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Atovaquone-induced oxidative stress activates pentose phosphate pathway and immunogenic cell death in ovarian cancer

ABSTRACT: Atovaquone-induced oxidative stress activates pentose phosphate pathway and immunogenic cell death in ovarian cancer

PROVIDER: PRJNA1216615 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR32153761_1.fastq.gz	Fastqsanger.gz
	SRR32153761_2.fastq.gz	Fastqsanger.gz
	SRR32153762_1.fastq.gz	Fastqsanger.gz
	SRR32153762_2.fastq.gz	Fastqsanger.gz
	SRR32153763_1.fastq.gz	Fastqsanger.gz

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Atovaquone-induced oxidative stress activates pentose phosphate pathway and immunogenic cell death in ovarian cancer

Project description:Atovaquone, an FDA-approved oxidative phosphorylation (OXPHOS) inhibitor, has shown promise in treating epithelial ovarian cancer (EOC), the deadliest gynecologic malignancy. However, the precise mechanisms underlying its antitumorigenic effects remain unclear. We employed a longitudinal transcriptomic approach to characterize the molecular effects of atovaquone on EOC cells. Our findings demonstrate that atovaquone disrupts cellular homeostasis and metabolism, activates stress responses, and primes immune recognition. We observed temporal downregulation of genes and pathways involved in key cellular processes, such as cell cycle and DNA replication, correlating with reduced proliferative capacity. Atovaquone also downregulated both OXPHOS and glycolysis, while upregulating the pentose phosphate pathway, suggesting a metabolic shift toward redox homeostasis restoration in response to severe oxidative stress. Consistent with oxidative stress, we found that atovaquone activated endoplasmic reticulum (ER) stress, which is linked to immunogenic cell death. During ER stress, calreticulin, a Damage-Associated Molecular Pattern (DAMP), translocates to the plasma membrane, where it promotes immune recognition. We observed that calreticulin was upregulated on the plasma membrane of atovaquone-treated EOC cells. Additionally, we detected increased levels of other DAMPs, such as High Mobility Group Box 1 (HMGB1) and Mitochondrial Transcription Factor A (TFAM), in the supernatant of atovaquone-treated cells, indicating the release of immunogenic molecules. Moreover, increased expression of ligands for activating receptors of NK cells was observed and co-culture experiments showed enhanced NK cell activity toward atovaquone-treated cells. These results highlight atovaquone’s potential as an adjuvant therapy that activates immune responses, offering a new avenue for combination therapies in EOC treatment.

2025-02-02 | GSE288243 | GEO

Atovaquone-induced oxidative stress activates the pentose phosphate pathway and Immunogenic cell death in ovarian cancer.

Project description: Not available

| S-EPMC12644797 | biostudies-literature

Progesterone increases metabolism via the pentose phosphate pathway in bovine uterine epithelial cells

Project description:During early pregnancy, glucose is essential for the uterine epithelium and the developing embryo. In cows, studies have shown that progesterone increases the secretion of glucose into the uterine lumen. Nevertheless, how progesterone affects glucose metabolism in the uterine epithelium has been sparsely investigated. Therefore, our objective was to investigate how progesterone influences glucose metabolism in immortalized bovine uterine epithelial (BUTE) cells. Progesterone treatment (10 μM) increased glucose consumption. To gain a more global picture of the effects of progesterone, RNAseq was performed after BUTE cells were treated with vehicle (DMSO) or 10 μM for 24 hours. KEGG analysis indicated that progesterone altered genes associated with metabolic pathways and glutathione metabolism. Manually examining genes unique to specific glucose metabolic pathways identified an increase in the rate-limiting enzyme in the pentose phosphate pathway—glucose-6-phosphate dehydrogenase. Functionally, a major product of the pentose phosphate pathway is NADPH, and progesterone treatment increased NADPH concentrations in BUTE cells. In cows, immunohistochemistry confirmed that glucose-6-phosphate dehydrogenase levels were higher in the uterine epithelium in the luteal phase when progesterone concentrations are high. In conclusion, progesterone increased glucose-6-phosphate dehydrogenase expression and metabolism via the pentose phosphate pathway in the bovine uterine epithelium. This metabolism could provide substrates for cell proliferation, molecules to be secreted into the uterine lumen that supports embryonic development, or maintain reduction/oxidation balance in the uterine epithelium.

