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Antidepressants fluoxetine mediates endoplasmic reticulum stress and autophagy of Non-small cell lung cancer cells through ATF4-AKT-mTOR signaling pathway

ABSTRACT: Antidepressants fluoxetine mediates endoplasmic reticulum stress and autophagy of Non-small cell lung cancer cells through ATF4-AKT-mTOR signaling pathway

PROVIDER: PRJNA823692 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR18644886_1.fastq.gz	Fastqsanger.gz
	SRR18644886_2.fastq.gz	Fastqsanger.gz
	SRR18644887_1.fastq.gz	Fastqsanger.gz
	SRR18644887_2.fastq.gz	Fastqsanger.gz
	SRR18644888_1.fastq.gz	Fastqsanger.gz

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Antidepressants fluoxetine mediates endoplasmic reticulum stress and autophagy of Non-small cell lung cancer cells through ATF4-AKT-mTOR signaling pathway

Project description:In order to investigate the specific mechanism of fluoxetine, we chose H460 cells that were more sensitive to the drug

2022-04-10 | GSE200209 | GEO

Endoplasmic reticulum stress leads to pancreatic beta-cell desensitization to incretin and beta-cell dysfunction via ATF4-mediated PDE4D expression

Project description:Pancreatic beta-cell dysfunction and eventual beta-cell loss are key steps in the course of type 2 diabetes (T2D). Endoplasmic reticulum (ER) stress, in particular the PERK-ATF4 pathway, has been implicated in promoting these beta-cell pathologies. However, the exact molecular events surrounding the PERK-ATF4 pathway in beta-cell dysfunction remain unknown. Here, we discovered that ATF4 transcriptionally promotes expression of PDE4D, which results in beta-cell dysfunction via downregulation of cAMP signaling. Beta-cell-specific transgenic expression of ATF4 resulted in early beta-cell dysfunction and loss, resembling accelerated T2D. ATF4 expression, rather than CHOP, promoted PDE4D expression, decreased cAMP signaling, and attenuated responses to incretins and elevated glucose. Further, beta-cells of leptin receptor-deficient diabetic (db/db) mice expressed increased levels of ATF4 and PDE4D, accompanying impaired beta-cell function. Moreover, inhibiting PDE4D activity with selective pharmacological inhibitors significantly ameliorated beta-cell dysfunction in both db/db mice and beta-cell-specific ATF4 transgenic mice. In summary, our findings support that ER stress causes beta-cell failure via ATF4-mediated PDE4D production, and this is a highly promising therapeutic target for protecting beta-cell function during progression of T2D.

2023-09-25 | GSE199534 | GEO

Ivermectin inhibits the growth of esophageal squamous cell carcinoma by activating ATF4-mediated endoplasmic reticulum stress-autophagy pathway

Project description:Esophageal squamous cell carcinoma (ESCC) is one of the most common form of malignancies in the world. However, there is currently a lack of effective chemotherapeutic drugs for ESCC, and it is urgent to develop new and safe drugs for this disease. Ivermectin is a broad-spectrum antiparasitic drug with demonstrable antitumor activity. However, the precise cellular and molecular mechanisms of ivermectin in cancers growth inhibition remain unclear. In this study, we report a role of ivermectin in ESCC suppression by activating the endoplasmic reticulum (ER) stress and autophagy. In transcriptome analysis, we found that ATF4 and DDIT3 are involved in ER stress activation by ivermectin. Moreover, ivermectin treatment suppressed the growth of ESCC xenograft tumors in nude mice. Taken together, our results identify the antitumor molecular basis of ivermectin targeting the ER stress-autophagy pathway and suggest that ivermectin is a potential drug for the treatment of ESCC.

2024-12-18 | GSE201404 | GEO

Ribosome footprinting in the cytosol and endoplasmic reticulum

Project description:In eukaryotic cells, the spatial regulation of protein expression is frequently conferred through the coupling of mRNA localization and the local control of translation. mRNA localization to the endoplasmic reticulum (ER) is a prominent example of such regulation and serves a ubiquitous role in segregating the synthesis of secretory and integral membrane proteins to the ER. Recent genomic and biochemical studies have now expanded this view to suggest a role for the ER in global protein synthesis. We have utilized cell fractionation and ribosome profiling to obtain a genomic survey of the subcellular organization of mRNA translation and report that ribosomal loading of mRNAs, a proxy for mRNA translation, is biased to the ER. Notably, ER-associated mRNAs encoding both cytosolic and topogenic signal-encoding proteins display similar ribosome loading densities, suggesting that ER-associated ribosomes serve a global role in mRNA translation. We propose that the partitioning of mRNAs and their translation between the cytosol and ER compartments may represent a novel mechanism for the post-transcriptional regulation of gene expression. HEK293 cells were fractionated between the cytosol and endoplasmic reticulum. Within each fraction, ribosome footprints were generated and sequenced. In parallel, total mRNA was sequenced.

