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Acyl-CoA synthetase long-chain family member 1

acyl-CoA synthetase
The protein encoded by this gene is an isozyme of the long-chain fatty-acid-coenzyme A ligase family. Although differing in substrate specificity, subcellular localization, and tissue distribution, all isozymes of this family convert free long-chain fatty acids into fatty acyl-CoA esters, and thereby play a key role in lipid biosynthesis and fatty acid degradation. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, HAD, CAN, V1a, Insulin
Papers using acyl-CoA synthetase antibodies
The rice OsRad21-4, an orthologue of yeast Rec8 protein, is required for efficient meiosis
Zhang Dabing et al., In Plant Physiology, 2005
... Fatty Acyl-CoA Synthetase is required for pollen development and sporopollenin biosynthesis in ...
Papers on acyl-CoA synthetase
An indexed, mapped mutant library enables reverse genetics studies of biological processes in Chlamydomonas reinhardtii.
Jonikas et al., Stanford, United States. In Plant Cell, Feb 2016
This study revealed a central role of the long-chain acyl-CoA synthetase LCS2 in the production of triacylglycerol from de novo synthesized fatty acids.
SREBP2 activation induces hepatic long-chain acyl-CoA synthetase 1 expression in vivo and in vitro through a SRE motif of ACSL1 C-promoter.
Liu et al., Palo Alto, United States. In J Biol Chem, Feb 2016
UNASSIGNED: Long-chain acyl-CoA synthetase 1 (ACSL1) plays a key role in fatty acid metabolism.
Genetic association of long-chain acyl-CoA synthetase 1 variants with fasting glucose, diabetes and subclinical atherosclerosis.
Bornfeldt et al., United States. In J Lipid Res, Jan 2016
UNASSIGNED: Long-chain acyl-CoA synthetase 1 (ACSL1) converts free fatty acids into acyl-CoAs.
Characterization of the promoter region of the bovine long-chain acyl-CoA synthetase 1 gene: Roles of E2F1, Sp1, KLF15, and E2F4.
Zhang et al., China. In Sci Rep, Dec 2015
Long-chain acyl-CoA synthetase 1 (ACSL1) plays key roles in fatty acid transport and degradation, as well as lipid synthesis.
Effects of Fatty Acid Quality and Quantity in the Japanese Diet on the Suppression of Lipid Accumulation.
Tsuduki et al., In J Oleo Sci, Dec 2015
DNA microarray analysis showed the 1975 diet suppressed Acyl-CoA synthetase and prostaglandin D2 synthase mRNA expressions in white adipose tissue.
Polyunsaturated fatty acid-phospholipid remodeling and inflammation.
Surette et al., Québec, Canada. In Curr Opin Endocrinol Diabetes Obes, Apr 2015
The expression of specific acyl-CoA synthetase, lysophospholipid acyltransferase and phospholipase A2 isotypes has recently been shown to have an impact on membrane PUFA content, on the production of lipid mediators and on inflammation.
Long-chain acyl-CoA synthetase in fatty acid metabolism involved in liver and other diseases: an update.
Qing et al., Hengyang, China. In World J Gastroenterol, Apr 2015
Long-chain acyl-CoA synthetase (ACSL) family members include five different ACSL isoforms, each encoded by a separate gene and have multiple spliced variants.
Lithium and the other mood stabilizers effective in bipolar disorder target the rat brain arachidonic acid cascade.
Rapoport, Bethesda, United States. In Acs Chem Neurosci, 2014
Lithium and carbamazepine also reduced expression of cytosolic phospholipase A2 (cPLA2) IVA, which releases AA from membrane phospholipids, whereas valproate uncompetitively inhibited in vitro acyl-CoA synthetase-4, which recycles AA into phospholipid.
Acyl-CoA metabolism and partitioning.
Coleman et al., In Annu Rev Nutr, 2013
The initial step in their synthesis is the activation of fatty acids by one of 13 long-chain acyl-CoA synthetase isoforms.
Intestinal acyl-CoA synthetase 5: activation of long chain fatty acids and behind.
Gassler et al., Aachen, Germany. In World J Gastroenterol, 2013
One of these modifiers is acyl-CoA synthetase 5 (ACSL5).
Microbial production of short-chain alkanes.
Lee et al., Taejŏn, South Korea. In Nature, 2013
A modified thioesterase was used to convert short-chain fatty acyl-ACPs to the corresponding FFAs, which were then converted to SCAs by the sequential reactions of E. coli fatty acyl-CoA synthetase, Clostridium acetobutylicum fatty acyl-CoA reductase and Arabidopsis thaliana fatty aldehyde decarbonylase.
Alternatively activated macrophages produce catecholamines to sustain adaptive thermogenesis.
Chawla et al., Palo Alto, United States. In Nature, 2012
Acting via the β(3)-adrenergic receptors, noradrenaline induces lipolysis in white adipocytes, whereas it stimulates the expression of thermogenic genes, such as PPAR-γ coactivator 1a (Ppargc1a), uncoupling protein 1 (Ucp1) and acyl-CoA synthetase long-chain family member 1 (Acsl1), in brown adipocytes.
Exome sequencing identifies ACSF3 as a cause of combined malonic and methylmalonic aciduria.
Venditti et al., Bethesda, United States. In Nat Genet, 2011
ACSF3 deficiency is the first human disorder identified as caused by mutations in a gene encoding a member of the acyl-CoA synthetase family, a diverse group of evolutionarily conserved proteins, and may emerge as one of the more common human metabolic disorders.
Adipose acyl-CoA synthetase-1 directs fatty acids toward beta-oxidation and is required for cold thermogenesis.
Coleman et al., Chapel Hill, United States. In Cell Metab, 2010
Long-chain acyl-CoA synthetase-1 (ACSL1) contributes 80% of total ACSL activity in adipose tissue and was believed to be essential for the synthesis of triacylglycerol.
Gene-nutrient interactions with dietary fat modulate the association between genetic variation of the ACSL1 gene and metabolic syndrome.
Roche et al., Dublin, Ireland. In J Lipid Res, 2010
Data show that ACSL1 rs9997745 polymorphism influences metabolic syndrome risk, most likely via disturbances in fatty acid metabolism, which was modulated by dietary fat consumption, particularly PUFA intake, suggesting novel gene-nutrient interactions.
Multiple erythroid isoforms of human long-chain acyl-CoA synthetases are produced by switch of the fatty acid gate domains.
Kuypers et al., Oakland, United States. In Bmc Mol Biol, 2005
Based on homology, two new isoforms for ACSL1 were predicted and characterized, one represented a switch of the Phe- to the Tyr-Gate domain motif, the other resulted from the exclusion of both.
Fatty acyl-coenzyme A is required for budding of transport vesicles from Golgi cisternae.
Rothman et al., Princeton, United States. In Cell, 1989
Using an inhibitor of long-chain acyl-CoA synthetase, we demonstrate that the fatty acid has to be activated by CoA to stimulate transport.
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