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Journal articles on the topic 'ACSL4'

Author: Grafiati

Published: 4 June 2021

Last updated: 9 February 2022

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1

Durgan, David J., Justin K. Smith, Margaret A. Hotze, Oluwaseun Egbejimi, Karalyn D. Cuthbert, Vlad G. Zaha, Jason R. B. Dyck, E. Dale Abel, and Martin E. Young. "Distinct transcriptional regulation of long-chain acyl-CoA synthetase isoforms and cytosolic thioesterase 1 in the rodent heart by fatty acids and insulin." American Journal of Physiology-Heart and Circulatory Physiology 290, no. 6 (June 2006): H2480—H2497. http://dx.doi.org/10.1152/ajpheart.01344.2005.

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The molecular mechanism(s) responsible for channeling long-chain fatty acids (LCFAs) into oxidative versus nonoxidative pathways is (are) poorly understood in the heart. Intracellular LCFAs are converted to long-chain fatty acyl-CoAs (LCFA-CoAs) by a family of long-chain acyl-CoA synthetases (ACSLs). Cytosolic thioesterase 1 (CTE1) hydrolyzes cytosolic LCFA-CoAs to LCFAs, generating a potential futile cycle at the expense of ATP utilization. We hypothesized that ACSL isoforms and CTE1 are differentially regulated in the heart during physiological and pathophysiological conditions. Using quantitative RT-PCR, we report that the five known acsl isoforms ( acsl1, acsl3, acsl4, acsl5, and acsl6) and cte1 are expressed in whole rat and mouse hearts, as well as adult rat cardiomyocytes (ARCs). Streptozotocin-induced insulin-dependent diabetes (4 wk) and fasting (≤24 h) both dramatically induced cte1 and repressed acsl6 mRNA, with no significant effects on the other acsl isoforms. In contrast, high-fat feeding (4 wk) induced cte1 without affecting expression of the acsl isoforms in the heart. Investigation into the mechanism(s) responsible for these transcriptional changes uncovered roles for peroxisome proliferator-activated receptor-α (PPARα) and insulin as regulators of specific acsl isoforms and cte1 in the heart. Culturing ARCs with oleate (0.1–0.4 mM) or the PPARα agonists WY-14643 (1 μM) and fenofibrate (10 μM) consistently induced acsl1 and cte1. Conversely, PPARα null mouse hearts exhibited decreased acsl1 and cte1 expression. Culturing ARCs with insulin (10 nM) induced acsl6, whereas specific loss of insulin signaling within the heart (cardiac-specific insulin receptor knockout mice) caused decreased acsl6 expression. Our data expose differential regulation of acsl isoforms and cte1 in the heart, where acsl1 and cte1 are PPARα-regulated genes, whereas acsl6 is an insulin-regulated gene.

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2

Wang, Wei, Xiao Hao, Lina Han, Zhe Yan, Wen-Jun Shen, Dachuan Dong, Kathrin Hasbargen, et al. "Tissue-Specific Ablation of ACSL4 Results in Disturbed Steroidogenesis." Endocrinology 160, no. 11 (August 27, 2019): 2517–28. http://dx.doi.org/10.1210/en.2019-00464.

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Abstract ACSL4 is a member of the ACSL family that catalyzes the conversion of long-chain fatty acids to acyl-coenzyme As, which are essential for fatty-acid incorporation and utilization in diverse metabolic pathways, including cholesteryl ester synthesis. Steroidogenic tissues such as the adrenal gland are particularly enriched in cholesteryl esters of long-chain polyunsaturated fatty acids, which constitute an important pool supplying cholesterol for steroid synthesis. The current studies addressed whether ACSL4 is required for normal steroidogenesis. CYP11A1 promoter‒mediated Cre was used to generate steroid tissue‒specific ACSL4 knockout (KO) mice. Results demonstrated that ACSL4 plays an important role in adrenal cholesteryl ester formation, as well as in determining the fatty acyl composition of adrenal cholesteryl esters, with ACSL4 deficiency leading to reductions in cholesteryl ester storage and alterations in cholesteryl ester composition. Statistically significant reductions in corticosterone and testosterone production, but not progesterone production, were observed in vivo, and these deficits were accentuated in ex vivo and in vitro studies of isolated steroid tissues and cells from ACSL4-deficient mice. However, these effects on steroid production appear to be due to reductions in cholesteryl ester stores rather than disturbances in signaling pathways. We conclude that ACSL4 is dispensable for normal steroidogenesis.

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3

Wu, Jinchun, Zhengxi He, Xianyu Liu, Yanhua Mou, Jingchen Lu, Chaojun Duan, and Bin Li. "High expression of ferroptosis-sensitizer ACSL4 as an indicator of good response to immune checkpoint inhibitors and preferable survival with increased TIICs in skin cutaneous melanoma." Journal of Clinical Oncology 39, no. 15_suppl (May 20, 2021): e21594-e21594. http://dx.doi.org/10.1200/jco.2021.39.15_suppl.e21594.

