Long-chain acyl-CoA synthetases and fatty acid channeling

Authors: Mashek, Douglas G; Li, Lei O; Coleman, Rosalind A

Source: Future Lipidology, Volume 2, Number 4, August 2007 , pp. 465-476(12)

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Abstract:

Thirteen homologous proteins comprise the long-chain acyl-CoA synthetase (ACSL), fatty acid transport protein (FATP), and bubblegum (ACSBG) subfamilies 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.

Keywords: acyl-CoA; ββ-oxidation; fatty acid; glycerolipid; phospholipid; triacylglycerol

Document Type: Research article

DOI: http://dx.doi.org/10.2217/17460875.2.4.465

Publication date: 2007-08-01

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Future Lipidology addresses therapeutic strategies and emerging topics in this complex area of cardiovascular medicine. The journal delivers essential information in concise, at-a-glance article formats. Key advances in the field are reported and analyzed by international experts, providing an authoritative but accessible forum.
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