Beta-oxidation of long-chain fatty acids by human fibroblasts: Evidence for a novel long-chain acyl-coenzyme a dehydrogenase

Richard I. Kelley

Research output: Contribution to journalArticle

Abstract

Fibroblasts from patients with long-chain acyl-CoA dehydrogenase deficiency were found to oxidize [1-14C]linoleate at an average rate of 60% of normal but [9,10(n)-3H]myristate at an average rate of only 37% of normal, a relationship reverse from that predicted by the chain-length specificities of the three known straight-chain mitochondrial acyl-CoA dehydrogenases. The residual long-chain beta-oxidative activity was found to be mitochondrial and associated with the accumulation of tetradecadienoate (C14:2w6) when the mutant fibroblasts were incubated with 100 μmol/L linoleate (C18:2w6) or eicosadienoate (C20:2w6). The results suggest the presence in human fibroblasts of a novel acyl-CoA dehydrogenase with activity toward 15 to 20 carbon-length fatty acids.

Original languageEnglish (US)
Pages (from-to)1002-1007
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume182
Issue number3
DOIs
StatePublished - Feb 14 1992

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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