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e21594 Background: Skin cutaneous melanoma (SKCM) has a high incidence and mortality. Immune checkpoint inhibitors (ICIs) are promising but show heterogeneous efficacy in the SKCM treatment. T cell-promoted tumor ferroptosis is a vital anti-tumor mechanism of ICIs. Acyl-CoA synthetase long chain family member 4 (ACSL4) can sensitize ferroptosis by facilitating lipid peroxidation. So we proposed that ACSL4 is a positive predictor for ICIs efficacy and correlated with tumor-infiltrating immune cells (TIICs) in SKCM. Methods: The responses of SKCM patients to ICIs were evaluated from Tumor Immune Dysfunction and Exclusion (TIDE) using the gene expression data of The Cancer Genome Atlas (TCGA)-SKCM downloaded from UCSC Xena browser and datasets within TIDE. The correlation between ACLS4 expression and survival was obtained from the Online consensus Survival webserver for Skin Cutaneous Melanoma (OSskcm) and TIDE databases. The relationships between ACSL4 and TIICs were evaluated using the database of Tumor Immune Estimation Resource 2.0 (TIMER2.0). Results: ACSL4 expression was positively correlated with the predicted responder of ICIs in TCGA dataset (R = 0.12, p = 0.0093) and therapy outcomes of ICIs in Gide2019_PD1+CTLA4 (Progression-free survival(PFS), contimuous z = -2.39, p = 0.0169) and Lauss2017_ACT (PFS, contimuous z = -2.08, p = 0.0371; overall survival(OS), contimuous z = -2.96, p = 0.00309). Favorable OS was observed in the patients with high ACSL4 expression in the TCGA (HR = 0.6567, 95% CI = 0.5015̃0.8599, p = 0.0022) and GSE19234 (HR = 0.4135, 95% CI = 0.1748̃0.9784, p = 0.0445) from OSskcm and the GSE8401 (contimuous z = -2,24, p = 0.025) and GSE54467 (contimuous z = -2.26, p = 0.0239) from TIDE database. TIICs including CD8+ T cells, CD4+ T cells (memory, Th2), B cells, neutrophils, monocytes, M1 macrophages, and cancer-associated fibroblasts (CAFs) were positively associated with the expression level of ACSL4. Conclusions: High ACSL4 expression maybe indicates a good response to ICIs and long survival in SKCM. The increased T cells within the tumor microenvironment correlated with high ACSL4 expression possibly implied the synergism effects of ferroptosis and ICIs, deserving further investigation. Keywords: ACSL4, ICIs, TIICs, SKCM.

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4

Singh, Amar B., Chin Fung K. Kan, Fredric B. Kraemer, Raymond A. Sobel, and Jingwen Liu. "Liver-specific knockdown of long-chain acyl-CoA synthetase 4 reveals its key role in VLDL-TG metabolism and phospholipid synthesis in mice fed a high-fat diet." American Journal of Physiology-Endocrinology and Metabolism 316, no. 5 (May 1, 2019): E880—E894. http://dx.doi.org/10.1152/ajpendo.00503.2018.

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Long-chain acyl-CoA synthetase 4 (ACSL4) has a unique substrate specificity for arachidonic acid. Hepatic ACSL4 is coregulated with the phospholipid (PL)-remodeling enzyme lysophosphatidylcholine (LPC) acyltransferase 3 by peroxisome proliferator-activated receptor δ to modulate the plasma triglyceride (TG) metabolism. In this study, we investigated the acute effects of hepatic ACSL4 deficiency on lipid metabolism in adult mice fed a high-fat diet (HFD). Adenovirus-mediated expression of a mouse ACSL4 shRNA (Ad-shAcsl4) in the liver of HFD-fed mice led to a 43% reduction of hepatic arachidonoyl-CoA synthetase activity and a 53% decrease in ACSL4 protein levels compared with mice receiving control adenovirus (Ad-shLacZ). Attenuated ACSL4 expression resulted in a substantial decrease in circulating VLDL-TG levels without affecting plasma cholesterol. Lipidomics profiling revealed that knocking down ACSL4 altered liver PL compositions, with the greatest impact on accumulation of abundant LPC species (LPC 16:0 and LPC 18:0) and lysophosphatidylethanolamine (LPE) species (LPE 16:0 and LPE 18:0). In addition, fasting glucose and insulin levels were higher in Ad-shAcsl4-transduced mice versus control (Ad-shLacZ). Glucose tolerance testing further indicated an insulin-resistant phenotype upon knockdown of ACSL4. These results provide the first in vivo evidence that ACSL4 plays a role in plasma TG and glucose metabolism and hepatic PL synthesis of hyperlipidemic mice.

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5

Wu, Hongxia, and Aiwen Liu. "Long non-coding RNA NEAT1 regulates ferroptosis sensitivity in non-small-cell lung cancer." Journal of International Medical Research 49, no. 3 (March 2021): 030006052199618. http://dx.doi.org/10.1177/0300060521996183.

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Objectives Ferroptosis is caused by iron-dependent lipid peroxide accumulation, the sensitivity of which might be regulated by acyl-CoA synthetase long chain family member 4 (ACSL4). Non-small-cell lung cancer (NSCLC) can resist oxidative stress and reduce the sensitivity of tumor cells to ferroptosis by changing the expression of some proteins. Mechanisms involving ferroptosis sensitivity in NSCLC are not fully understood. Methods A dual-luciferase reporter assay was used to confirm a targeting relationship between long non-coding (lnc)RNA NEAT1 and ACSL4. Overexpression and silencing assays of NEAT1 function were used to determine its roles in cell death (by TUNEL staining) and lipid peroxidation (by malondialdehyde levels). Expression of ferroptosis-related proteins (SLCA11, GPX4, and TFR4) was evaluated by western blot in NSCLC cells treated or not with the ferroptosis inducer erastin. Results Erastin-induced cell death was positively correlated with ACSL4 level. NEAT1 regulated levels of ACSL4 and proteins related to the ferroptosis and classical apoptosis pathways. Levels of ACSL4, SLC7A11, and GPX4 were decreased more by NEAT1 silencing plus erastin than by erastin alone. Conclusion NEAT1 regulates ferroptosis and ferroptosis sensitivity, with the latter depending on ACSL4, suggesting that targeting NEAT1 or ACSL4 may be a viable therapeutic approach to the treatment of NSCLC.

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6

Fan, Yongliang, Ziyin Han, Xubin Lu, Huimin Zhang, Abdelaziz Adam Idriss Arbab, Juan J. Loor, Yi Yang, and Zhangping Yang. "Identification of Milk Fat Metabolism-Related Pathways of the Bovine Mammary Gland during Mid and Late Lactation and Functional Verification of the ACSL4 Gene." Genes 11, no. 11 (November 16, 2020): 1357. http://dx.doi.org/10.3390/genes11111357.

