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

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Science  19 Sep 1997:
Vol. 277, Issue 5333, pp. 1827-1830
DOI: 10.1126/science.277.5333.1827

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Abstract

Renal 25–hydroxyvitamin D3 1α-hydroxylase [1α(OH)ase] catalyzes metabolic activation of 25–hydroxyvitamin D3 into 1α,25–dihydroxyvitamin D3[1α,25(OH)2D3], an active form of vitamin D, and is inhibited by 1α,25(OH)2D3. 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 (P450VD1 α). Expression of 1α(OH)ase was suppressed by 1α,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 1α(OH)ase through liganded VDR.

  • * To whom correspondence should be addressed. E-mail: uskato{at}hongo.ecc.u-tokyo.ac.jp

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