRNA levels were increased 90-fold in liver by treatment with Wy-14,643 and that Acot1 mRNA is also increased 15-fold in the liver of hepatocyte nuclear factor 4 alpha (HNF4alpha ) knockout animals. Our study identified a direct repeat 1 (DR1) located in the Acot1 gene promotor in mouse, which binds the peroxisome proliferator-activated receptor alpha (PPARalpha ) and the HNF4alpha . Chromatin immunoprecipitation assay (ChIP) showed that the identified DR1 bound PPARalpha /retinoid X receptor alpha (RXRalpha ) and HNF4alpha , whereas the binding in ChIP was abrogated in the PPARalpha and HNF4alpha knockout mouse models. Reporter gene assays showed activation of the Acot1 promotor in cells by the PPARalpha agonist Wy-14,643, following co-transfection with PPARalpha /RXRalpha . However, transfection with a plasmid containing HNF4alpha also resulted in an increase in promotor activity. Taken together, these data show that Acot1 is under regulation by an interplay between of HNF4alpha and PPARalpha .


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