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Journal of Lipid Research, Vol. 47, 2451-2461, November 2006
Copyright © 2006 by American Society for Biochemistry and Molecular Biology

The mechanism mediating the activation of acetyl-coenzyme A carboxylase- gene transcription by the liver X receptor agonist T0-901317

Saswata Talukdar and F. Bradley Hillgartner¹

Department of Biochemistry and Molecular Pharmacology, School of Medicine, West Virginia University, Morgantown, WV 26506

Published, JLR Papers in Press, August 24, 2006.

¹ To whom correspondence should be addressed. e-mail: fbhillgartner{at}hsc.wvu.edu

In birds and mammals, agonists of the liver X receptor (LXR) increase the expression of enzymes that make up the fatty acid synthesis pathway. Here, we investigate the mechanism by which the synthetic LXR agonist, T0-901317, increases the transcription of the acetyl-coenzyme A carboxylase- (ACC) gene in chick embryo hepatocyte cultures. Transfection analyses demonstrate that activation of ACC transcription by T0-901317 is mediated by a cis-acting regulatory unit (–101 to –71 bp) that is composed of a liver X receptor response element (LXRE) and a sterol-regulatory element (SRE). The SRE enhances the ability of the LXRE to activate ACC transcription in the presence of T0-901317. Treating hepatocytes with T0-901317 increases the concentration of mature sterol-regulatory element binding protein-1 (SREBP-1) in the nucleus and the acetylation of histone H3 and histone H4 at the ACC LXR response unit. These results indicate that T0-901317 increases hepatic ACC transcription by directly activating LXR•retinoid X receptor (RXR) heterodimers and by increasing the activity of an accessory transcription factor (SREBP-1) that enhances ligand induced-LXR•RXR activity.

Supplementary key words fatty acid synthesis • sterol-regulatory element binding protein • thyroid hormone • chicken • histone acetylation

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