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The concentration of bovine milk fat changes regularly with lactation stages. In particular, milk fat percentage is higher in late lactation than mid lactation. Furthermore, milk fat composition is highly subject to a few genes. Thus, transcriptome sequencing was performed to explore the expression patterns of differentially-expressed genes (DEGs) in the parenchymal mammary gland of Holstein dairy cows between mid and late lactation. The 725 DEGs were screened (fold change > 2 and p-value < 0.05), and the peroxisome proliferator-activated receptor (PPAR) signaling pathway associated with lipid synthesis had a significant variation between the two periods (p-value < 0.05). The activation of the PPAR signal pathway may a key factor in the increasing of milk fat content in late lactation compared to mid lactation. Acyl-CoA synthetase long-chain family member 4 (ACSL4), a member of the PPAR signaling pathway, was upregulated in late lactation compared to mid lactation (p < 0.05). ACSL4 catalyzes the activation of long-chain fatty acids for cellular lipid synthesis. However, it remains uncertain that the molecular mechanism of milk fat synthesis is regulated by ACSL4 in dairy cows. Subsequently, the function verification of ACSL4 was performed in bovine mammary epithelial cells (BMECs). The upregulated expression of ACSL4 was accompanied by the increase of the concentration of intracellular triglycerides, whereas knockdown of ACSL4 decreased the concentration of intracellular triglycerides, which demonstrated that ACSL4 plays an important role in modulating milk fat synthesis. In conclusion, the results displayed that ACSL4 expression regulates triglyceride metabolism in ruminant mammary cells.

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7

Jin, Zheng-Long, Wen-Ying Gao, Shao-Jun Liao, Tao Yu, Qing Shi, Shang-Zhen Yu, and Ye-Feng Cai. "Paeonol inhibits the progression of intracerebral haemorrhage by mediating the HOTAIR/UPF1/ACSL4 axis." ASN Neuro 13 (January 2021): 175909142110106. http://dx.doi.org/10.1177/17590914211010647.

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Intracerebral haemorrhage (ICH) is a devastating subtype of stroke with high morbidity and mortality. It has been reported that paeonol (PAN) inhibits the progression of ICH. However, the mechanism by which paeonol mediates the progression of ICH remains unclear. To mimic ICH in vitro, neuronal cells were treated with hemin. An in vivo model of ICH was established to detect the effect of paeonol on ferroptosis in neurons during ICH. Cell viability was tested by MTT assay. Furthermore, cell injury was detected by GSH, MDA and ROS assays. Ferroptosis was examined by iron assay. RT-qPCR and western blotting were used to detect gene and protein expression, respectively. The correlation among HOTAIR, UPF1 and ACSL4 was explored by FISH, RNA pull-down and RIP assays. Paeonol significantly inhibited the ferroptosis of neurons in ICH mice. In addition, paeonol significantly reversed hemin-induced injury and ferroptosis in neurons, while this phenomenon was notably reversed by HOTAIR overexpression. Moreover, paeonol notably inhibited ferroptosis in hemin-treated neuronal cells via inhibition of ACSL4. Additionally, HOTAIR bound to UPF1, and UPF1 promoted the degradation of ACSL4 by binding to ACSL4. Furthermore, HOTAIR overexpression reversed paeonol-induced inhibition of ferroptosis by mediating the UPF1/ACSL4 axis. Paeonol inhibits the progression of ICH by mediating the HOTAIR/UPF1/ACSL4 axis. Therefore, paeonol might serve as a new agent for the treatment of ICH.

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8

Sen, Progga, Chin Fung Kelvin Kan, Amar B. Singh, Monica Rius, Fredric B. Kraemer, Elizabeth Sztul, and Jingwen Liu. "Identification of p115 as a novel ACSL4 interacting protein and its role in regulating ACSL4 degradation." Journal of Proteomics 229 (October 2020): 103926. http://dx.doi.org/10.1016/j.jprot.2020.103926.

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9

Soupene, Eric, and Frans A. Kuypers. "Multiple Erythroid Isoforms of Human Long-Chain acyl-CoA Synthetases Are Produced by a Switch of the Fatty Acid Gate-Domains." Blood 106, no. 11 (November 16, 2005): 1672. http://dx.doi.org/10.1182/blood.v106.11.1672.1672.

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Abstract In mammals, long-chain acyl-CoA synthetases (ACSL) are necessary for fatty acid degradation, phospholipid remodeling, and production of long acyl-CoA esters that regulate various physiological processes. These enzymes play a crucial role in plasma membrane phospholipid turnover in erythrocytes, maintaining the complex phospholipid molecular species composition essential for proper membrane function. The mechanism by which this highly dynamic turnover together with an ever-changing plasma fatty acid pool maintains phospholipid composition is poorly understood. We have previously cloned Acyl-CoA Synthetase Long-chain member 6 (ACSL6), the isoform responsible for activation of long-chain fatty acids in erythrocytes. Two additional transcript variants of this protein were subsequently isolated from brain and testis. We report the expression of four different variants of ACLS6 in reticulocytes, one as we originally reported, two of which are novel, one as was identified in brain cells. PCR amplifications using primers for the predicted variable regions were performed from cDNAs of CD34 positive erythroid progenitors, K562 cells, fetal blood cells, reticulocytes and placenta. ACSL variants were expressed in E. coli host BL21DE3 cells using the pET28a vector, and detected by His tag immuno detection. Sequence alignments were generated using sequences retrieved from RefSeq and GenBank databases on the NCBI site. Exon and intron definition for ACSL members were obtained using evidence viewer and model maker available at the map viewer page of each gene. We identified four different spliced variants of ACSL6 in erythroid cells based on a mutually exclusive exon pair. Each exon of this pair encodes a slightly different short motif that contains the fatty acid Gate domain, a conserved structural domain found in all vertebrate and invertebrate ACSL homologs. The motif differs in the presence of either the aromatic residue phenylalanine (Phe) or tyrosine (Tyr), and seems to play a role in substrate specificity. One of the new forms contained an exon not found in any other ACSL isoforms. Erythroid precursors also express the closely related ACSL1, and we characterized two additional isoforms of this protein, similar to ACSL6. When analyzed on denaturing SDS polyacrylamide gel both ACSL1 and 6 appeared to exist as a dimer. Based on our results, we propose the generation of two different Gate-domains by alternative splicing of the two exons in these proteins. One represents a switch of the Phe to the Tyr Gate-domain motif, the other resulted of the exclusion of both. Swapping of this motif appears to be common to all mammalian homologs of ACSL1 and 6. We conclude that the Phe to a Tyr substitution in the Gate-domain, or its removal, together with the formation of homo or heterodimers will allow ACSL6 the structural diversity to define substrate specificity that maintains the complex plasma membrane phospholipid molecular species composition in erythrocytes.

