Journal
FUTURE LIPIDOLOGY
Volume 2, Issue 4, Pages 465-476Publisher
FUTURE MEDICINE LTD
DOI: 10.2217/17460875.2.4.465
Keywords
acyl-CoA; beta-oxidation; fatty acid; glycerolipid; phospholipid; triacylglycerol
Categories
Funding
- NIDDK NIH HHS [R01 DK059935, F32 DK068993, P30 DK034987, P30 DK056350, R01 DK059935-07] Funding Source: Medline
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Thirteen homologous proteins comprise the long-chain acyl-CoA synthetase (ACSL), fatty acid transport protein (FATF), 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.
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