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

Science. 1997 Sep 19;277(5333):1827-30. 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.

MeSH terms

  • 25-Hydroxyvitamin D3 1-alpha-Hydroxylase / genetics*
  • 25-Hydroxyvitamin D3 1-alpha-Hydroxylase / metabolism*
  • Amino Acid Sequence
  • Animals
  • COS Cells
  • Calcifediol / metabolism
  • Calcitriol / biosynthesis*
  • Calcitriol / metabolism
  • Calcitriol / pharmacology
  • Cloning, Molecular
  • Feedback
  • Gene Expression Regulation, Enzymologic*
  • Kidney / enzymology
  • Kidney / metabolism
  • Ligands
  • Mice
  • Mice, Knockout
  • Molecular Sequence Data
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • Receptors, Calcitriol / metabolism
  • Transfection

Substances

  • Ligands
  • RNA, Messenger
  • Receptors, Calcitriol
  • 25-Hydroxyvitamin D3 1-alpha-Hydroxylase
  • Calcitriol
  • Calcifediol

Associated data

  • GENBANK/AB005989
  • GENBANK/AB006034