The dual role of FSP1 in programmed cell death: resisting ferroptosis in the cell membrane and promoting necroptosis in the nucleus of THP-1 cells.


Journal

Molecular medicine (Cambridge, Mass.)
ISSN: 1528-3658
Titre abrégé: Mol Med
Pays: England
ID NLM: 9501023

Informations de publication

Date de publication:
15 Jul 2024
Historique:
received: 02 02 2024
accepted: 10 06 2024
medline: 16 7 2024
pubmed: 16 7 2024
entrez: 15 7 2024
Statut: epublish

Résumé

Acute monocytic leukemia-M5 (AML-M5) remains a challenging disease due to its high morbidity and poor prognosis. In addition to the evidence mentioned earlier, several studies have shown that programmed cell death (PCD) serves a critical function in treatment of AML-M5. However, the role and relationship between ferroptosis and necroptosis in AML-M5 remains unclear. THP-1 cells were mainly treated with Erastin and IMP-366. The changes of ferroptosis and necroptosis levels were detected by CCK-8, western blot, quantitative real-time PCR, and electron microscopy. Flow cytometry was applied to detect the ROS and lipid ROS levels. MDA, 4-HNE, GSH and GSSG were assessed by ELISA kits. Intracellular distribution of FSP1 was studied by immunofluorescent staining and western blot. The addition of the myristoylation inhibitor IMP-366 to erastin-treated acute monocytic leukemia cell line THP-1 cell not only resulted in greater susceptibility to ferroptosis characterized by lipid peroxidation, glutathione (GSH) depletion and mitochondrial shrinkage, as the FSP1 position on membrane was inhibited, but also increased p-RIPK1 and p-MLKL protein expression, as well as a decrease in caspase-8 expression, and triggered the characteristic necroptosis phenomena, including cytoplasmic translucency, mitochondrial swelling, membranous fractures by FSP1 migration into the nucleus via binding importin α2. It is interesting to note that ferroptosis inhibitor fer-1 reversed necroptosis. We demonstrated that inhibition of myristoylation by IMP-366 is capable of switching ferroptosis and ferroptosis-dependent necroptosis in THP-1 cells. In these findings, FSP1-mediated ferroptosis and necroptosis are described as alternative mechanisms of PCD of THP-1 cells, providing potential therapeutic strategies and targets for AML-M5.

Sections du résumé

BACKGROUND BACKGROUND
Acute monocytic leukemia-M5 (AML-M5) remains a challenging disease due to its high morbidity and poor prognosis. In addition to the evidence mentioned earlier, several studies have shown that programmed cell death (PCD) serves a critical function in treatment of AML-M5. However, the role and relationship between ferroptosis and necroptosis in AML-M5 remains unclear.
METHODS METHODS
THP-1 cells were mainly treated with Erastin and IMP-366. The changes of ferroptosis and necroptosis levels were detected by CCK-8, western blot, quantitative real-time PCR, and electron microscopy. Flow cytometry was applied to detect the ROS and lipid ROS levels. MDA, 4-HNE, GSH and GSSG were assessed by ELISA kits. Intracellular distribution of FSP1 was studied by immunofluorescent staining and western blot.
RESULTS RESULTS
The addition of the myristoylation inhibitor IMP-366 to erastin-treated acute monocytic leukemia cell line THP-1 cell not only resulted in greater susceptibility to ferroptosis characterized by lipid peroxidation, glutathione (GSH) depletion and mitochondrial shrinkage, as the FSP1 position on membrane was inhibited, but also increased p-RIPK1 and p-MLKL protein expression, as well as a decrease in caspase-8 expression, and triggered the characteristic necroptosis phenomena, including cytoplasmic translucency, mitochondrial swelling, membranous fractures by FSP1 migration into the nucleus via binding importin α2. It is interesting to note that ferroptosis inhibitor fer-1 reversed necroptosis.
CONCLUSION CONCLUSIONS
We demonstrated that inhibition of myristoylation by IMP-366 is capable of switching ferroptosis and ferroptosis-dependent necroptosis in THP-1 cells. In these findings, FSP1-mediated ferroptosis and necroptosis are described as alternative mechanisms of PCD of THP-1 cells, providing potential therapeutic strategies and targets for AML-M5.