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10

Yu, Xiang, Xibi Fang, Hang Xiao, Zhihui Zhao, Steffen Maak, Mengyan Wang, and Runjun Yang. "The effect of acyl-CoA synthetase long-chain family member 5 on triglyceride synthesis in bovine preadipocytes." Archives Animal Breeding 62, no. 1 (May 6, 2019): 257–64. http://dx.doi.org/10.5194/aab-62-257-2019.

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Abstract. Acyl-CoA synthetase long-chain family member 5 (ACSL5) is a member of the acyl coenzyme A (CoA) long-chain synthase families (ACSLs), and it plays a key role in fatty acid metabolism. In this study, we proved an association between the ACSL5 gene and triglyceride metabolism at the cellular level in cattle. pBI-CMV3-ACSL5 and pGPU6/GFP/Neo-ACSL5 plasmids were constructed and transfected into bovine preadipocytes by electroporation. The expression level of ACSL5 was detected by real-time quantitative PCR and western blot. The triglyceride content was detected by a triglyceride kit. The results indicated that the expression level of ACSL5 mRNA and protein in the pBI-CMV3-ACSL5-transfected group was significantly increased compared with those in the control group. Furthermore, the pGPU6/GFP/Neo-ACSL5-transfected group was significantly decreased compared with those in the control group. A cell triglyceride test showed that overexpression or silencing of the ACSL5 gene could affect synthesis of cellular triglycerides. This study investigated the mechanism of ACSL on bovine fat deposition, and also provides a new candidate gene for meat quality traits in beef cattle.

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11

Doll, Sebastian, Bettina Proneth, Yulia Y. Tyurina, Elena Panzilius, Sho Kobayashi, Irina Ingold, Martin Irmler, et al. "ACSL4 dictates ferroptosis sensitivity by shaping cellular lipid composition." Nature Chemical Biology 13, no. 1 (November 14, 2016): 91–98. http://dx.doi.org/10.1038/nchembio.2239.

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12

Wu, Xinyu, Fangming Deng, Yirong Li, Garrett Daniels, Xinxin Du, Qinghu Ren, Jinhua Wang, et al. "ACSL4 promotes prostate cancer growth, invasion and hormonal resistance." Oncotarget 6, no. 42 (November 30, 2015): 44849–63. http://dx.doi.org/10.18632/oncotarget.6438.

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13

Brown, Caitlin W., John J. Amante, Hira Lal Goel, and Arthur M. Mercurio. "The α6β4 integrin promotes resistance to ferroptosis." Journal of Cell Biology 216, no. 12 (September 28, 2017): 4287–97. http://dx.doi.org/10.1083/jcb.201701136.

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Increases in lipid peroxidation can cause ferroptosis, a form of cell death triggered by inhibition of glutathione peroxidase 4 (GPX4), which catalyzes the reduction of lipid peroxides and is a target of ferroptosis inducers, such as erastin. The α6β4 integrin protects adherent epithelial and carcinoma cells from ferroptosis induced by erastin. In addition, extracellular matrix (ECM) detachment is a physiologic trigger of ferroptosis, which is evaded by α6β4. The mechanism that enables α6β4 to evade ferroptosis involves its ability to protect changes in membrane lipids that are proferroptotic. Specifically, α6β4-mediated activation of Src and STAT3 suppresses expression of ACSL4, an enzyme that enriches membranes with long polyunsaturated fatty acids and is required for ferroptosis. Adherent cells lacking α6β4 require an inducer, such as erastin, to undergo ferroptosis because they sustain GPX4 expression, despite their increase in ACSL4. In contrast, ECM detachment of cells lacking α6β4 is sufficient to trigger ferroptosis because GPX4 is suppressed. This causal link between α6β4 and ferroptosis has implications for cancer biology and therapy.

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14

Kuwata, Hiroshi, and Shuntaro Hara. "Role of acyl-CoA synthetase ACSL4 in arachidonic acid metabolism." Prostaglandins & Other Lipid Mediators 144 (October 2019): 106363. http://dx.doi.org/10.1016/j.prostaglandins.2019.106363.

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15

Xu, Yixin, Xuehan Li, Yan Cheng, Mingan Yang, and Rurong Wang. "Inhibition of ACSL4 attenuates ferroptotic damage after pulmonary ischemia‐reperfusion." FASEB Journal 34, no. 12 (October 18, 2020): 16262–75. http://dx.doi.org/10.1096/fj.202001758r.

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16

Yuan, Hua, Xuemei Li, Xiuying Zhang, Rui Kang, and Daolin Tang. "Identification of ACSL4 as a biomarker and contributor of ferroptosis." Biochemical and Biophysical Research Communications 478, no. 3 (September 2016): 1338–43. http://dx.doi.org/10.1016/j.bbrc.2016.08.124.

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17

Ansari, Israr-ul H., Melissa J. Longacre, Scott W. Stoker, Mindy A. Kendrick, Lucas M. O'Neill, Laura J. Zitur, Luis A. Fernandez, James M. Ntambi, and Michael J. MacDonald. "Characterization of Acyl-CoA synthetase isoforms in pancreatic beta cells: Gene silencing shows participation of ACSL3 and ACSL4 in insulin secretion." Archives of Biochemistry and Biophysics 618 (March 2017): 32–43. http://dx.doi.org/10.1016/j.abb.2017.02.001.

