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These results suggest that ACSL1, ACSL4 and ACSL5 expression is regulated by ER signaling pathways and ACSL5 is a potential novel biomarker for predicting prognosis of breast cancer patients.
Study identified a genetic variant in the 3'-UTR region of ACSL1 gene (rs8086) that may play a significant role in predicting outcomes of stage II/III patients with colon cancer, so that patients with T/T genotype had a significantly higher risk of tumor recurrence than those carrying at least one C allele.
The mRNA levels of ACSL1 were positively associated with those of HBXIP in clinical breast cancer tissues. Thus, we conclude that the oncoprotein HBXIP is able to up-regulate ACSL1 through activating the transcriptional factor Sp1 in breast cancer.
evidence in humans of ACSL1 SNPs associated with fasting glucose, diabetes, and subclinical atherosclerosis
SRE motif in ACSL1 is essential for SREBP2-mediated activation of C-ACSL1 gene transcription.
ACSL1 is a programmable mediator of insulin sensitivity and cellular lipid content.
the cell surface protein CD36/FAT directly facilitates fatty acid transport across the plasma membrane, whereas the intracellular acyl-CoA synthetases FATP4 and ACSL1 enhance fatty acid uptake indirectly by metabolic trapping
Data indicate that expression of miR-205 is negatively related to that of ACSL1 in clinical hepatocellular carcinoma (HCC) tissues.
INSR rs1366600, ACSL1 rs2292899 and FABP2 rs11724758 could influence the susceptibility to type 2 diabetes in Chinese Han population, most likely through their effects on the specific miRNA-binding sites.
long-chain acyl-CoA synthetase 1 has a role in eicosapentaenoic acid suppression of palmitate-induced cytokine production
Findings suggest that the ACSL1 gene polymorphism rs6552828 is not associated with elite endurance athletic status in Caucasians, yet a marginal association seems to exist for the Chinese (Han) male population.
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.
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.
ACSL1-mediated metabolic trapping of exogenous LCFA accelerates LCFA uptake rates, albeit to a lesser extent in females, which distinctly affects LCFA trafficking to acyl intermediates but not triglyceride storage or mitochondrial oxidation and is affected by female sex hormones.
Data (including data from studies in cell line from knockout mice) suggest high incorporation of long-chain fatty acids, partly mediated by Acsl1, plays role in supply of octanoic acid for ghrelin acylation/lipoylation in ghrelin-producing cells.
Acyl-CoA synthetase 1 deficiency alters cardiolipin species and impairs mitochondrial function
long-chain acyl-CoA synthetase isoform 1 (ACSL1) deficiency in the heart activated mTORC1, thereby inhibiting autophagy and increasing the number of damaged mitochondria.
Acsl1(M-/-) mice were more insulin sensitive, and, during an overnight fast, their respiratory exchange ratio was higher, indicating greater glucose use and during endurance exercise, Acsl1(M-/-) mice ran only 48% as far as controls.
These data indicate that Acsl1-deficiency causes diastolic dysfunction and that mTOR activation is linked to the development of cardiac hypertrophy in Acsl1(H-/-) mice.
Data indicate that the expression levels of ACSL1 and its metabolite triglyceride levels were remarkably increased in hepatitis B virus X protein (HBx)-induced liver cancer tissues from the HBx transgenic mice model.
Increases understanding of the role of ACSL1 in monocytes/macrophages in inflammation and diabetes-accelerated atherosclerosis offers hope for new treatment to combat diabetic vascular disease[review]
Acyl-CoA synthetase 1 is induced by Gram-negative bacteria and lipopolysaccharide and is required for phospholipid turnover in stimulated macrophages
Endothelial ACSL1 is not required for inflammatory and apoptotic effects of a saturated fatty acid-rich environment.
the reduced ABCA1 and cholesterol efflux in macrophages subjected to conditions of diabetes and elevated fatty load may, at least in part, be mediated by ACSL1
Acsl1 knockdown stimulated expression of lipogenic genes.
ACSL1 plays a critical role by promoting the inflammatory phenotype of macrophages associated with type 1 diabetes
Acsl1 is required for heart fatty acid oxidation. Heart-specific Acsl1 deficiency causes cardiac hypertrophy.
Acsl1(A-/-) adipocytes incorporated [(14)C]oleate into glycerolipids normally, but fatty acid oxidation rates were 50%-90% lower than in control adipocytes and mitochondria.
O-GlcNAc interrupts a known interaction between Sp1 and sterol regulatory element binding protein 2 (SREBP2), thereby inhibiting expression of the gene encoding acetyl-CoA synthetase 1, which is involved in lipid synthesis.
Normoleptinemic control ACS-transgenic mice developed severe dilated cardiomyopathy with thickened left ventricular walls and profound impairment of systolic function on echocardiogram
Together, our findings suggest that a constitutive interaction between FATP1 and ACSL1 contributes to the efficient cellular uptake of LCFAs in adipocytes through vectorial acylation.
primary role of ACSL1 in adipocytes not in control of lipid influx, as previously considered, but in lipid efflux and fatty acid-induced insulin resistance
The pig ACSL1 gene expresses differently in different tissues and pig breeds.
Authors have sequenced 3,013 bp of the pig acyl coenzyme A long-chain synthetase 1 (ACSL1) gene.
The initial QTL analysis suggested the ACSL1 gene as a candidate gene for fatty acid composition in bovine skeletal muscle; subsequent analyses indicate that ACSL1 or a gene in close proximity plays a functional role in the lipid composition of beef.
The results of this study suggest that suggest that SLC27A6, ACSL1, FABP3, AGPAT6, and LPIN1 coordinately regulate the channeling of fatty acids toward copious milk fat synthesis in bovine mammary.
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.
, LACS 2
, acyl-CoA synthetase 1
, fatty-acid-Coenzyme A ligase, long-chain 1
, fatty-acid-Coenzyme A ligase, long-chain 2
, lignoceroyl-CoA synthase
, long-chain acyl-CoA synthetase 1
, long-chain acyl-CoA synthetase 2
, long-chain fatty acid-CoA ligase 2
, long-chain fatty-acid-coenzyme A ligase 1
, long-chain-fatty-acid--CoA ligase 1
, palmitoyl-CoA ligase 1
, palmitoyl-CoA ligase 2
, paltimoyl-CoA ligase 1
, acetate-CoA ligase
, acetyl-CoA synthetase
, acetyl-Coenzyme A synthetase 1 (ADP forming)
, fatty acid Coenzyme A ligase, long chain 2
, Acyl CoA synthetase, long chain
, long-chain-fatty-acid--CoA ligase, liver isozyme
, acyl coenzyme A synthetase long-chain 1
, fatty acid coenzyme A ligase long-chain 2
, palmitoyl-CoA ligase