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Citric acid, an ovarian cancer metabolite, induces pyroptosis via caspase-4/TXNIP-NLRP3-GSDMD pathway in ovarian cancer

ABSTRACT: Citric acid, an ovarian cancer metabolite, induces pyroptosis via caspase-4/TXNIP-NLRP3-GSDMD pathway in ovarian cancer

PROVIDER: PRJNA784786 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR17073211_1.fastq.gz	Fastqsanger.gz
	SRR17073211_2.fastq.gz	Fastqsanger.gz
	SRR17073212_1.fastq.gz	Fastqsanger.gz
	SRR17073212_2.fastq.gz	Fastqsanger.gz
	SRR17073213_1.fastq.gz	Fastqsanger.gz

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Similar Datasets

Citric acid, an ovarian cancer metabolite, induces pyroptosis via caspase-4/TXNIP-NLRP3-GSDMD pathway in ovarian cancer

Project description:Malignant tumors display profound changes in cellular metabolism, yet how these altered metabolites affect the development and growth of tumors is not fully understood. Here, we used metabolomics to analyze the metabolic profile differences in ovarian cancer, and found that citric acid (CA) is the most significantly downregulated metabolite. Recently, CA has been reported to inhibit the growth of a variety of tumor cells, but whether it is involved in pyroptosis of ovarian cancer and its potential molecular mechanisms still remains to be further investigated. Here, we demonstrated that CA inhibits the growth of ovarian cancer cells in a dose-dependent manner. RNA-seq analysis revealed that CA significantly promoted the expression of thioredoxin interacting protein (TXNIP) and caspase-4 (CASP4). Morphologic examination by transmission electron microscopy indicated that CA-treated ovarian cancer cells exhibited typical pyroptosis characteristics. Further mechanistic analyses showed that CA facilitates pyroptosis via CASP4/TXNIP-NLRP3-Gesdermin-d (GSDMD) pathway in ovarian cancer. This study elucidated that CA induces ovarian cancer cell death through classical and non-classical pyroptosis pathways, which may be beneficial as an ovarian cancer therapy.

2022-08-01 | GSE189851 | GEO

Corilagin Induces Pyroptosis in AML Cells by Activating the TXNIP-Caspase-3-GSDME Pathway

Project description:Acute myeloid leukemia (AML) is a challenging hematological malignancy characterized by high relapse rates and limited treatment options. Compound corilagin, an ellagitannin derived from ethnopharmacological plants, shows promise as an anti-cancer agent, although its anti-leukemic effects remain poorly understood. This study aims to investigate whether corilagin induces cell death in AML cells and explore the underlying mechanisms. In AML cells, corilagin induces pyroptosis, as characterized by the formation of pyroptotic bubbles, increased lactate dehydrogenase (LDH) release and a higher proportion of propidium iodide (PI)-positive cells. Corilagin activates caspase-3, which in turn cleaves gasdermin E (GSDME) to generate GSDME-NT, promoting pyroptosis. Additionally, corilagin activates thioredoxin-interacting protein (TXNIP), and the knockdown of TXNIP rescues cells from corilagin-induced pyroptosis. Corilagin reduces cell viability and induces pyroptosis in primary AML cells, and in an AML cell-derived xenograft (CDX) mouse model, it inhibits leukemia progression and prolongs survival. These findings imply that corilagin induces pyroptosis in AML through the TXNIP/caspase-3/GSDME pathway, presenting a prospective novel therapeutic strategy for AML treatment.

2026-02-11 | GSE315428 | GEO

A palmitoylation-depalmitoylation relay spatiotemporally controls GSDMD activation in pyroptosis [I]

Project description:Gasdermin D (GSDMD) is the executioner of pyroptosis, which is important for host defense against pathogen infection. After activation, caspase-mediated cleavage of GSDMD liberates an N-terminal fragment (GSDMD-NT), which oligomerizes and forms pores in the plasma membrane, leading to cell death and subsequent release of proinflammatory cytokines. How this process is spatiotemporally controlled to promote pyroptosis in cells has been a fundamental, unaddressed question. Here, we identify GSDMD as a substrate for reversible S-palmitoylation on cysteine 192 (Cys192) in response to lipopolysaccharide (LPS) stimulation. We found that the palmitoyl acyltransferase DHHC7palmitoylates GSDMD to direct its cleavage by caspases in pyroptosis by promoting the interaction of GSDMD and caspases. We further show that after GSDMD cleavage, palmitoylation of GSDMD-NTpromotes its plasma membrane translocation and binding, and then acyl protein thioesterase 2 (APT2) depalmitoylates GSDMD-NT to unmask the Cys192 residue to promote oxidation-mediated oligomerization and pyroptosis. Perturbation of either palmitoylation or depalmitoylation suppresses pyroptosis, extends the survival of mice from LPS-induced lethal septic shock and sensitizes mice to bacterial infection. Thus. our findings reveal a model through which a palmitoylation-depalmitoylationrelay spatially and temporally controls GSDMD activation in pyroptosis.

