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Originally published In Press as doi:10.1074/jbc.M005894200 on October 10, 2000

J. Biol. Chem., Vol. 276, Issue 2, 974-983, January 12, 2001
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Thyroid Hormone Stimulates Acetyl-CoA Carboxylase-alpha Transcription in Hepatocytes by Modulating the Composition of Nuclear Receptor Complexes Bound to a Thyroid Hormone Response Element*

Yanqiao Zhang, Liya Yin, and F. Bradley HillgartnerDagger

From the Department of Biochemistry, School of Medicine, West Virginia University, Morgantown, West Virginia 26506

Triiodothyronine (T3) stimulates a 7-fold increase in transcription of the acetyl-CoA carboxylase-alpha (ACCalpha ) gene in chick embryo hepatocytes. Here, we characterized an ACCalpha T3 response element (ACCalpha -T3RE) with unique functional and protein binding properties. ACCalpha -T3RE activated transcription both in the absence and presence of T3, with a greater activation observed in the presence of T3. In nuclear extracts from hepatocytes incubated in the absence of T3, ACCalpha -T3RE bound protein complexes (complexes 1 and 2) containing the liver X receptor (LXR) and the retinoid X receptor (RXR). In nuclear extracts from hepatocytes incubated in the presence of T3 for 24 h, ACCalpha -T3RE bound a different set of complexes. One complex contained LXR and RXR (complex 3) and another contained the nuclear T3 receptor (TR) and RXR (complex 4). Mutations of ACCalpha -T3RE that inhibited the binding of complexes 1 and 2 decreased transcriptional activation in the absence of T3, and mutations of ACCalpha -T3RE that inhibited the binding of complexes 3 and 4 decreased transcriptional activation in the presence of T3. The stimulation of ACCalpha transcription caused by T3 was closely associated with changes in the binding of complexes 1-4 to ACCalpha -T3RE. These data suggest that T3 regulates ACCalpha transcription by a novel mechanism involving changes in the composition of nuclear receptor complexes bound to ACCalpha -T3RE. We propose that complexes containing LXR/RXR ensure a basal level of ACCalpha expression for the synthesis of structural lipids in cell membranes and that complexes containing LXR/RXR and TR/RXR mediate the stimulation of ACCalpha expression caused by T3.

* This work was supported by Cooperative State Research Service/United States Department of Agriculture Grant 980-3711.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.

Dagger To whom correspondence should be addressed: Dept. of Biochemistry, P.O. Box 9142, West Virginia University, Morgantown, WV 26506-9142. Tel.: 304-293-7751; Fax: 304-293-6846; E-mail: fbhillgartner@ hsc.wvu.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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