25-Hydroxyvitamin D 3 1α-Hydroxylase and Vitamin D Synthesis-Reference-Cited by-同舟云学术

25-Hydroxyvitamin D 3 1α-Hydroxylase and Vitamin D Synthesis

Published:1997-09-19 Issue:5333 Volume:277 Page:1827-1830
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Takeyama Ken-ichi¹²³,Kitanaka Sachiko¹²³,Sato Takashi¹²³,Kobori Masato¹²³,Yanagisawa Junn¹²³,Kato Shigeaki¹²³

Affiliation:

1. K. Takeyama, S. Kitanaka, T. Sato, J. Yanagisawa, Institute of Molecular and Cellular Biosciences, University of Tokyo, Yayoi, Bunkyo-ku, Tokyo 113, Japan.

2. M. Kobori, Molecular Medicine Laboratories, Institute for Drug Discovery Research, Yamanouchi Pharmaceutical, 21 Miyukigaoka, Tukuba-shi, Ibaraki 305, Japan.

3. 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.

Abstract

Renal 25–hydroxyvitamin D 3 1α-hydroxylase [1α(OH)ase] catalyzes metabolic activation of 25–hydroxyvitamin D 3 into 1α,25–dihydroxyvitamin D 3 [1α,25(OH) 2 D 3 ], an active form of vitamin D, and is inhibited by 1α,25(OH) 2 D 3 . 1α(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 (P450 VD1 α ). Expression of 1α(OH)ase was suppressed by 1α,25(OH) 2 D 3 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 1α(OH)ase through liganded VDR.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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