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18

Radif, Yassmeen, Haarith Ndiaye, Vasiliki Kalantzi, Ruth Jacobs, Andrew Hall, Shane Minogue, and Mark G. Waugh. "The endogenous subcellular localisations of the long chain fatty acid-activating enzymes ACSL3 and ACSL4 in sarcoma and breast cancer cells." Molecular and Cellular Biochemistry 448, no. 1-2 (February 15, 2018): 275–86. http://dx.doi.org/10.1007/s11010-018-3332-x.

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19

Vurgun, Eren, İrem Yağmur Diker, Neslihan Çoban, Filiz Geyik, Gamze Güven, and Nihan Erginel Ünaltuna. "ACSL4 gen polimorfizminin (rs7886473) metabolik sendrom ve lipid düzeyleri üzerine etkisi." Cukurova Medical Journal 43, Ek 1 (December 30, 2018): 151–57. http://dx.doi.org/10.17826/cumj.407589.

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20

Chang, Caitlin A., Julie Lauzon, Adam Kirton, and Bob Argiropoulos. "An ACSL4 Hemizygous Intragenic Deletion in a Patient With Childhood Stroke." Pediatric Neurology 100 (November 2019): 100–101. http://dx.doi.org/10.1016/j.pediatrneurol.2019.06.014.

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21

Meloni, I., V. Parri, R. De Filippis, F. Ariani, R. Artuso, M. Bruttini, E. Katzaki, et al. "The XLMR gene ACSL4 plays a role in dendritic spine architecture." Neuroscience 159, no. 2 (March 2009): 657–69. http://dx.doi.org/10.1016/j.neuroscience.2008.11.056.

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22

Cooke, Mariana, Ulises Orlando, Paula Maloberti, Ernesto J. Podestá, and Fabiana Cornejo Maciel. "Tyrosine phosphatase SHP2 regulates the expression of acyl-CoA synthetase ACSL4." Journal of Lipid Research 52, no. 11 (September 8, 2011): 1936–48. http://dx.doi.org/10.1194/jlr.m015552.

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23

Feng, Ji, Pei-zhi Lu, Guang-zhi Zhu, Shing Chung Hooi, Yong Wu, Xiao-wei Huang, Hui-qi Dai, et al. "ACSL4 is a predictive biomarker of sorafenib sensitivity in hepatocellular carcinoma." Acta Pharmacologica Sinica 42, no. 1 (June 15, 2020): 160–70. http://dx.doi.org/10.1038/s41401-020-0439-x.

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Torres Ruiz, S., I. Garrido Cano, R. Cervera Vidal, C. Hernando Melia, M. T. M. Martinez, S. Zazo, O. Burgués, et al. "299P MicroRNAs-449 regulate doxorubicin response through ACSL4 modulation in TNBC." Annals of Oncology 32 (September 2021): S494—S495. http://dx.doi.org/10.1016/j.annonc.2021.08.582.

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25

Xing, Xuekun, Hui Wang, Lan Zhao, Yunxiao Bai, Fei Xie, Junjie He, and Chenxi Lv. "Niacin downregulates chemokine (c-c motif) ligand 2 (CCL2) expression and inhibits fat synthesis in rat liver cells." Tropical Journal of Pharmaceutical Research 19, no. 5 (June 26, 2020): 977–82. http://dx.doi.org/10.4314/tjpr.v19i5.10.

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Purpose: To elucidate the role of chemokine (c-c motif) ligand 2 (CCL2) in fat metabolism in hepatocytes. Methods: Following partial hepatectomy, regenerated rat liver cells were isolated and cultured for 24 h were transfected with recombinant plasmid pEGFP-N1-CCL2 using liposomes. Niacin was added to the culture medium to inhibit fat synthesis. CCL2 expression was measured using western blot, while the expression of acly-coa synthetase long chain family 4 (ACSL4) and apolipoprotein E (ApoE) were assessed using real-time PCR. Results: At 12 h after transfection, GFP-positive rates in the pEGFP-N1 and pEGFP-N1-CCL2 transfection groups were 42.4 ± 5.6 % and 45.1 ± 3.5 %, respectively. Expression levels of CCL2 increased over time in pEGFP-N1 transfection group, pEGFP-N1-ccl2 transfection group, and niacin and pEGFP-N1-ccl2 transfection co-treatment group; however, CCL2 expression levels in the niacin and pEGFP-N1-ccl2 transfection co-treatment groups were similar to that of pEGFP-N1 transfection group, which were significantly lower than those of the pEGFP-N1-ccl2 transfection group. Expressionlevel trends of fat-related genes ACSL4 and ApoE were similar to that of CCL2. Conclusion: Niacin downregulates the expression of CCL2, thereby inhibiting lipid synthesis in liver cells. Keywords: Chemokine 2, Niacin, Hepatectomy, Lipid synthesis, Transfection

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Cui, Yu, Yan Zhang, Xiaolong Zhao, Liming Shao, Guoping Liu, Chengjian Sun, Rui Xu, and Zhaolong Zhang. "ACSL4 exacerbates ischemic stroke by promoting ferroptosis-induced brain injury and neuroinflammation." Brain, Behavior, and Immunity 93 (March 2021): 312–21. http://dx.doi.org/10.1016/j.bbi.2021.01.003.

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27

Tian, Xiangyang, Shuyuan Li, and Guoyan Ge. "Apatinib Promotes Ferroptosis in Colorectal Cancer Cells by Targeting ELOVL6/ACSL4 Signaling." Cancer Management and Research Volume 13 (February 2021): 1333–42. http://dx.doi.org/10.2147/cmar.s274631.

