Acyl-CoA synthase ACSL4: an essential target in ferroptosis and fatty acid metabolism
Long-chain acyl-coenzyme A (CoA) synthase 4 (ACSL4) is an enzyme that esterifies CoA into specific polyunsaturated fatty acids, such as arachidonic acid and adrenic acid. Based on accumulated evidence, the ACSL4-catalyzed biosynthesis of arachidonoyl-CoA contributes to the execution of ferroptosis b...
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| Published in | Chinese medical journal Vol. 136; no. 21; pp. 2521 - 2537 |
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| Main Authors | , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
China
Lippincott Williams & Wilkins
05.11.2023
Lippincott Williams & Wilkins Ovid Technologies Department of Nephrology, The Second Xiangya Hospital, Central South University, Changsha, Hunan 410000, China%Hunan Key Laboratory of Kidney Disease and Blood Purification, Changsha, Hunan 410000, China Wolters Kluwer |
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| Abstract | Long-chain acyl-coenzyme A (CoA) synthase 4 (ACSL4) is an enzyme that esterifies CoA into specific polyunsaturated fatty acids, such as arachidonic acid and adrenic acid. Based on accumulated evidence, the ACSL4-catalyzed biosynthesis of arachidonoyl-CoA contributes to the execution of ferroptosis by triggering phospholipid peroxidation. Ferroptosis is a type of programmed cell death caused by iron-dependent peroxidation of lipids; ACSL4 and glutathione peroxidase 4 positively and negatively regulate ferroptosis, respectively. In addition, ACSL4 is an essential regulator of fatty acid (FA) metabolism. ACSL4 remodels the phospholipid composition of cell membranes, regulates steroidogenesis, and balances eicosanoid biosynthesis. In addition, ACSL4-mediated metabolic reprogramming and antitumor immunity have attracted much attention in cancer biology. Because it facilitates the cross-talk between ferroptosis and FA metabolism, ACSL4 is also a research hotspot in metabolic diseases and ischemia/reperfusion injuries. In this review, we focus on the structure, biological function, and unique role of ASCL4 in various human diseases. Finally, we propose that ACSL4 might be a potential therapeutic target. |
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| AbstractList | Long-chain acyl-coenzyme A (CoA) synthase 4 (ACSL4) is an enzyme that esterifies CoA into specific polyunsaturated fatty acids, such as arachidonic acid and adrenic acid. Based on accumulated evidence, the ACSL4-catalyzed biosynthesis of arachidonoyl-CoA contributes to the execution of ferroptosis by triggering phospholipid peroxidation. Ferroptosis is a type of programmed cell death caused by iron-dependent peroxidation of lipids; ACSL4 and glutathione peroxidase 4 positively and negatively regulate ferroptosis, respectively. In addition, ACSL4 is an essential regulator of fatty acid (FA) metabolism. ACSL4 remodels the phospholipid composition of cell membranes, regulates steroidogenesis, and balances eicosanoid biosynthesis. In addition, ACSL4-mediated metabolic reprogramming and antitumor immunity have attracted much attention in cancer biology. Because it facilitates the cross-talk between ferroptosis and FA metabolism, ACSL4 is also a research hotspot in metabolic diseases and ischemia/reperfusion injuries. In this review, we focus on the structure, biological function, and unique role of ASCL4 in various human diseases. Finally, we propose that ACSL4 might be a potential therapeutic target.ABSTRACTLong-chain acyl-coenzyme A (CoA) synthase 4 (ACSL4) is an enzyme that esterifies CoA into specific polyunsaturated fatty acids, such as arachidonic acid and adrenic acid. Based on accumulated evidence, the ACSL4-catalyzed biosynthesis of arachidonoyl-CoA contributes to the execution of ferroptosis by triggering phospholipid peroxidation. Ferroptosis is a type of programmed cell death caused by iron-dependent peroxidation