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Volume 271, Number 47, Issue of November 22, 1996 pp. 29715-29721
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Transcriptional Synergism between Vitamin D-responsive Elements in the Rat 25-Hydroxyvitamin D3 24-Hydroxylase (CYP24) Promoter

(Received for publication, April 8, 1996, and in revised form, August 26, 1996)

David M. Kerry , Prem P. Dwivedi , Christopher N. Hahn , Howard A. Morris , John L. Omdahl and Brian K. May

From the Department of Biochemistry, University of Adelaide, Adelaide, South Australia 5005, Australia and the  Department of Biochemistry, University of New Mexico, Albequerque, New Mexico 87131

Transcription of the CYP24 gene is induced by 1,25-(OH)2D3 through a vitamin D receptor-dependent process. The functional activities of three possible vitamin D response elements (VDREs), located on the antisense strand of the rat CYP24 promoter, were investigated by transient expression of native and mutant promoter constructs in COS-1, JTC-12, and ROS 17/2.8 cells. A putative VDRE with a half-site spacing of 6 base pairs at -249/-232 (VDRE-3) did not contribute to 1,25-(OH)2D3 induced expression in the native promoter, although activity has been reported when the element was fused to the heterologous thymidine kinase promoter. Two VDREs with half-site spacings of 3 base pairs at -150/-136 and -258/-244 (VDRE-1 and VDRE-2, respectively), showed transcriptional synergism in COS-1 cells when treated with 1,25-(OH)2D3 (10-7 to 10-11 M). The contribution of both VDREs was hormone-concentration dependent from 10-10 to 10-12 M, with VDRE-1 demonstrating greatest sensitivity to 1,25-(OH)2D3. Transactivation by VDRE-1 was always greater than VDRE-2, but the converse was observed for the binding of vitamin D receptor-retinoid X receptor complex by each VDRE in gel mobility shift assays. The synergy observed between VDRE-1 and VDRE-2 may have important implications in cellular responses to different circulating levels of 1,25-(OH)2D3.


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