Identifiants

pubmed: 39009982
doi: 10.1186/s10020-024-00861-4
pii: 10.1186/s10020-024-00861-4
doi:

Substances chimiques

Reactive Oxygen Species 0
AGFG1 protein, human 0
N-(4-(N-(3-methoxypyrazin-2-yl)sulfamoyl)phenyl)-3-(5-nitrothiophene-2-yl)acrylamide 0
Piperazines 0
erastin 0
Acrylamides 0
Sulfonamides 0
RNA-Binding Proteins 0
Nuclear Pore Complex Proteins 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

102

Subventions

Organisme : the National Natural Sciences Foundation of China
ID : 81800386
Organisme : the Hunan Provincial Natural Science Foundation of China
ID : 2021JJ30020
Organisme : the financial supports from the scientific research project of health commission of Hunan province
ID : 202101021784
Organisme : the financial supports from the science and technology plan project of Hengyang City
ID : 202150063459
Organisme : College Students' Research Learning and Innovative Experiment Plan in University of South China
ID : 202110555098
Organisme : College Students' Research Learning and Innovative Experiment Plan in University of South China
ID : S202110555307
Organisme : College Students' Research Learning and Innovative Experiment Plan in University of South China
ID : X202110555516
Organisme : College Students' Research Learning and Innovative Experiment Plan in University of South China
ID : X202110555523
Organisme : College Students' Research Learning and Innovative Experiment Plan in University of South China
ID : X202110555529
Organisme : College Students' Research Learning and Innovative Experiment Plan in University of South China
ID : S202210555256
Organisme : College Students' Research Learning and Innovative Experiment Plan in University of South China
ID : 2022X10555115

Informations de copyright

© 2024. The Author(s).

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Auteurs

Xiaoqian Tan (X)

Department of Physiology, Clinical Anatomy and Reproductive Medicine Application Institute, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, China.
School of Basic Medical Sciences, Xiangnan University, Chenzhou, 423000, Hunan, China.

Yinling He (Y)

Department of Physiology, Clinical Anatomy and Reproductive Medicine Application Institute, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, China.

Panpan Yu (P)

Department of Physiology, Clinical Anatomy and Reproductive Medicine Application Institute, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, China.

Yunong Deng (Y)

Department of Physiology, Clinical Anatomy and Reproductive Medicine Application Institute, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, China.

Zhongcheng Xie (Z)

Department of Physiology, Clinical Anatomy and Reproductive Medicine Application Institute, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, China.

Jiami Guo (J)

Department of Physiology, Clinical Anatomy and Reproductive Medicine Application Institute, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, China.

Qin Hou (Q)

Department of Physiology, Clinical Anatomy and Reproductive Medicine Application Institute, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, China.

Pin Li (P)

Department of Physiology, Clinical Anatomy and Reproductive Medicine Application Institute, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, China.

Xiaoyan Lin (X)

Department of Physiology, Clinical Anatomy and Reproductive Medicine Application Institute, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, China.

Siyu Ouyang (S)

Department of Physiology, Clinical Anatomy and Reproductive Medicine Application Institute, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, China.

Wentao Ma (W)

Department of Physiology, Clinical Anatomy and Reproductive Medicine Application Institute, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, China.

Yushu Xie (Y)

Class of Clinical Medicine, University of South China, Hengyang, 421001, Hunan, China.

Zilong Guo (Z)

Class of Clinical Medicine, University of South China, Hengyang, 421001, Hunan, China.

Dandan Chen (D)

Class of Clinical Medicine, University of South China, Hengyang, 421001, Hunan, China.

Zhixia Zhang (Z)

Class of Clinical Medicine, University of South China, Hengyang, 421001, Hunan, China.

Yunyu Zhu (Y)

Class of Clinical Medicine, University of South China, Hengyang, 421001, Hunan, China.

Fei Huang (F)

Class of Clinical Medicine, University of South China, Hengyang, 421001, Hunan, China.

Ziye Zhao (Z)

Class of Clinical Medicine, University of South China, Hengyang, 421001, Hunan, China.

Cen Zhang (C)

Class of Clinical Medicine, University of South China, Hengyang, 421001, Hunan, China.

Zhirong Guo (Z)

Class of Clinical Medicine, University of South China, Hengyang, 421001, Hunan, China.

Xi Chen (X)

Department of Physiology, Clinical Anatomy and Reproductive Medicine Application Institute, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, China.

Tianhong Peng (T)

Department of Physiology, Clinical Anatomy and Reproductive Medicine Application Institute, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, China. 2602406228@qq.com.

Liang Li (L)

Department of Physiology, Clinical Anatomy and Reproductive Medicine Application Institute, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, China. 26002860@qq.com.

Wei Xie (W)

Department of Physiology, Clinical Anatomy and Reproductive Medicine Application Institute, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, China. weixiehy@126.com.

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