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J. Biol. Chem., Vol. 281, Issue 15, 10010-10015, April 14, 2006

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Role of Histone Deacetylase in the Expression of CTP:Phosphocholine Cytidylyltransferase ^*

Claudia Banchio¹, Susanne Lingrell, and Dennis E. Vance²

From the Department of Biochemistry and Canadian Institutes of Health Research Group in Molecular and Cell Biology of Lipids, University of Alberta, Edmonton, Alberta T6G 2S2, Canada and the Biology Division, Instituto de Biología Molecular y Celular de Rosario, Consejo Nacional de Investigaciones Científicas y Técnicas, Area Biologia, Departamento de Ciencias Biologicas, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Suipacha 531, Rosario S2002LRK, Argentina

Histone acetylation plays an important role in chromatin remodeling and gene expression. The molecular mechanisms involved in cell-specific expression of CTP:phosphocholine cytidylyltransferase (CT) are not fully understood. In this study, we investigated whether or not histone deacetylation is involved in repression of CT expression in quiescent C3H10T1/2 mouse embryo fibroblasts. We have examined the contributions of the Sp1 and E2F binding sites in the repression of CT gene expression. Immunoprecipitation experiments showed that histone deacetylase 1 (HDAC1) and HDAC activity are associated with Sp1 in serum-starved cells or during serum stimulation. However, HDAC1 association with E2F was only detected in serum-starved cells. By chromatin immunoprecipitation assays, we detected both direct and indirect association of HDAC1 with the CT promoter. Treatment with the HDAC inhibitor trichostatin A induced CT expression. Our data suggest that HDAC1 plays a critical role in CT repression and that Sp1 and E2F may serve as key targets for HDAC1-mediated CT repression in fibroblasts.

Received for publication, December 19, 2005 , and in revised form, February 16, 2006.

^* This work was supported by a grant from the Canadian Institutes of Health Research (MOP 5182). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence may be addressed. Tel.: 54-341-4350661: Fax: 54-341-4804601; E-mail: cbanchio{at}fbioyf.unr.edu.ar. ² Canada Research Chair for the Molecular and Cell Biology of Lipids and Scientist of the Alberta Heritage Foundation for Medical Research. To whom correspondence may be addressed. Tel.: 780-492-8286; Fax: 780-492-3383; E-mail: dennis.vance{at}ualberta.ca.

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