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Volume 271, Number 48, Issue of November 29, 1996 pp. 30381-30385
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Functional Assessment of Two Vitamin D-responsive Elements in the Rat 25-Hydroxyvitamin D₃ 24-Hydroxylase Gene

(Received for publication, November 27, 1995, and in revised form, May 14, 1996)

Yoshihiko Ohyama , Keiichi Ozono ^¶ , Motoyuki Uchida , Michiko Yoshimura , Toshimasa Shinki ^** , Tatsuo Suda ^** and Osamu Yamamoto

From the  Graduate Department of Gene Science, Faculty of Science, Hiroshima University, 1-3-1 Kagamiyama, Higashi-Hiroshima 739, Japan, ^¶ Osaka Medical Center for Maternal and Child Health, 840 Murodo-cho, Izumi, Osaka 590-02, Japan,  Bio-Medical Research Laboratories, Kureha Chemical Industry Company, Ltd., 3-26-2 Hyakunin-cho, Shinjuku-ku, Tokyo 169, Japan, and ^** Department of Biochemistry, School of Dentistry, Showa University, 1-5-8 Hatanodai, Shinagawa-ku, Tokyo 142, Japan

Two vitamin D-responsive elements (VDRE-1 and VDRE-2) were recently identified in the 5-upstream region of the rat 25-hydroxyvitamin D₃ 24-hydroxylase gene at 151/137 and 259/245, respectively. We studied the transcriptional regulation of this gene by vitamin D by means of mutational analysis. Introducing mutations into VDRE-1 and VDRE-2 in the native promoter 291/+9 reduced vitamin D-dependent chloramphenicol acetyltransferase activity by 86 and 41%, respectively. Mutation of the direct repeat 169/155 located at 3 base pairs upstream of VDRE-1 also caused 50% decrease of chloramphenicol acetyltransferase activity. Connection of the element 169/155 to VDRE-1 enhanced the vitamin D responsiveness of VDRE-1 5-fold through the heterologous -globin promoter. The fragment 291/102 containing the two VDREs showed two shifted bands in the presence of the vitamin D receptor and retinoid X receptor in gel retardation analysis, and the appearance of the slower migrating band indicates that two sets of receptor complexes bind to this fragment simultaneously. These results demonstrate that VDRE-1 is a stronger mediator of vitamin D function than VDRE-2 due to the presence of the accessory element 169/155 located adjacent to VDRE-1, although VDRE-2 exhibits a smaller dissociation constant for the vitamin D receptor-retinoid X receptor complex than VDRE-1.

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