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

K Takeyama, S Kitanaka, T Sato, M Kobori… - Science, 1997 - science.org
K Takeyama, S Kitanaka, T Sato, M Kobori, J Yanagisawa, S Kato
Science, 1997science.org
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 …
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.
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