Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Fisetin induces autophagy in pancreatic cancer cells via endoplasmic reticulum stress- and mitochondrial stress-dependent pathways

ABSTRACT: Fisetin induces autophagy in pancreatic cancer cells via endoplasmic reticulum stress- and mitochondrial stress-dependent pathways

PROVIDER: PRJNA481372 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR7527700_1.fastq.gz	Fastqsanger.gz
	SRR7527700_2.fastq.gz	Fastqsanger.gz
	SRR7527701_1.fastq.gz	Fastqsanger.gz
	SRR7527701_2.fastq.gz	Fastqsanger.gz
	SRR7527702_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 12

Similar Datasets

Fisetin induces autophagy in pancreatic cancer cells via endoplasmic reticulum stress- and mitochondrial stress-dependent pathways

Project description:Pancreatic cancer is one of the most aggressive tumors and has poor survival rates. Fisetin, a natural flavonoid, was recently reported to have antitumor effects in various cancer models. Autophagy is a conserved catabolic process that maintains cellular homoeostasis in response to stress, and together with apoptosis, determines cell fate. Herein, we examined the effect of fisetin on pancreatic cancer. We reveal that fisetin inhibits Panc-1 cell proliferation in vivo and in vitro. We found that AMPK-dependent autophagy was enhanced after fisetin treatment.However RNA-seq analysis revealed that the unfolded protein response, which is activated by ER stress, was enriched. We also found that there may be crosstalk between the AMPK- and p8-dependent pathways.

2019-02-25 | GSE117189 | GEO

Lipid bilayer stress-activated IRE-1 modulates autophagy during endoplasmic reticulum stress

Project description:Metabolic disorders such as obesity and nonalcoholic fatty liver disease (NAFLD) are emerging disorders that affect the global population. One facet of the disorders is attributed to the disturbance of membrane lipid homeostasis. Perturbation of endoplasmic reticulum (ER) homeostasis through changes in membrane phospholipid composition results in activation of the unfolded protein response (UPR) and causes dramatic translational and transcriptional changes in cell. To restore cellular homeostasis, the three highly conserved UPR transducers ATF6, IRE1, and PERK mediate cellular processes upon ER stress. The roles of the UPR in proteostatic stress caused by the accumulation of misfolded protein is well understood but lipid perturbation-induced UPR remains elusive. We found that genetically attenuated PC synthesis in C. elegans causes lipid droplets accumulation if not for the intervention of the UPR program. Transcriptional profiling of lipid perturbation-induced ER stress animals shows a unique subset of genes modulated in an UPR-dependent manner that are unaffected by proteostatic stress. Among these, we identified IRE1-modulated autophagy genes that trigger liberation of free fatty acids from excess lipid droplets suggesting a stress release mechanism by which free fatty acids are rechannelling to restore lipid homeostasis. Considering the important role of lipid homeostasis and how its impairment contributes to the pathologies in metabolic diseases, our data uncovers the indispensable role of a fully functional UPR program in regulating lipid homeostais in the face of chronic ER stress.

2018-10-31 | GSE99763 | GEO

EMD37 triggers endoplasmic reticulum stress in cancer cells

Project description:EMD37 triggers endoplasmic reticulum stress in cancer cells

| PRJNA828545 | ENA

Transcriptional changes associated with endoplasmic reticulum stress in the eye imaginal disc of Drosophila melanogaster

Project description:We obtained transcriptional profiles of third instar eye imaginal disc nuclei with or without endoplasmic reticulum stress using next generation sequencing (NGS). We employed an isolation of nuclei tagged in specific cell type (INTACT) protocol (Ma and Weake, J. of Vis. Exp., 2014) to label nuclear membranes of GMR-GAL4-expressing cells with EGFP. The experimental group also expressed a mutant allele of the membrane visual protein rhodopsin (Rh-1(G69D)), which is known to cause endoplasmic reticulum stress and initiate Unfolded Protein Response (UPR) signaling. The goal of this study was to characterize the transcriptional changes associated with endoplasmic reticulum stress responses in a commonly used platform, the eye imaginal disc.

2021-09-20 | GSE150058 | GEO

EMD37 triggers endoplasmic reticulum stress in cancer cells

Project description:Targeting endoplasmic reticulum (ER) stress presents a promising strategy in cancer therapy. We have previously reported that a series of 1,2,4-oxadiazole derivatives induces the degradation of epidermal growth factor receptor and c-Met which are implicated in tumorigenesis. Based on our previous SAR studies, herein, we synthesized EMD37, a novel 1,2,4-oxadiazole derivative, and systematically investigated its anticancer activity.

2023-04-19 | GSE201134 | GEO

Perturbation of placental endocrine function by endoplasmic reticulum stress leads to maladaptation of maternal hepatic glucose metabolism

Project description:To investigate whether ER stress underpins the secretion of mis-glycosylated glycoproteins by trophoblast, we treated trophoblast-like BeWo cells with the ER stress inducer thapsigargin (Tg), an inhibitor specific for sarco/endoplasmic reticulum Ca2+-ATPase.

2022-12-04 | E-MTAB-10943 | biostudies-arrayexpress

Endoplasmic reticulum (ER) stress and the unfolded protein response (UPR)

Project description:We are currently studying how these information-carrying oligosaccharides are involved in cellular stress responses, particularly in human genetic diseases called Congenital Disorders Of Glycosylation in which oligosaccharide assembly is defective. We are interested in endoplasmic stress responses/unfolded protein responses. ER glycans and ER lectins are intimately involved in the folding of ER proteins. Therefore, ER lectins and ER glycosyltransferases may be controlled by these stress responses, to produce and/or recognize key glycans in the stress response. Our model system is the human dermal fibroblast. We have successfully calibrated the ER stress responses in these cells by determining the magnitudes of various stress effects (such as chaperone transcription) with different forms of ER stress. We are also completing a study in which activation the signaling molecules Ire1 and ATF6 are also calibrated. We prepared multiple identical aliquots of RNA from cells stressed under several of these calibrated conditions. Endoplasmic reticulum (ER) stress and the unfolded protein response (UPR): Study of the role of ER stress in the expression of genes for ER transferases and lectins that participate in ER folding and quality control using human skin fibroblasts. The UPR response in these cells has been calibrated using various readouts in response to different stresses: 1) 40 nM L-azetidine-2-carboxylate (AZC) 1 hour, 2) 0.2 mg/ml castanospermine, 24 hours, 3) 2 mM Dithiothreitol (DTT), 20 minutes, 4) 100nm Thapsigargin (TG), 30 minutes, 5) 5 ug/ml tunicamycin, 5 hours, 6) untreated control cells

2011-02-17 | E-GEOD-27349 | biostudies-arrayexpress

Endoplasmic reticulum stress engenders immune-resistant, latent pancreatic cancer metastases

Project description:Endoplasmic reticulum stress engenders immune-resistant, latent pancreatic cancer metastases

| PRJNA428722 | ENA

Epithelial endoplasmic reticulum stress orchestrates a protective IgA response I

Project description:Epithelial endoplasmic reticulum stress orchestrates a protective IgA response I

| PRJNA512503 | ENA

Epithelial endoplasmic reticulum stress orchestrates a protective IgA response II

Project description:Epithelial endoplasmic reticulum stress orchestrates a protective IgA response II

| PRJNA512502 | ENA