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28

Parkes, Heidi A., Elaine Preston, Donna Wilks, Mercedes Ballesteros, Lee Carpenter, Leonie Wood, Edward W. Kraegen, Stuart M. Furler, and Gregory J. Cooney. "Overexpression of acyl-CoA synthetase-1 increases lipid deposition in hepatic (HepG2) cells and rodent liver in vivo." American Journal of Physiology-Endocrinology and Metabolism 291, no. 4 (October 2006): E737—E744. http://dx.doi.org/10.1152/ajpendo.00112.2006.

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Accumulation of intracellular lipid in obesity is associated with metabolic disease in many tissues including liver. Storage of fatty acid as triglyceride (TG) requires the activation of fatty acids to long-chain acyl-CoAs (LC-CoA) by the enzyme acyl-CoA synthetase (ACSL). There are five known isoforms of ACSL (ACSL1, -3, -4, -5, -6), which vary in their tissue specificity and affinity for fatty acid substrates. To investigate the role of ACSL1 in the regulation of lipid metabolism, we used adenoviral-mediated gene transfer to overexpress ACSL1 in the human hepatoma cell-line HepG2 and in liver of rodents. Infection of HepG2 cells with the adenoviral construct AdACSL1 increased ACSL activity >10-fold compared with controls after 24 h. HepG2 cells overexpressing ACSL1 had a 40% higher triglyceride (TG) content (93 ± 3 vs. 67 ± 2 nmol/mg protein in controls, P < 0.05) after 24-h exposure to 1 mM oleate. Furthermore, ACSL1 overexpression produced a 60% increase in cellular LCA-CoA content (160 ± 6 vs. 100 ± 6 nmol/g protein in controls, P < 0.05) and increased [14C]oleate incorporation into TG without significantly altering fatty acid oxidation. In mice, AdACSL1 administration increased ACSL1 mRNA and protein more than fivefold over controls at 4 days postinfection. ACSL1 overexpression caused a twofold increase in TG content in mouse liver (39 ± 4 vs. 20 ± 2 μmol/g wet wt in controls, P < 0.05), and overexpression in rat liver increased [1-14C]palmitate clearance into liver TG. These in vitro and in vivo results suggest a pivotal role for ACSL1 in regulating TG synthesis in liver.

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Ren, Hongyan, Zaidong Hua, Jinhua Meng, Adrian Molenaar, Yanzhen Bi, Ni Cheng, and Xinmin Zheng. "Generation of Acsl4 Gene Knockout Mouse Model by CRISPR/Cas9-Mediated Genome Engineering." Critical Reviews in Biomedical Engineering 47, no. 5 (2019): 419–26. http://dx.doi.org/10.1615/critrevbiomedeng.2019030342.

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Shimbara-Matsubayashi, Satoko, Hiroshi Kuwata, Nobutada Tanaka, Masaru Kato, and Shuntaro Hara. "Analysis on the Substrate Specificity of Recombinant Human Acyl-CoA Synthetase ACSL4 Variants." Biological and Pharmaceutical Bulletin 42, no. 5 (May 1, 2019): 850–55. http://dx.doi.org/10.1248/bpb.b19-00085.

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Budna, Joanna, Piotr Celichowski, Sandra Knap, Maurycy Jankowski, Magdalena Magas, Mariusz J. Nawrocki, Piotr Ramlau, et al. "Fatty Acids Related Genes Expression Undergo Substantial Changes in Porcine Oviductal Epithelial Cells During Long-Term Primary Culture." Medical Journal of Cell Biology 6, no. 2 (September 1, 2018): 39–47. http://dx.doi.org/10.2478/acb-2018-0008.

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Abstract The process of reproduction requires several factors, leading to successful fertilization of an oocyte by a single spermatozoon. One of them is the complete maturity of an oocyte, which is acquired during long stages of folliculogenesis and oogenesis. Additionally, the oviduct, composed of oviductal epithelial cells (OECs), has a prominent influence on this event through sperm modification and supporting oocyte’s movement towards uterus. OECs were isolated from porcine oviducts. Cells were kept in primary in vitro culture for 30 days. After 24h and on days 7, 15 and 30 cells were harvested, and RNA was isolated. Transcript changes were analyzed using microarrays. Fatty acids biosynthetic process and fatty acids transport ontology groups were selected for analysis and described. Results of this study indicated that majority of genes in both ontology groups were up-regulated on day 7, 15 and 30 of primary in vitro culture. We analyzed genes involved in fatty acids biosynthetic process, including: GGT1, PTGES, INSIG1, SCD, ACSL3, FADS2, FADS1, ACSS2, ALOX5AP, ACADL, SYK, ACACA, HSD17B8, FADS3, OXSM, and transport, including: ABCC2, ACSL4, FABP3, PLA2G3, PPARA, SYK, PPARD, ACACA and P2RX7. Elevated levels of fatty acids in bovine and human oviducts are known to reduce proliferation capacity of OECs and promote inflammatory responses in their microenvironment. Most of measured genes could not be connected to reproductive events. However, the alterations in cellular proliferation, differentiation and genes expression during in vitro long-term culture were significant. Thus, we can treat them as putative markers of changes in OECs physiology.

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Li, Yang, Dongcheng Feng, Zhanyu Wang, Yan Zhao, Ruimin Sun, Donghai Tian, Deshun Liu, et al. "Ischemia-induced ACSL4 activation contributes to ferroptosis-mediated tissue injury in intestinal ischemia/reperfusion." Cell Death & Differentiation 26, no. 11 (February 8, 2019): 2284–99. http://dx.doi.org/10.1038/s41418-019-0299-4.

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Cao, Yang, Sutian Wang, Shunqi Liu, Yanli Wang, Haiguo Jin, Huihai Ma, Xiaotong Luo, Yang Cao, and Zhengxing Lian. "Effects of Long-Chain Fatty Acyl-CoA Synthetase 1 on Diglyceride Synthesis and Arachidonic Acid Metabolism in Sheep Adipocytes." International Journal of Molecular Sciences 21, no. 6 (March 17, 2020): 2044. http://dx.doi.org/10.3390/ijms21062044.

