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

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Coenzymes
Fibroblasts
Oxidoreductases
Fatty Acids
Linoleic Acid
Oxidation
Acyl-CoA Dehydrogenases
Long-Chain Acyl-CoA Dehydrogenase
Acyl-CoA Dehydrogenase
Myristic Acid
Chain length
Carbon

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Beta-oxidation of long-chain fatty acids by human fibroblasts : Evidence for a novel long-chain acyl-coenzyme a dehydrogenase. / Kelley, Richard I.

In: Biochemical and Biophysical Research Communications, Vol. 182, No. 3, 14.02.1992, p. 1002-1007.

Research output: Contribution to journalArticle

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