of lipids; ACSL4 and glutathione peroxidase 4 positively and negatively regulate ferroptosis, respectively. In addition, ACSL4 is an essential regulator of fatty acid (FA) metabolism. ACSL4 remodels the phospholipid composition of cell membranes, regulates steroidogenesis, and balances eicosanoid biosynthesis. In addition, ACSL4-mediated metabolic reprogramming and antitumor immunity have attracted much attention in cancer biology. Because it facilitates the cross-talk between ferroptosis and FA metabolism, ACSL4 is also a research hotspot in metabolic diseases and ischemia/reperfusion injuries. In this review, we focus on the structure, biological function, and unique role of ASCL4 in various human diseases. Finally, we propose that ACSL4 might be a potential therapeutic target. Long-chain acyl-coenzyme A (CoA) synthase 4 (ACSL4) is an enzyme that esterifies CoA into specific polyunsaturated fatty acids, such as arachidonic acid and adrenic acid. Based on accumulated evidence, the ACSL4-catalyzed biosynthesis of arachidonoyl-CoA contributes to the execution of ferroptosis by triggering phospholipid peroxidation. Ferroptosis is a type of programmed cell death caused by iron-dependent peroxidation of lipids; ACSL4 and glutathione peroxidase 4 positively and negatively regulate ferroptosis, respectively. In addition, ACSL4 is an essential regulator of fatty acid (FA) metabolism. ACSL4 remodels the phospholipid composition of cell membranes, regulates steroidogenesis, and balances eicosanoid biosynthesis. In addition, ACSL4-mediated metabolic reprogramming and antitumor immunity have attracted much attention in cancer biology. Because it facilitates the cross-talk between ferroptosis and FA metabolism, ACSL4 is also a research hotspot in metabolic diseases and ischemia/reperfusion injuries. In this review, we focus on the structure, biological function, and unique role of ASCL4 in various human diseases. Finally, we propose that ACSL4 might be a potential therapeutic target. |
| Abstract_FL | Long-chain acyl-coenzyme A (CoA) synthase 4 (ACSL4) is an enzyme that esterifies CoA into specific polyunsaturated fatty acids, such as arachidonic acid and adrenic acid. Based on accumulated evidence, the ACSL4-catalyzed biosynthesis of arachidonoyl-CoA contributes to the execution of ferroptosis by triggering phospholipid peroxidation. Ferroptosis is a type of programmed cell death caused by iron-dependent peroxidation of lipids; ACSL4 and glutathione peroxidase 4 positively and negatively regulate ferroptosis, respectively. In addition, ACSL4 is an essential regulator of fatty acid (FA) metabolism. ACSL4 remodels the phospholipid composition of cell membranes, regulates steroidogenesis, and balances eicosanoid biosynthesis. In addition, ACSL4-mediated metabolic reprogramming and antitumor immunity have attracted much attention in cancer biology. Because it facilitates the cross-talk between ferroptosis and FA metabolism, ACSL4 is also a research hotspot in metabolic diseases and ischemia/reperfusion injuries. In this review, we focus on the structure, biological function, and unique role of ASCL4 in various human diseases. Finally, we propose that ACSL4 might be a potential therapeutic target. |
| Author | Li, Li Liu, Chongbin Luo, Shilu Jiang, Na Sun, Lin Ding, Kaiyue Yang, Ming |
| AuthorAffiliation | Department of Nephrology, The Second Xiangya Hospital, Central South University, Changsha, Hunan 410000, China%Hunan Key Laboratory of Kidney Disease and Blood Purification, Changsha, Hunan 410000, China |
| AuthorAffiliation_xml | – name: Department of Nephrology, The Second Xiangya Hospital, Central South University, Changsha, Hunan 410000, China%Hunan Key Laboratory of Kidney Disease and Blood Purification, Changsha, Hunan 410000, China – name: 1 Department of Nephrology, The Second Xiangya Hospital, Central South University, Changsha, Hunan 410000, China – name: 2 Hunan Key Laboratory of Kidney Disease and Blood Purification, Changsha, Hunan 410000, China |