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Long-chain fatty acyl-CoA synthetase (ACSLs) is an essential enzyme for the synthesis of fatty acyl-CoA. ACSL1 plays a key role in the synthesis of triglycerides, phospholipids, and cholesterol esters. Background: In the current study, triglyceride content did not increase after overexpression of the ACSL1 gene. Methods: RNA-seq and lipid metabolome profiling were performed to determine why triglyceride levels did not change with ACSL1 overexpression. Results: Fatty acyl-CoA produced by ACSL1 was determined to be involved in the diglyceride synthesis pathway, and diglyceride content significantly increased when ACSL1 was overexpressed. Moreover, the arachidonic acid (AA) content in sheep adipocytes significantly increased, and the level of cyclooxygenase 2 (COX2) expression, the downstream metabolic gene, was significantly downregulated. Knocking down the ACSL1 gene was associated with an increase in COX2 mRNA expression, as well as an increase in prostaglandin content, which is the downstream metabolite of AA. Conclusions: The overexpression of the ACSL1 gene promotes the production of AA via downregulation of COX2 gene expression.

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Pourfarzam, Morteza, Negar Dinarvand, Hossein Khanahmad, SayyedMohammadreza Hakimian, Abdolkarim Sheikhi, and Bahman Rashidi. "Evaluation of long-chain acyl-coenzyme A synthetase 4 (ACSL4) expression in human breast cancer." Research in Pharmaceutical Sciences 15, no. 1 (2020): 48. http://dx.doi.org/10.4103/1735-5362.278714.

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Sun, Xiao-Jie, and Ge-Liang Xu. "Overexpression of Acyl-CoA Ligase 4 (ACSL4) in Patients with Hepatocellular Carcinoma and its Prognosis." Medical Science Monitor 23 (September 9, 2017): 4343–50. http://dx.doi.org/10.12659/msm.906639.

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Park, Sujeong, Jinjoo Oh, Yong-Il Kim, Seong-Kyu Choe, Churl-Hong Chun, and Eun-Jung Jin. "Suppression of ABCD2 dysregulates lipid metabolism via dysregulation of miR-141:ACSL4 in human osteoarthritis." Cell Biochemistry and Function 36, no. 7 (September 27, 2018): 366–76. http://dx.doi.org/10.1002/cbf.3356.

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Ben-Zaken, Sigal, Yoav Meckel, Dan Nemet, and Alon Eliakim. "Prevalence of ACSL (rs6552828) polymorphism among runners." Acta Kinesiologiae Universitatis Tartuensis 24 (January 2, 2019): 121–28. http://dx.doi.org/10.12697/akut.2018.24.09.

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The ACSL A/G polymorphism is associated with endurance trainability. Previous studies have demonstrated that homozygotes of the minor AA allele had a reduced maximal oxygen consumption response to training compared to the common GG allele homozygotes, and that the ACSL A/G single nucleotide polymorphism explained 6.1% of the variance in the VO2max response to endurance training. The contribution of ACSL single nucleotide polymorphism to endurance trainability was shown in nonathletes, however, its potential role in professional athletes is not clear. Moreover, the genetic basis to anaerobic trainability is even less studied. Therefore, the aim of the present study was to examine the prevalence of ACSL single nucleotide polymorphism among professional Israeli long distance runners (n=59), middle distance runners (n=31), sprinters and jumpers (n=48) and non-athletic controls (n=60). The main finding of the present study was that the ACSL1 AA genotype, previously shown to be associated with reduced endurance trainability, was not higher among sprinters and jumpers (15%) compared to middle- (16%) and long-distance runners (15%). This suggests that in contrast to previous studies indicating that the ACSL1 single nucleotide polymorphism may influence endurance trainability among non-athletic individuals, the role of this polymorphism among professional athletes is still not clear.

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Mercade, A., A. Sanchez, and J. M. Folch. "Assignment of theacyl-CoA synthetase long-chain family member 4 (ACSL4)gene to porcine chromosome X." Animal Genetics 36, no. 1 (February 2005): 76. http://dx.doi.org/10.1111/j.1365-2052.2004.01222.x.

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Xiao, Feng-Jun, Dan Zhang, Ye Wu, Qing-Hua Jia, Lin Zhang, Yu-Xiang Li, Yue-Feng Yang, Hua Wang, Chu-Tse Wu, and Li-Sheng Wang. "miRNA-17-92 protects endothelial cells from erastin-induced ferroptosis through targeting the A20-ACSL4 axis." Biochemical and Biophysical Research Communications 515, no. 3 (July 2019): 448–54. http://dx.doi.org/10.1016/j.bbrc.2019.05.147.

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Xiaofei, Jiang, Shi Mingqing, Sui Miao, Yuan Yizhen, Zhang Shuang, Xia Qinhua, and Zhao Kai. "Oleanolic acid inhibits cervical cancer Hela cell proliferation through modulation of the ACSL4 ferroptosis signaling pathway." Biochemical and Biophysical Research Communications 545 (March 2021): 81–88. http://dx.doi.org/10.1016/j.bbrc.2021.01.028.

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Ruść, A., H. Sieczkowska, E. Krzęcio, K. Antosik, A. Zybert, M. Koćwin-Podsiadła, and S. Kamiński. "The association between acyl-CoA synthetase (ACSL4) polymorphism and intramuscular fat content in (Landrace × Yorkshire) × Duroc pigs." Meat Science 89, no. 4 (December 2011): 440–43. http://dx.doi.org/10.1016/j.meatsci.2011.05.008.

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Belkaid, Anissa, Rodney J. Ouellette, and Marc E. Surette. "17β-estradiol-induced ACSL4 protein expression promotes an invasive phenotype in estrogen receptor positive mammary carcinoma cells." Carcinogenesis 38, no. 4 (March 10, 2017): 402–10. http://dx.doi.org/10.1093/carcin/bgx020.

