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A novel bystander effect in tamoxifen treatment: PPIB derived from ER+ cells attenuates ER- cells via endoplasmic reticulum stress-induced apoptosis

ABSTRACT: A novel bystander effect in tamoxifen treatment: PPIB derived from ER+ cells attenuates ER- cells via endoplasmic reticulum stress-induced apoptosis

PROVIDER: PRJNA1040911 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR26844901_1.fastq.gz	Fastqsanger.gz
	SRR26844901_2.fastq.gz	Fastqsanger.gz
	SRR26844902_1.fastq.gz	Fastqsanger.gz
	SRR26844902_2.fastq.gz	Fastqsanger.gz
	SRR26844903_1.fastq.gz	Fastqsanger.gz

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Similar Datasets

A novel bystander effect in tamoxifen treatment: PPIB derived from ER+ cells attenuates ER- cells via endoplasmic reticulum stress-induced apoptosis

Project description:Tamoxifen (TAM) is the frontline therapy for estrogen receptor-positive (ER+) breast cancer in premenopausal women that interrupts ER signaling. As tumors with elevated heterogeneity, amounts of ER-negative (ER-) cells are present in ER+ breast cancer that cannot be directly killed by TAM. Despite complete remissions have been achieved in clinical practice, the mechanism underlying the elimination of ER- cells during TAM treatment remains an open issue. Herein, we deciphered the elimination of ER- cells in TAM treatment from the perspective of the bystander effect. Markable reductions were observed in tumorigenesis of ER- breast cancer cells by applying both supernatants from TAM-treated ER+ cells and a transwell co-culture system, validating the presence of a TAM-induced bystander effect. The major antitumor protein derived from ER- cells, peptidyl-prolyl cis-trans isomerase B (PPIB), is the mediator of the TAM-induced bystander effect identified by quantitative proteomics. The attenuation of ER- cells was attributed to activated BiP/eIF2α/CHOP axis and promoted endoplasmic reticulum stress (ERS)-induced apoptosis, which can also be triggered by PPIB independently. Altogether, our study revealed a novel TAM-induced bystander effect in TAM treatment of ER+ breast cancer, raising the possibility to develop PPIB as a synergistic antitumor agent or even substitute endocrine therapy.

2024-02-12 | GSE247920 | GEO

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

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

Unfolded protein response (UPR) and endoplasmic reticulum (ER) stress in acromegaly

Project description:Acromegaly is a growth hormone (GH) excess pathological condition in humans and is associated with somatic disfigurement and a wide variety of systemic manifestations such as arthritis, neuropathies, carpal tunnel syndrome, reproductive disorders, metabolic disorders, and gastrointestinal complications. Studying the effect of growth hormone (GH) excess at the cellular level could help in understanding the underlying causes of acromegaly complications. In our previous publications, we have shown that excess GH increases DNA damage and impairs DNA repair pathways in somatic cells. In addition, we revealed that excessive GH reduces the number of stem cells and causes premature aging. Exaggerated growth is one of the main features of acromegaly and therefore, in this research, we have focused on protein production and biogenesis in acromegaly and whether excess GH is associated with unfolded protein response (UPR) and endoplasmic reticulum (ER) stress. Acromegaly-associated abnormal growth can be caused by hypertrophy or hyperplasia. Using pathway enrichment analysis of RNA seq data from our Zebrafish Acromegaly Model and Flow Cytometry Analysis, here we show a progressive increase in hepatocyte cell size and enrichment of hypertrophy pathways in the muscle and liver. That was associated with a progressive enrichment of protein production pathways and ribosome biogenesis. Moreover, using GSEA (Gene Set Enrichment Analysis) of acromegaly RNA seq data, here we show that endoplasmic reticulum (ER) stress is an accompanying feature of acromegaly disease. Our model exhibited endoplasmic reticulum (ER) stress in various organs, especially in the brain.

2021-03-04 | GSE153755 | GEO

Unfolded protein response (UPR) and endoplasmic reticulum (ER) stress in acromegaly

Project description:Unfolded protein response (UPR) and endoplasmic reticulum (ER) stress in acromegaly

| PRJNA643979 | ENA

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) Chaperones Are Effector Genes Mediating Long-Term Memory Consolidation

Project description:Endoplasmic Reticulum (ER) Chaperones Are Effector Genes Mediating Long-Term Memory Consolidation

| PRJNA704968 | ENA

GENE EXPRESSION ANALYSIS IN TOMATO (Lycopersicon esculentum) UNDER ENDOPLASMIC RETICULUM (ER) STRESS

Project description:GENE EXPRESSION ANALYSIS IN TOMATO (Lycopersicon esculentum) UNDER ENDOPLASMIC RETICULUM (ER) STRESS

| PRJNA911166 | ENA

Endoplasmic Reticulum (ER) Chaperones Are Effector Genes Mediating Long-Term Memory Consolidation

Project description:Purpose: We investigated Nr4a effector genes following a hippocampus dependent learning task using a dominant mouse model of Nr4a. Method: We performed total RNA sequencing after training for hippocampus-dependent memory from Nr4ADN and control littermates Results: Using an unbiased analysis of gene expression after training for hippocampus-dependent memory, we found that Nr4a transcription factors regulate expression of specific effector genes encoding endoplasmic reticulum (ER) chaperones that drive protein folding, enabling membrane proteins to more efficiently traffic to the cell surface. Conclusion: This study identified the effector genes of Nr4a transcription factors involved in learning and memory.

2021-03-01 | GSE167566 | GEO

Tmem45b Modulates itch via Endoplasmic Reticulum Calcium Regulation

Project description:Chronic itch is detected by dorsal root ganglia (DRG) that severely impairs quality of life. However, its underlying mechanisms remain poorly understood. We identified that Tmem45b was contained in natriuretic peptide type B (Nppb)-, mas-related G-protein coupled receptor member A3 (Mrgpra3)-, and Mrgprd-positive DRG neurons, which are associated with itch sensation. The role of Tmem45b in itch sensation has not been explored. Tmem45b conditional knockout (cKO) mice exhibited decreased scratching to β-alanine, and increased scratching to chloroquine. Notably, Tmem45b cKO alleviated chronic itch. Furthermore, Tmem45b cKO impaired the calcium response to β-alanine and allyl isothiocyanate but not to chloroquine in dissociated DRG neurons. Tmem45b deficiency led to significant downregulation of sarco/endoplasmic reticulum calcium transport ATPase 1 (Serca1), impairing calcium storage capacity of endoplasmic reticulum (ER). Inhibition of Serca1 in DRG neurons reduced intracellular calcium release triggered by β-alanine and chloroquine. Together,Tmem45b deficiency may reduce nonhistaminergic itch and disrupt ER calcium regulation, highlighting a potential target for chronic itch therapy.

2026-01-01 | GSE304359 | GEO

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