2024-10-09 | GSE269076 | GEO

Conserved Spermatogonial Gene Networks Couple to Glutathione and Pentose Phosphate Metabolism but not Cysteine Biosynthesis

Project description:Here, gene profiles in rat spermatogonial stem cell lines are compared to publicly available mouse, monkey and human spermatogonial gene profiles. Interestingly, rat spermatogonia expressed metabolic control factors Foxa1, Foxa2 and Foxa3. Germline Foxa2 was enriched in Gfra1Hi and Gfra1Low undifferentiated A-single spermatogonia. Foxa2-bound loci in spermatogonial chromatin were over-represented by conserved stemness genes (Dusp6, Gfra1, Etv5, Rest, Nanos2, Foxp1) that intersect bioinformatically with conserved glutathione/pentose phosphate metabolism genes (Tkt, Gss, Gclc, Gclm, Gpx1, Gpx4, Fth), marking elevated spermatogonial GSH:GSSG. Cystine-uptake and intracellular conversion to cysteine typically couple glutathione biosynthesis to pentose phosphate metabolism. Rat spermatogonia, curiously, displayed poor germline stem cell viability in cystine-containing media, and, like primate spermatogonia, exhibited reduced transsulfuration pathway markers. Exogenous cysteine, cysteine-like mercaptans, somatic testis cells and ferroptosis inhibitors counteracted the cysteine starvation-induced spermatogonial death and stimulated spermatogonial growth factor activity in vitro.

2020-12-17 | GSE163302 | GEO

IRG1/itaconate axis modulates lung tumor microenvironment via pentose phosphate pathway

Project description:IRG1/itaconate axis modulates lung tumor microenvironment via pentose phosphate pathway

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A defective pentose phosphate pathway reduces inflammatory macrophage responses during hypercholesterolemia

Project description:A defective pentose phosphate pathway reduces inflammatory macrophage responses during hypercholesterolemia

| PRJNA420032 | ENA

Evolutionary engineering of the pentose phosphate pathway in Saccharomyces cerevisiae.

Project description:Engineering the pentose phosphate pathway in Saccharomyces cerevisiae using an evolutionary engineering based strategy.

| PRJEB6586 | ENA

IRG1/itaconate axis modulates lung tumor microenvironment via pentose phosphate pathway [sav25]

Project description:IRG1/itaconate axis modulates lung tumor microenvironment via pentose phosphate pathway [sav25]

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IRG1/itaconate axis modulates lung tumor microenvironment via pentose phosphate pathway [sav24]

Project description:IRG1/itaconate axis modulates lung tumor microenvironment via pentose phosphate pathway [sav24]

| PRJNA1077937 | ENA

The Pentose Phosphate Pathway in pathogenic Francisella

Project description:Metabolic pathways are now considered as intrinsic virulence attributes of pathogenic bacteria and hence represent potential targets for anti-bacterial strategies. Here, we addressed the role of the pentose phosphate pathway (PPP) and its connections with other metabolic pathways in the pathophysiology of Francisella novicida. We have previously shown that this intracellular bacterial pathogen used gluconeogenesis to metabolize host-derived nutrients in the cytosolic compartment of infected macrophages. Francisella species, which lacks the oxidative branch of the PPP, are equipped with all the genes of the non-oxidative branch (i.e. tktA, tal, rpiA and rpe, encoding transketolase, transaldolase, ribose-phosphate isomerase and ribulose phosphate epimerase, respectively). The involvement of the PPP in the early stage of intracellular life cycle of F. novicida was first demonstrated with the study of PPP inactivation mutants. Indeed, inactivation of tktA, rpiA or rpe genes, severely impaired intramacrophagic multiplication during the first 24–hours. However, time-lapse video microscopy demonstrated that rpiA and rpe mutants were able to resume late intracellular bacterial multiplication. To get further insight into the links between the PPP and other metabolic networks of the bacterium, we next performed a thorough proteo-metabolomic analysis of these mutants. We show that the PPP constitutes a major bacterial metabolic hub with multiple connections with glycolysis, tricarboxylic acid cycle and other metabolic pathways, such as fatty acid degradation and sulfur metabolism. Hence, our study highlights how, by its multiple connections with other metabolic pathways, PPP is instrumental to Francisella pathogenesis and growth in its intracellular niche.

2021-07-27 | PXD023550 | Pride

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