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Pei, Zhaohui, Yandong Liu, Suqin Liu, Wei Jin, Yuanfei Luo, Mingming Sun, Yu Duan, et al. "FUNDC1 insufficiency sensitizes high fat diet intake-induced cardiac remodeling and contractile anomaly through ACSL4-mediated ferroptosis." Metabolism 122 (September 2021): 154840. http://dx.doi.org/10.1016/j.metabol.2021.154840.

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Wei, Xiang, Xin Yi, Xue-Hai Zhu, and Ding-Sheng Jiang. "Posttranslational Modifications in Ferroptosis." Oxidative Medicine and Cellular Longevity 2020 (November 26, 2020): 1–12. http://dx.doi.org/10.1155/2020/8832043.

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Ferroptosis was first coined in 2012 to describe the form of regulated cell death (RCD) characterized by iron-dependent lipid peroxidation. To date, ferroptosis has been implicated in many diseases, such as carcinogenesis, degenerative diseases (e.g., Huntington’s, Alzheimer’s, and Parkinson’s diseases), ischemia-reperfusion injury, and cardiovascular diseases. Previous studies have identified numerous targets involved in ferroptosis; for example, acyl-CoA synthetase long-chain family member 4 (ACSL4) and p53 induce while glutathione peroxidase 4 (GPX4) and apoptosis-inducing factor mitochondria-associated 2 (AIFM2, also known as FSP1) inhibit ferroptosis. At least three major pathways (the glutathione-GPX4, FSP1-coenzyme Q10 (CoQ10), and GTP cyclohydrolase-1- (GCH1-) tetrahydrobiopterin (BH4) pathways) have been identified to participate in ferroptosis regulation. Recent advances have also highlighted the crucial roles of posttranslational modifications (PTMs) of proteins in ferroptosis. Here, we summarize the recently discovered knowledge regarding the mechanisms underlying ferroptosis, particularly the roles of PTMs in ferroptosis regulation.

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Wang, Jiachen, Zhao Wang, Jiaxiang Yuan, Jiaxiang Wang, and Xinsheng Shen. "The positive feedback between ACSL4 expression and O-GlcNAcylation contributes to the growth and survival of hepatocellular carcinoma." Aging 12, no. 9 (May 1, 2020): 7786–800. http://dx.doi.org/10.18632/aging.103092.

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Cui, Canqi, Tingting Li, Yun Xie, Jie Yang, Chenyang Fu, Yixuan Qiu, Linyan Shen, et al. "Enhancing Acsl4 in absence of mTORC2/Rictor drove β-cell dedifferentiation via inhibiting FoxO1 and promoting ROS production." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1867, no. 12 (December 2021): 166261. http://dx.doi.org/10.1016/j.bbadis.2021.166261.

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Sha, Rui, Yaqian Xu, Chenwei Yuan, Xiaonan Sheng, Ziping Wu, Jing Peng, Yaohui Wang, et al. "Predictive and prognostic impact of ferroptosis-related genes ACSL4 and GPX4 on breast cancer treated with neoadjuvant chemotherapy." EBioMedicine 71 (September 2021): 103560. http://dx.doi.org/10.1016/j.ebiom.2021.103560.

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Young, Pamela A., Can E. Senkal, Amanda L. Suchanek, Trisha J. Grevengoed, Dennis D. Lin, Liyang Zhao, Amanda E. Crunk, et al. "Long-chain acyl-CoA synthetase 1 interacts with key proteins that activate and direct fatty acids into niche hepatic pathways." Journal of Biological Chemistry 293, no. 43 (September 6, 2018): 16724–40. http://dx.doi.org/10.1074/jbc.ra118.004049.

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Fatty acid channeling into oxidation or storage modes depends on physiological conditions and hormonal signaling. However, the directionality of this channeling may also depend on the association of each of the five acyl-CoA synthetase isoforms with specific protein partners. Long-chain acyl-CoA synthetases (ACSLs) catalyze the conversion of long-chain fatty acids to fatty acyl-CoAs, which are then either oxidized or used in esterification reactions. In highly oxidative tissues, ACSL1 is located on the outer mitochondrial membrane (OMM) and directs fatty acids into mitochondria for β-oxidation. In the liver, however, about 50% of ACSL1 is located on the endoplasmic reticulum (ER) where its metabolic function is unclear. Because hepatic fatty acid partitioning is likely to require the interaction of ACSL1 with other specific proteins, we used an unbiased protein interaction technique, BioID, to discover ACSL1-binding partners in hepatocytes. We targeted ACSL1 either to the ER or to the OMM of Hepa 1–6 cells as a fusion protein with the Escherichia coli biotin ligase, BirA*. Proteomic analysis identified 98 proteins that specifically interacted with ACSL1 at the ER, 55 at the OMM, and 43 common to both subcellular locations. We found subsets of peroxisomal and lipid droplet proteins, tethering proteins, and vesicle proteins, uncovering a dynamic role for ACSL1 in organelle and lipid droplet interactions. Proteins involved in lipid metabolism were also identified, including acyl-CoA–binding proteins and ceramide synthase isoforms 2 and 5. Our results provide fundamental and detailed insights into protein interaction networks that control fatty acid metabolism.

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Bhat, S. S., K. R. Schmidt, S. Ladd, K. C. Kim, C. E. Schwartz, R. J. Simensen, B. R. DuPont, R. E. Stevenson, and A. K. Srivastava. "Disruption of DMD and deletion of ACSL4 causing developmental delay, hypotonia, and multiple congenital anomalies." Cytogenetic and Genome Research 112, no. 1-2 (November 3, 2005): 170–75. http://dx.doi.org/10.1159/000087531.

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Killion, Elizabeth A., Andrew R. Reeves, Mahmoud A. El Azzouny, Qing-Wu Yan, Defne Surujon, John D. Griffin, Thomas A. Bowman, et al. "A role for long-chain acyl-CoA synthetase-4 (ACSL4) in diet-induced phospholipid remodeling and obesity-associated adipocyte dysfunction." Molecular Metabolism 9 (March 2018): 43–56. http://dx.doi.org/10.1016/j.molmet.2018.01.012.

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