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ENO1 promotes liver carcinogenesis through YAP1-dependent arachidonic acid metabolism

ABSTRACT: ENO1 promotes liver carcinogenesis through YAP1-dependent arachidonic acid metabolism

PROVIDER: PRJNA761712 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR15815259.fastq.gz	Fastqsanger.gz
	SRR15815260.fastq.gz	Fastqsanger.gz
	SRR15815261_1.fastq.gz	Fastqsanger.gz
	SRR15815261_2.fastq.gz	Fastqsanger.gz
	SRR15815262_1.fastq.gz	Fastqsanger.gz

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ENO1 promotes liver carcinogenesis through YAP1-dependent arachidonic acid metabolism

Project description:Enolase 1 (ENO1) is a glycolytic enzyme that plays essential roles in various pathological activities including cancer development. However, the mechanisms underlying ENO1-contributed tumorigenesis are not well explained. Here, we uncover that ENO1, as an RNA-binding protein, binds to the cytosine-uracil-guanine-rich elements of YAP1 messenger RNA to promote its translation. ENO1 and YAP1 positively regulate alternative arachidonic acid (AA) metabolism by inverse regulation of PLCB1 and HPGD (15-hydroxyprostaglandin dehydrogenase). The YAP1/PLCB1/HPGD axis-mediated activation of AA metabolism and subsequent accumulation of prostaglandin E2 (PGE2) are responsible for ENO1-mediated cancer progression, which can be retarded by aspirin. Finally, aberrant activation of ENO1/YAP1/PLCB1 and decreased HPGD expression in clinical hepatocellular carcinoma samples indicate a potential correlation between ENO1-regulated AA metabolism and cancer development. These findings underline a new function of ENO1 in regulating AA metabolism and tumorigenesis, suggesting a therapeutic potential for aspirin in patients with liver cancer with aberrant expression of ENO1 or YAP1.

2023-05-19 | GSE183703 | GEO

HDAC5 regulates arachidonic acid metabolism via cPLA2

Project description:We performed HDAC5 knockdown in pancreatic cancer cells along with RNA sequencing. The result helped us to verify that HDAC5 regulates GATA1 dependent cPLA2 expression and arachidonic acid metabolism.

2022-10-11 | GSE185837 | GEO

HDAC5 regulates arachidonic acid metabolism via cPLA2

Project description:HDAC5 regulates arachidonic acid metabolism via cPLA2

| PRJNA770975 | ENA

PCNA regulates metabolism by stabilizing ENO1 and 6PGD

Project description:The essential roles of PCNA as a scaffold protein in DNA replication and repair are well established, while its more recently discovered cytosolic roles are less explored. Alpha-enolase (ENO1) and 6-phosphogluconate dehydrogenase (6PGD), important proteins in glycolysis and the Pentose Phosphate Pathway (PPP), respectively, both contain PCNA interacting motifs. Here we show reduced binding to PCNA when the PCNA interacting motif APIM in ENO1 is mutated. Mutant cells have lower ENO1 protein levels, have reduced glucose consumption, altered glycolytic metabolite and nucleoside phosphate pools and increased activation of the citric acid cycle (TCA) compared to parental cells. Treatment of a panel of haematological cell lines with a cell penetrating peptide containing APIM (ATX-101), lead to a metabolic shift with reduction in glycolytic metabolite and nucleoside phosphate pools as well reduced levels of ENO1 and 6PGD proteins. These results suggests that PCNA stabilize ENO1 and 6PGD, and that targeting PCNA reduce the glycolysis, PPP and nucleoside phosphate pools via destabilization of these proteins.

2023-03-10 | PXD028314 | Pride

ENO1 siRNA knockdown in Human HeLa cells

Project description:HeLa cells were either treated with ENO1 or control siRNAs using the protocol of the RNAiMax reagent (ENO1 pool: SMARTpool ON-TARGETplus L-004034-00-0005 and control pool: ON-TARGETplus non-targeting siRNAs 1-4). Three replicates per condition were produced.

2020-10-27 | E-MTAB-9032 | biostudies-arrayexpress

Targeting the vulnerability of arachidonic acid metabolism to enhance immunotherapy efficacy in ARID1A-deficient colorectal cancer [RNA-Seq]

Project description:ARID1A, a core constituent of SWI/SNF complex, is mutated in about 10% of colorectal cancer (CRC). This study demonstrates a synergistic effect of arachidonic acid metabolism inhibitors with immune checkpoint inhibitors (ICIs) by regulating functionality of CD8+ T cells and vasculogenic mimicry (VM) formation in ARID1A-deficient CRC. Mechanistically, ATAC-seq and ChIP-qPCR demonstrated that the lack of ARID1A results in reduced levels of the key enzymes PTGS1 and PTGS2, which control the arachidonic acid pathway. This reduction generated a reliance on the remaining functionality of arachidonic acid pathway in ARID1A-deficient cells.

2024-11-26 | GSE278083 | GEO

Targeting the vulnerability of arachidonic acid metabolism to enhance immunotherapy efficacy in ARID1A-deficient colorectal cancer [ChIP-Seq]

2024-11-26 | GSE278082 | GEO

Targeting the vulnerability of arachidonic acid metabolism to enhance immunotherapy efficacy in ARID1A-deficient colorectal cancer [ATAC-seq]

2024-11-26 | GSE278081 | GEO

Targeting the intersection of angiopoietin-TIE2 signaling with arachidonic acid metabolism can prevent septic death

Project description:Neonatal sepsis is a major cause of childhood mortality. Limited diagnostic tools and mechanistic insights have hampered our abilities to develop prophylactic or therapeutic interventions. Biomarkers in human neonatal sepsis have been repeatedly identified as associated with dysregulation of angiopoietin signaling and altered arachidonic acid metabolism. We here show that these two pathways appear to be functionally connected via reactive oxygen species (ROS) with a direct role of nitric oxide (NO). Targeting this intersection with oral administration of arachidonic acid and/or the NO donor L-arginine provided prophylactic as well as therapeutic protection from septic death.

2024-05-29 | GSE239431 | GEO

ENO1 suppresses cancer cell ferroptosis by degrading the mRNA of iron regulatory protein 1

Project description:ENO1 (α-Enolase 1) is a key glycolytic enzyme that catalyzes the dehydratation of 2-phosphoglycerate to phosphoenolpyruvate. It also belongs to a member of the RNA degradosome of Escherichia coli and facilitates RNA degradation, but it’s currently unknown whether ENO1 possesses similar function in eukaryotes. To test this possibility,we performed RNA-seq assays expressing NTC or ENO1 shRNA, respectively.

2021-09-10 | GSE153989 | GEO

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