| Author_FL | Yang Ming Jiang Na Ding Kaiyue Liu Chongbin Sun Lin Luo Shilu Li Li |
| Author_FL_xml | – sequence: 1 fullname: Ding Kaiyue – sequence: 2 fullname: Liu Chongbin – sequence: 3 fullname: Li Li – sequence: 4 fullname: Yang Ming – sequence: 5 fullname: Jiang Na – sequence: 6 fullname: Luo Shilu – sequence: 7 fullname: Sun Lin |
| Author_xml | – sequence: 1 givenname: Kaiyue surname: Ding fullname: Ding, Kaiyue organization: Department of Nephrology, The Second Xiangya Hospital, Central South University, Changsha, Hunan 410000, China – sequence: 2 givenname: Chongbin surname: Liu fullname: Liu, Chongbin organization: Department of Nephrology, The Second Xiangya Hospital, Central South University, Changsha, Hunan 410000, China – sequence: 3 givenname: Li surname: Li fullname: Li, Li organization: Department of Nephrology, The Second Xiangya Hospital, Central South University, Changsha, Hunan 410000, China – sequence: 4 givenname: Ming surname: Yang fullname: Yang, Ming organization: Department of Nephrology, The Second Xiangya Hospital, Central South University, Changsha, Hunan 410000, China – sequence: 5 givenname: Na surname: Jiang fullname: Jiang, Na organization: Department of Nephrology, The Second Xiangya Hospital, Central South University, Changsha, Hunan 410000, China – sequence: 6 givenname: Shilu surname: Luo fullname: Luo, Shilu organization: Department of Nephrology, The Second Xiangya Hospital, Central South University, Changsha, Hunan 410000, China – sequence: 7 givenname: Lin surname: Sun fullname: Sun, Lin organization: Department of Nephrology, The Second Xiangya Hospital, Central South University, Changsha, Hunan 410000, China |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/37442770$$D View this record in MEDLINE/PubMed |
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| Keywords | Ferroptosis Metabolic diseases Long-chain acyl-coenzyme A (CoA) synthase 4 (ACSL4) Fatty acid metabolism Ischemia/reperfusion Cancer |
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| PublicationTitle_FL | Chinese Medical Journal |
| PublicationYear | 2023 |
| Publisher | Lippincott Williams & Wilkins Lippincott Williams & Wilkins Ovid Technologies Department of Nephrology, The Second Xiangya Hospital, Central South University, Changsha, Hunan 410000, China%Hunan Key Laboratory of Kidney Disease and Blood Purification, Changsha, Hunan 410000, China Wolters Kluwer |
| Publisher_xml | – name: Lippincott Williams & Wilkins – name: Lippincott Williams & Wilkins Ovid Technologies – name: Department of Nephrology, The Second Xiangya Hospital, Central South University, Changsha, Hunan 410000, China%Hunan Key Laboratory of Kidney Disease and Blood Purification, Changsha, Hunan 410000, China – name: Wolters Kluwer |
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| Snippet | Long-chain acyl-coenzyme A (CoA) synthase 4 (ACSL4) is an enzyme that esterifies CoA into specific polyunsaturated fatty acids, such as arachidonic acid and... |
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| StartPage | 2521 |
| SubjectTerms | Adenosine Cholesterol Fatty acids Ferroptosis Hypoxia Intellectual disabilities Kinases Lipids Metabolism MicroRNAs Oxidation Phosphatase Polyunsaturated fatty acids Proteins Review |
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| Title | Acyl-CoA synthase ACSL4: an essential target in ferroptosis and fatty acid metabolism |
| URI | https://ovidsp.ovid.com/ovidweb.cgi?T=JS&NEWS=n&CSC=Y&PAGE=fulltext&D=ovft&AN=00029330-990000000-00688 https://www.ncbi.nlm.nih.gov/pubmed/37442770 https://www.proquest.com/docview/2885952558 https://www.proquest.com/docview/2838253814 https://d.wanfangdata.com.cn/periodical/zhcmj202321001 https://pubmed.ncbi.nlm.nih.gov/PMC10617883 https://doaj.org/article/ae47db64a2d44548b7e6d8524cfdb3e4 |
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