2011-12-20 | E-GEOD-31539 | biostudies-arrayexpress

Tunicamycin-induced Endoplasmic Reticulum-Quality Control Pathway and Endoplasmic Reticulum-Associated Degradation Mechanism in the diatom Phaeodactylum tricornutum

Project description:Tunicamycin-induced Endoplasmic Reticulum-Quality Control Pathway and Endoplasmic Reticulum-Associated Degradation Mechanism in the diatom Phaeodactylum tricornutum

| PRJNA862509 | ENA

EMD37 triggers endoplasmic reticulum stress in cancer cells

Project description:EMD37 triggers endoplasmic reticulum stress in cancer cells

| PRJNA828545 | ENA

Ivermectin inhibits the growth of esophageal squamous cell carcinoma by activating ATF4-mediated endoplasmic reticulum stress-autophagy pathway

Project description:Ivermectin inhibits the growth of esophageal squamous cell carcinoma by activating ATF4-mediated endoplasmic reticulum stress-autophagy pathway

| PRJNA831453 | ENA

The eIF2 kinase PERK and the integrated stress response facilitate activation of ATF6 during endoplasmic reticulum stress

Project description:Disruptions of the endoplasmic reticulum (ER) that perturb protein folding cause ER stress and elicit an unfolded protein response (UPR) that involves translational and transcriptional changes in gene expression aimed at expanding the ER processing capacity and alleviating cellular injury. Three ER stress sensors PERK, ATF6, and IRE1 implement the UPR. PERK phosphorylation of eIF2 during ER stress represses protein synthesis, which prevents further influx of ER client proteins, along with preferential translation of ATF4, a transcription activator of the integrated stress response. In this study we show that the PERK/eIF2α~P/ATF4 pathway is required not only for translational control, but also activation of ATF6 and its target genes. The PERK pathway facilitates both the synthesis of ATF6 and trafficking of ATF6 from the ER to the Golgi for intramembrane proteolysis and activation of ATF6. As a consequence, liver-specific depletion of PERK significantly reduces both the translational and transcriptional phases of the UPR, leading to reduced protein chaperone expression, disruptions of lipid metabolism, and enhanced apoptosis. These findings show that the regulatory networks of the UPR are fully integrated, and helps explain the diverse pathologies associated with loss of PERK. 14 gene expression arrays, 3 WT control arrays; 3 lsPERK control arrays; 4 WT Treated arrays; 4 lsPERK treated arrays. Comparison of gene expression profiles for treated vs control in wildtype and knock-out.

2012-01-20 | E-GEOD-29929 | biostudies-arrayexpress

Expression data from children and adolescents treated with Fluoxetine

Project description:It is well-known that between 40 and 50% of patients taking antidepressants do not respond to treatment or relapse. Genome wide gene expression studies can help us to understand better the response to antidepressants, revealing the effects of both genetic background and environmental/epigenetic factors. We used microarrays to detail the response to Fluoxetine in children and adolescents, analysing the expression just before intake of drug and 8 weeks after starting the treatment.

2019-12-31 | GSE128387 | GEO

Antidepressants Fluoxetine Mediates Endoplasmic Reticulum Stress and Autophagy of Non-Small Cell Lung Cancer Cells Through the ATF4-AKT-mTOR Signaling Pathway.

Project description:Fluoxetine, one of the latest clinical antidepressants, is reported to have the anti-proliferative effect on cancer cells via immune-related pathways. However, the mechanism is still not known. This study mainly focused on the discovery of the molecular basis of the inhibitory effect of fluoxetine in lung cancer. The specific anti-proliferation effect and autophagy induced by fluoxetine on lung cancer cell were shown in CCK8 and immunofluorescence. The RNA sequence hinted that the endoplasmic reticulum (ER) stress-related protein and mTOR pathway were enriched after fluoxetine treatment. Western blot results revealed that the ER stress pathway was activated by fluoxetine, including PERK, ATF4, and CHOP, while the AKT/mTOR pathway was inhibited. In addition, the transfection of ATF4 siRNA further discovered that ER stress participated in the inhibition of AKT/mTOR pathway and the induction of anti-proliferation and autophagy in the fluoxetine-treated cells. More importantly, fluoxetine was demonstrated to play cytotoxic activity in cancer cells without affecting normal cells. Our results showed that fluoxetine triggered the ATF4-AKT-mTOR signaling pathway to induce cell cycle arrest and autophagy restraining cancer cells' growth in lung cancer. This study found fluoxetine unaffected the proliferation of normal lung epithelial cells, providing safe clinical therapeutic strategies for lung cancer patients with depression.

| S-EPMC9127500 | biostudies-literature

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