2024-02-25 | GSE252893 | GEO

A palmitoylation-depalmitoylation relay spatiotemporally controls GSDMD activation in pyroptosis [II]

2024-02-25 | GSE252911 | GEO

The Card19 locus regulates apoptosis and pyroptosis downstream of caspase activation and gasdermin D cleavage independently from IL-1 cytokine release

Project description:Cell death plays a critical role in inflammatory responses. During pyroptosis, inflammatory caspases cleave Gasdermin D (GSDMD) to release an N-terminal fragment that generates plasma membrane pores that mediate cell lysis and IL-1 release. However, certain stimuli and cell types release IL-1 cytokines through GSDMD pores in cells that remain viable, a process termed hyperactivation. How these distinct cell fate choices are regulated downstream of GSDMD pore formation is unknown. Here, we demonstrate that the Card19 locus promotes lysis downstream of caspase activation. Despite being largely protected from cell death, CARD19-deficient macrophages had no defect in caspase activation, IL-1 secretion, or GSDMD cleavage. CARD19, a mitochondrial protein, was not responsible for the observed phenotypes, nor was the recently identified pore forming protein NINJ1 which regulates terminal pore formation during multiple forms of cell death. Furthermore, previously identified cell death phenotypes attributed to Sterile alpha and heat Armadillo motif-containing protein (SARM) were revealed to be caused by a passenger mutation. Importantly, Card19-/ mice had increased susceptibility to Yersinia infection, including increased mortality, higher bacterial burdens and pronounced splenomegaly. These findings implicate the Card19 locus as a factor that couples caspase processing and GSDMD cleavage to cell death, providing insight into how the checkpoint between hyperactivation and cell death is regulated.

2021-03-21 | GSE168489 | GEO

Corilagin Induces Pyroptosis in AML Cells by Activating the TXNIP-Caspase-3-GSDME Pathway

Project description:Corilagin Induces Pyroptosis in AML Cells by Activating the TXNIP-Caspase-3-GSDME Pathway

| PRJNA1397143 | ENA

Caspases 3 and 7 restrict intestinal inflammation by regulating stem cell function and gsdmd-mediated pyroptosis

Project description:Aberrant intestinal epithelial cell (IEC) death is a hallmark of inflammatory bowel disease (IBD), observed in patient samples and animal models of colitis. While multiple cell death pathways contribute to disease pathogenesis, the dominant modalities and their regulatory mechanisms in IBD remain poorly defined. In this study, we demonstrate that mice with intestinal epithelial cell-specific deletion of caspase-3 and -7 (Casp3/7 Tg) exhibit exacerbated colitis, increased mortality, and impaired epithelial regeneration, phenotypes not observed in other cell death-related knockout models. These findings highlight a previously unrecognized protective role of caspase-3/7 in controlling inflammation and tissue regeneration following intestinal injury. Mechanistically, caspase-3/7 deficiency negatively affects intestinal stem cell proliferation and promotes GSDMD-dependent pyroptosis, compromising barrier integrity and return to steady state conditions. Together, our results identify caspase-3/7 as key regulators of epithelial integrity and inflammation and suggest their modulation as a promising therapeutic strategy in IBD and colorectal cancer.

2026-02-13 | GSE297859 | GEO

Ceramide induces pyroptosis through TXNIP/NLRP3/GSDMD pathway in HUVECs.

Project description: Not available

| S-EPMC9749313 | biostudies-literature

Cardiotoxin from Naja atra Activates the NLRP3/Caspase-1/GSDMD Pyroptosis Pathway to Induce Skin Tissue Injury

Project description:Cardiotoxin from Naja atra Activates the NLRP3/Caspase-1/GSDMD Pyroptosis Pathway to Induce Skin Tissue Injury

| PRJNA1473889 | ENA

ATPase activity of RIOK2 transports FADD–RIPK1–Caspase-8 complex from lysosome to ER and triggers spatial cleavage of GSDMD

Project description:We identified RIOK2 as a FADD-interacting protein that is essential for caspase-8-dependent cleavage of GSDMD. RIOK2’s ATPase activity drives the transport of lysosome to ER through activating myosin II and thereby translocate FADD-RIPK1-caspase-8 complex from lysosome to ER. Importantly, RIOK2’s ATPase activity also promotes the association of RIOK2 with FADD–RIPK1–caspase-8 complex and directly activates cleavage of caspase-8 and GSDMD both at ER and in vitro.

2024-05-07 | PXD052041 |

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