Human cytochrome P450 27C1 catalyzes 3,4-desaturation of retinoids

FEBS Lett. 2016 May;590(9):1304-12. doi: 10.1002/1873-3468.12167. Epub 2016 Apr 17.

Abstract

In humans, a considerable fraction of the retinoid pool in skin is derived from vitamin A2 (all-trans 3,4-dehydroretinal). Vitamin A2 may be locally generated by keratinocytes, which can convert vitamin A1 (all-trans retinol) into vitamin A2 in cell culture. We report that human cytochrome P450 (hP450) 27C1, a previously 'orphan' enzyme, can catalyze this reaction. Purified recombinant hP450 27C1 bound and desaturated all-trans retinol, retinal, and retinoic acid, as well as 11-cis-retinal. Although the physiological role of 3,4-dehydroretinoids in humans is unclear, we have identified hP450 27C1 as an enzyme capable of efficiently mediating their formation.

Keywords: Cytochrome P450; desaturation; mass spectrometry; retinoids; spectroscopy.

Publication types

  • Letter
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, N.I.H., Extramural

MeSH terms

  • Cytochrome P450 Family 27 / metabolism*
  • Humans
  • Retinoids / metabolism*

Substances

  • Retinoids
  • CYP27C1 protein, human
  • Cytochrome P450 Family 27