Protein tyrosine phosphatase 1 protects human pancreatic cancer from erastin-induced ferroptosis

Huang, Xiao-Dong; Xiao, Fengjun; Guo, Yutong; Sun, Yang; Zhang, Yikun; Shi, Xiaorui

doi:10.1016/j.asjsur.2021.11.048

Cited by 6 publications

(3 citation statements)

References 38 publications

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“…Ye et al [156] found that the abrogation of adenosine 5′-diphosphate ribosylation factor 6 (ARF6) could increase the ACSL4 protein levels and, thus, promote RSL3-induced ferroptosis in pancreatic cancer cells, and ROSI inhibiting ACSL4 could abolish this effect, indicating that ARF6 is an upstream regulator of ACSL4. Similarly, in pancreatic ductal adenocarcinoma, the suppression of ACSL4 expression by upregulated tyrosine phosphatase mitochondria 1 (protein tyrosine phosphatase, mitochondrial 1) could inhibit ferroptosis [157] . Moreover, ACSL4 is also involved in cervical cancer, although its role has not been clearly elucidated.…”

Section: Acsl4 In Human Diseasesmentioning

confidence: 99%

“…Similarly, in pancreatic ductal adenocarcinoma, the suppression of ACSL4 expression by upregulated tyrosine phosphatase mitochondria 1 (protein tyrosine phosphatase, mitochondrial 1) could inhibit ferroptosis. [ 157 ] Moreover, ACSL4 is also involved in cervical cancer, although its role has not been clearly elucidated. The circular RNA LIM domain only 1 (LOM1) was found to be downregulated in cervical cancer tissues and could function as a competing endogenous RNA by sponging miR-4192 to repress the target gene ACSL4 .…”

Section: Acsl4 In Human Diseasesmentioning

confidence: 99%

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Acyl-CoA synthase ACSL4: an essential target in ferroptosis and fatty acid metabolism

Ding

Liu

et al. 2023

Chinese Medical Journal

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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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Section: Acsl4 In Human Diseasesmentioning

confidence: 99%

Section: Acsl4 In Human Diseasesmentioning

confidence: 99%

Acyl-CoA synthase ACSL4: an essential target in ferroptosis and fatty acid metabolism

Ding

Liu

et al. 2023

Chinese Medical Journal

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“…The expression of ACSL4 was downregulated in PDAC and negatively correlated with the expression of PTPMT1 [ 63 ]. High PTPMT1 levels inhibit ferroptosis by suppressing ACSL4 expression, yielding a lower overall survival rate in PDAC.…”

Section: Acsl3 and Acsl4 In Cancersmentioning

confidence: 99%

ACSL3 and ACSL4, Distinct Roles in Ferroptosis and Cancers

Yang

Zhu

Wang

et al. 2022

Cancers

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The long-chain fatty acyl CoA synthetase (ACSLs) family of enzymes contributes significantly to lipid metabolism and produces acyl-coenzyme A by catalyzing fatty acid oxidation. The dysregulation of ACSL3 and ACSL4, which belong to the five isoforms of ACSLs, plays a key role in cancer initiation, development, metastasis, and tumor immunity and may provide several possible therapeutic strategies. Moreover, ACSL3 and ACSL4 are crucial for ferroptosis, a non-apoptotic cell death triggered by the accumulation of membrane lipid peroxides due to iron overload. Here, we present a summary of the current knowledge on ACSL3 and ACSL4 and their functions in various cancers. Research on the molecular mechanisms involved in the regulation of ferroptosis is critical to developing targeted therapies for cancer.

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