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Nucleic Acids Research 2005 33(8):2440-2451; doi:10.1093/nar/gki502
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Published online 29 April 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Article

Regulation of the human cyclin C gene via multiple vitamin D3-responsive regions in its promoter

Lasse Sinkkonen, Marjo Malinen, Katri Saavalainen, Sami Väisänen and Carsten Carlberg*

Department of Biochemistry, University of Kuopio PO Box 1627, FIN-70211 Kuopio, Finland

*To whom correspondence should be addressed. Tel: +358 17 163062; Fax: +358 17 2811510; Email: carlberg{at}messi.uku.fi

Received January 13, 2005. Revised March 22, 2005. Accepted March 22, 2005.

The candidate human tumor suppressor gene cyclin C is a primary target of the anti-proliferative hormone 1{alpha},25-dihydroxyvitamin D3 [1{alpha},25(OH)2D3], but binding sites for the 1{alpha},25(OH)2D3 receptor (VDR), so-called 1{alpha},25(OH)2D3 response elements (VDREs), have not yet been identified in the promoter of this gene. We screened various cancer cell lines by quantitative PCR and found that the 1{alpha},25(OH)2D3 inducibility of cyclin C mRNA expression, in relationship with the 24-hydroxylase (CYP24) gene, was best in MCF-7 human breast cancer cells. To characterize the molecular mechanisms, we analyzed 8.4 kb of the cyclin C promoter by using chromatin immunoprecipitation assays (ChIP) with antibodies against acetylated histone 4, VDR and its partner receptor, retinoid X receptor (RXR). The histone 4 acetylation status of all 23 investigated regions of the cyclin C promoter did not change significantly in response to 1{alpha},25(OH)2D3, but four independent promoter regions showed a consistent, 1{alpha},25(OH)2D3-dependent association with VDR and RXR over a time period of 240 min. Combined in silico/in vitro screening identified in each of these promoter regions a VDRE and reporter gene assays confirmed their functionality. Moreover, re-ChIP assays monitored simultaneous association of VDR with RXR, coactivator, mediator and RNA polymerase II proteins on these regions. Since cyclin C protein is associated with those mediator complexes that display transcriptional repressive properties, this study contributes to the understanding of the downregulation of a number of secondary 1{alpha},25(OH)2D3-responding genes.


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