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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...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Lippincott Williams & Wilkins
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10617883/ https://www.ncbi.nlm.nih.gov/pubmed/37442770 http://dx.doi.org/10.1097/CM9.0000000000002533 |
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author | Ding, Kaiyue Liu, Chongbin Li, Li Yang, Ming Jiang, Na Luo, Shilu Sun, Lin |
author_facet | Ding, Kaiyue Liu, Chongbin Li, Li Yang, Ming Jiang, Na Luo, Shilu Sun, Lin |
author_sort | Ding, Kaiyue |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-10617883 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Lippincott Williams & Wilkins |
record_format | MEDLINE/PubMed |
spelling | pubmed-106178832023-11-05 Acyl-CoA synthase ACSL4: an essential target in ferroptosis and fatty acid metabolism Ding, Kaiyue Liu, Chongbin Li, Li Yang, Ming Jiang, Na Luo, Shilu Sun, Lin Chin Med J (Engl) Review Articles 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. Lippincott Williams & Wilkins 2023-11-05 2023-07-05 /pmc/articles/PMC10617883/ /pubmed/37442770 http://dx.doi.org/10.1097/CM9.0000000000002533 Text en Copyright © 2023 The Chinese Medical Association, produced by Wolters Kluwer, Inc. under the CC-BY-NC-ND license. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution-Non Commercial-No Derivatives License 4.0 (CCBY-NC-ND), where it is permissible to download and share the work provided it is properly cited. The work cannot be changed in any way or used commercially without permission from the journal. http://creativecommons.org/licenses/by-nc-nd/4.0 (https://creativecommons.org/licenses/by-nc-nd/4.0/) |
spellingShingle | Review Articles Ding, Kaiyue Liu, Chongbin Li, Li Yang, Ming Jiang, Na Luo, Shilu Sun, Lin Acyl-CoA synthase ACSL4: an essential target in ferroptosis and fatty acid metabolism |
title | Acyl-CoA synthase ACSL4: an essential target in ferroptosis and fatty acid metabolism |
title_full | Acyl-CoA synthase ACSL4: an essential target in ferroptosis and fatty acid metabolism |
title_fullStr | Acyl-CoA synthase ACSL4: an essential target in ferroptosis and fatty acid metabolism |
title_full_unstemmed | Acyl-CoA synthase ACSL4: an essential target in ferroptosis and fatty acid metabolism |
title_short | Acyl-CoA synthase ACSL4: an essential target in ferroptosis and fatty acid metabolism |
title_sort | acyl-coa synthase acsl4: an essential target in ferroptosis and fatty acid metabolism |
topic | Review Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10617883/ https://www.ncbi.nlm.nih.gov/pubmed/37442770 http://dx.doi.org/10.1097/CM9.0000000000002533 |
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