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Acyl-CoA metabolism and partitioning.
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- Author(s): Grevengoed TJ;Grevengoed TJ; Klett EL; Coleman RA
- Source:
Annual review of nutrition [Annu Rev Nutr] 2014; Vol. 34, pp. 1-30. Date of Electronic Publication: 2014 Apr 10.- Publication Type:
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Review- Language:
English - Source:
- Additional Information
- Source: Publisher: Annual Reviews Country of Publication: United States NLM ID: 8209988 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1545-4312 (Electronic) Linking ISSN: 01999885 NLM ISO Abbreviation: Annu Rev Nutr Subsets: MEDLINE
- Publication Information: Publication: Palo Alto Ca : Annual Reviews
Original Publication: Palo Alto, Calif. : Annual Reviews Inc., c1981- - Subject Terms: Lipid Metabolism* ; Models, Biological*; Acyl Coenzyme A/*metabolism ; Cell Membrane/*metabolism ; Coenzyme A Ligases/*metabolism ; Endoplasmic Reticulum/*metabolism ; Fatty Acid Transport Proteins/*metabolism; Animals ; Cell Membrane/enzymology ; Coenzyme A Ligases/genetics ; Endoplasmic Reticulum/enzymology ; Fatty Acid Transport Proteins/genetics ; Gene Expression Regulation ; Humans ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Protein Transport
- Abstract: Long-chain fatty acyl-coenzyme As (CoAs) are critical regulatory molecules and metabolic intermediates. The initial step in their synthesis is the activation of fatty acids by one of 13 long-chain acyl-CoA synthetase isoforms. These isoforms are regulated independently and have different tissue expression patterns and subcellular locations. Their acyl-CoA products regulate metabolic enzymes and signaling pathways, become oxidized to provide cellular energy, and are incorporated into acylated proteins and complex lipids such as triacylglycerol, phospholipids, and cholesterol esters. Their differing metabolic fates are determined by a network of proteins that channel the acyl-CoAs toward or away from specific metabolic pathways and serve as the basis for partitioning. This review evaluates the evidence for acyl-CoA partitioning by reviewing experimental data on proteins that are believed to contribute to acyl-CoA channeling, the metabolic consequences of loss of these proteins, and the potential role of maladaptive acyl-CoA partitioning in the pathogenesis of metabolic disease and carcinogenesis.
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PLoS One. 2012;7(9):e45087. (PMID: 23024797) - Grant Information: K08 DK090141 United States DK NIDDK NIH HHS; R01 DK059935 United States DK NIDDK NIH HHS; DK59935 United States DK NIDDK NIH HHS; K08DK090141 United States DK NIDDK NIH HHS
- Contributed Indexing: Keywords: acyl-CoA binding protein; acyl-CoA synthetase; bubblegum; cancer; fatty acid binding protein; fatty acid transport protein; metabolic syndrome; triacylglycerol; β-oxidation
- Accession Number: 0 (Acyl Coenzyme A)
0 (Fatty Acid Transport Proteins)
0 (Protein Isoforms)
EC 6.2.1.- (Coenzyme A Ligases) - Publication Date: Date Created: 20140514 Date Completed: 20150330 Latest Revision: 20211021
- Publication Date: 20221213
- Accession Number: PMC5881898
- Accession Number: 10.1146/annurev-nutr-071813-105541
- Accession Number: 24819326
- Source:
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