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25-Hydroxyvitamin D$_3$ 1α-Hydroxylase and Vitamin D Synthesis

Ken-ichi Takeyama, Sachiko Kitanaka, Takashi Sato, Masato Kobori, Junn Yanagisawa and Shigeaki Kato
Science
New Series, Vol. 277, No. 5333 (Sep. 19, 1997), pp. 1827-1830
Stable URL: http://www.jstor.org/stable/2893844
Page Count: 4
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Abstract

Renal 25-hydroxyvitamin D$_3$ 1α-hydroxylase [1α(OH)ase] catalyzes metabolic activation of 25-hydroxyvitamin D$_3$ into 1α,25-dihydroxyvitamin D$_3$ [1α25(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$_{VD1\alpha}$). 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.

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