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Science 19 September 1997:
Vol. 277. no. 5333, pp. 1827 - 1830
DOI: 10.1126/science.277.5333.1827
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Reports

25-Hydroxyvitamin D3 1alpha -Hydroxylase and Vitamin D Synthesis

Ken-ichi Takeyama, Sachiko Kitanaka, Takashi Sato, Masato Kobori, Junn Yanagisawa, Shigeaki Kato *

Renal 25-hydroxyvitamin D3 1alpha -hydroxylase [1alpha (OH)ase] catalyzes metabolic activation of 25-hydroxyvitamin D3 into 1alpha ,25-dihydroxyvitamin D3 [1alpha ,25(OH)2D3], an active form of vitamin D, and is inhibited by 1alpha ,25(OH)2D3. 1alpha (OH)ase, which was cloned from the kidney of mice lacking the vitamin D receptor (VDR-/- mice), is a member of the P450 family of enzymes (P450VD1alpha ). Expression of 1alpha (OH)ase was suppressed by 1alpha ,25(OH)2D3 in VDR+/+ and VDR+/- mice but not in VDR-/- mice. These results indicate that the negative feedback regulation of active vitamin D synthesis is mediated by 1alpha (OH)ase through liganded VDR.

K. Takeyama, S. Kitanaka, T. Sato, J. Yanagisawa, Institute of Molecular and Cellular Biosciences, University of Tokyo, Yayoi, Bunkyo-ku, Tokyo 113, Japan.
M. Kobori, Molecular Medicine Laboratories, Institute for Drug Discovery Research, Yamanouchi Pharmaceutical, 21 Miyukigaoka, Tukuba-shi, Ibaraki 305, Japan.
S. Kato, Institute of Molecular and Cellular Biosciences, University of Tokyo, Yayoi, Bunkyo-ku, Tokyo 113, Japan, and CREST, Japan Science and Technology, 4-1-8 Honcho, Kawaguchi, Saitama 332, Japan.
*   To whom correspondence should be addressed. E-mail: uskato{at}hongo.ecc.u-tokyo.ac.jp

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