Long-chain acyl-CoA synthetases and fatty acid channeling

Douglas G. Mashek, Lei O. Li, Rosalind A. Coleman

Research output: Contribution to journalReview article

126 Scopus citations

Abstract

Thirteen homologous proteins comprise the king-chain acyl-CoA synthetase (ACSL), fatty acid transport protein (FATP), and bubblegum (ACSBG) sublamilles that activate long-chain and very-long-chain fatty acids to form acyl-CoAs. Gain- and loss-of-function studies show marked differences in the ability of these enzymes to channel fatty acids into different pathways of complex lipid synthesis. Furthermore, the ability of the ACSLs and FATPs to enhance cellular FA uptake does not always require these proteins to be present on the plasma membrane; instead, fatty acid uptake can be increased by enhancing its conversion to acyl-CoA and its metabolism in downstream pathways. Since altered fatty acid metabolism is a hallmark of numerous metabolic diseases and pathological conditions, the ACSL, FATP and ACSBG isoforms are likely to play important roles in disease etiology.

Original languageEnglish (US)
Pages (from-to)465-476
Number of pages12
JournalFuture Lipidology
Volume2
Issue number4
DOIs
StatePublished - Aug 1 2007

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Keywords

  • Acyl-CoA
  • Fatty acid
  • Glycerolipid
  • Phospholipid
  • Triacylglycerol
  • β-oxidation

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