25-Hydroxyvitamin D3 1alpha-hydroxylase and vitamin D synthesis

Science. 1997 Sep 19;277(5333):1827-30. doi: 10.1126/science.277.5333.1827.

K Takeyama ¹, S Kitanaka, T Sato, M Kobori, J Yanagisawa, S Kato

Affiliations

Affiliation

1 Institute of Molecular and Cellular Biosciences, University of Tokyo, Yayoi, Bunkyo-ku, Tokyo 113, Japan.

PMID: 9295274 DOI: 10.1126/science.277.5333.1827

Abstract

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.

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