Involvement of microsomal fatty aldehyde dehydrogenase in the alpha-oxidation of phytanic acid

FEBS Lett. 1998 Jun 16;429(3):225-8. doi: 10.1016/s0014-5793(98)00574-2.

Abstract

We investigated the role of microsomal fatty aldehyde dehydrogenase (FALDH) in the conversion of pristanal into pristanic acid. Cultured skin fibroblasts from controls and patients with Sjögren-Larsson syndrome (SLS) who are genetically deficient in FALDH activity were incubated with [2,3-(3)H]phytanic acid. The release of aqueous-soluble radioactivity by the SLS cells was decreased to 25% of normal, consistent with an intact formation of pristanal but a deficiency of further oxidation. SLS cells also accumulated four-fold more radioactivity in N-alkyl-phosphatidyl ethanolamine, which arises from incorporation of free aldehyde into phosphatidyl ethanolamine. Recombinant human FALDH expressed in Chinese hamster ovary cells readily oxidized pristanal and cultured fibroblasts from SLS patients showed a severe deficiency in FALDH activity (13% of normal) when pristanal was used as substrate. Nevertheless, SLS patients did not accumulate phytanic acid in their plasma. We conclude that FALDH is involved in the oxidation of pristanal to pristanic acid and that this reaction is deficient in patients with SLS.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Aldehyde Oxidoreductases / genetics
  • Aldehyde Oxidoreductases / metabolism*
  • Aldehydes / metabolism*
  • Animals
  • CHO Cells
  • Cricetinae
  • Fatty Acids / metabolism*
  • Fibroblasts / cytology
  • Fibroblasts / metabolism
  • Humans
  • Microsomes / enzymology*
  • Oxidation-Reduction
  • Phosphatidylethanolamines / metabolism
  • Phytanic Acid / metabolism*
  • Recombinant Proteins / metabolism
  • Sjogren-Larsson Syndrome / enzymology*

Substances

  • Aldehydes
  • Fatty Acids
  • Phosphatidylethanolamines
  • Recombinant Proteins
  • pristanal
  • Phytanic Acid
  • pristanic acid
  • Aldehyde Oxidoreductases
  • long-chain-aldehyde dehydrogenase