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Originally published In Press as doi:10.1074/jbc.M200971200 on February 25, 2002

J. Biol. Chem., Vol. 277, Issue 18, 15736-15744, May 3, 2002
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Polyunsaturated Fatty Acyl Coenzyme A Suppress the Glucose-6-phosphatase Promoter Activity by Modulating the DNA Binding of Hepatocyte Nuclear Factor 4alpha *

Fabienne RajasDagger , Amandine Gautier, Isabelle Bady, Sandrine Montano, and Gilles Mithieux

From the INSERM U. 449, Faculté de Médecine Laennec, Rue Guillaume Paradin, 69372 Lyon cedex 08, France

Glucose-6-phosphatase confers on gluconeogenic tissues the capacity to release endogenous glucose in blood. The expression of its gene is modulated by nutritional mechanisms dependent on dietary fatty acids, with specific inhibitory effects of polyunsaturated fatty acids (PUFA). The presence of consensus binding sites of hepatocyte nuclear factor 4 (HNF4) in the -1640/+60 bp region of the rat glucose-6-phosphatase gene has led us to consider the hypothesis that HNF4alpha could be involved in the regulation of glucose-6-phosphatase gene transcription by long chain fatty acid (LCFA). Our results have shown that the glucose-6-phosphatase promoter activity is specifically inhibited in the presence of PUFA in HepG2 hepatoma cells, whereas saturated LCFA have no effect. In HeLa cells, the glucose-6-phosphatase promoter activity is induced by the co-expression of HNF4alpha or HNF1alpha . PUFA repress the promoter activity only in HNF4alpha -cotransfected HeLa cells, whereas they have no effects on the promoter activity in HNF1alpha -cotransfected HeLa cells. From gel shift mobility assays, deletion, and mutagenesis experiments, two specific binding sequences have been identified that appear able to account for both transactivation by HNF4alpha and regulation by LCFA in cells. The binding of HNF4alpha to its cognate sites is specifically inhibited by polyunsaturated fatty acyl coenzyme A in vitro. These data strongly suggest that the mechanism by which PUFA suppress the glucose-6-phosphatase gene transcription involves an inhibition of the binding of HNF4alpha to its cognate sites in the presence of polyunsaturated fatty acyl-CoA thioesters.

* This work was supported by a grant from the "Fondation de France" and from the University Claude Bernard Lyon I (Bonus Qualité Recherche).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 Supported by a postdoctoral fellowship from the "Institut Nestlé" and the "Fondation pour la Recherche Médicale." To whom correspondence and reprint requests should be addressed: INSERM U. 449, Faculté de Médecine Laennec, Rue Guillaume Paradin, 69372 Lyon cedex 08, France. Tel.: 33-478-77-86-29; Fax: 33-478-77-87-62; E-mail: rajas@laennec.univ-lyon1.fr.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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