Unique property of liver mitochondrial P450 to catalyze the two physiologically important reactions involved in both cholesterol catabolism and vitamin D activation

FEBS Lett. 1990 Nov 12;274(1-2):175-7. doi: 10.1016/0014-5793(90)81357-t.

Abstract

The cDNA for vitamin D 25-hydroxylase in rat liver mitochondria was transfected in COS cells in order to confirm our previous postulation that both 5 beta-cholestane-3 alpha, 7 alpha, 12 alpha-triol 27-hydroxylation and vitamin D 25-hydroxylation are catalyzed by a common enzyme. As a result it was found that both enzyme activities could be reconstituted from the solubilized extract of mitochondria of these cells, NADPH, NADPH-adrenodoxin reductase and adrenodoxin, giving unequivocal evidence that the two enzyme activities are catalyzed by a common enzyme.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 25-Hydroxyvitamin D3 1-alpha-Hydroxylase / genetics
  • 25-Hydroxyvitamin D3 1-alpha-Hydroxylase / metabolism*
  • Animals
  • Blotting, Western
  • Cell Line
  • Cholesterol / metabolism*
  • Cytochrome P-450 Enzyme System / metabolism*
  • Mitochondria, Liver / enzymology*
  • Rats
  • Transfection
  • Vitamin D / metabolism*

Substances

  • Vitamin D
  • Cytochrome P-450 Enzyme System
  • Cholesterol
  • 25-Hydroxyvitamin D3 1-alpha-Hydroxylase