Homo sapiens
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA234099 | ENA |
REPOSITORIES: ENA
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Project description:PUR alpha protein induces endoplasmic reticulum stress response and cell differentiation pathways in prostate cancer
| PRJNA111461 | ENA
Project description:Effects of calcitriol on expressions of ER stress related genes were evaluated with microarray. Calcitriol, the active form of vitamin D, is known to induce apoptosis in cancer cells and increase intracellular calcium. Increase in cytopalsmic calcicium levels may indicate a decrease in endoplasmic reticulum (ER) calcium levels since ER is the main storage unit for calcium. Decrease in ER calcium levels are known to induce ER stress which can lead to apoptosis. However the effects of calcitriol on ER stress have not been reported before. Here we hypotesized that the cellular effects of calcitriol can be explained by induction of ER stress. We have tested this hypothesis by assessing calcitriol induced transcriptomic alterations with a focus on ER stress related genes.
2015-01-01 | GSE53975 | GEO
Project description:Endoplasmic reticulum (ER) stress and the unfolded protein response (UPR)
| PRJNA137213 | ENA
Project description:Increased endoplasmic reticulum stress response is involved in clopidogrel-induced apoptosis of gastric epithelial cells
| PRJNA206434 | ENA
Project description:Folate and vitamin B12 imbalance induces endoplasmic reticulum stress and cholesterol biosynthesis gene expression in human adipocytes
| PRJNA184810 | ENA
Project description:Endoplasmic reticulum (ER) stress triggers an adaptive response which fosters tumor cell survival and resilience to stress conditions. Activation of the endoplasmic reticulum stress response, through its PERK branch, promotes the phosphorylation of the α-subunit of translation initiation factor eIF2alpha, thereby repressing general protein translation and selectively augmenting the translation of ATF4 with the downstream CHOP transcription factor and the protein disulfide oxidase ERO1. Here, we show that ISRIB, a small molecule, which inhibits the action of the phosphorylated α-subunit of eIF2, thereby activating protein translation, synergistically interacts with the genetic deficiency of protein disulfide oxidase ERO1 enfeebling tumor growth and spreading. ISRIB represses CHOP signal but surprisingly does not inhibit ERO1. Mechanistically, ISRIB increases the ER protein load with a prominent perturbing effect on ERO1 deficient Triple-Negative breast cells, which have adapted to live with low client protein load, while ERO1 deficiency selectively impairs VEGF-dependent angiogenesis. Strikingly, ERO1-deficient Triple Negative Breast Cancer xenografts have augmented ER stress response and PERK branch. In vivo, ISRIB synergistically with ERO1 deficiency inhibits the growth of Triple-Negative Breast cancer xenografts by impairing proliferation and angiogenesis, while it is not effective on the xenograft counterparts with ERO1. In summary, these results demonstrate that ISRIB together with ERO1 deficiency synergistically shatters a feature of the adaptive ER stress response while ERO1 deficiency selectively impairs angiogenesis in tumors, thereby together promoting tumor cytotoxicity. Therefore, our findings suggest two surprising findings in breast tumors: ERO1 is not regulated via CHOP and ISRIB represents a therapeutic option to efficiently inhibit tumor progression in those tumors with limited ERO1 and high PERK.
2022-07-20 | E-MTAB-11313 | biostudies-arrayexpress
Project description:Breast cancer treatment has significantly improved, achieving a five-year survival rate of 90%. However, 30% to 50% of survivors continue to suffer from persistent pain, a common long-term side effect. Tramadol, an analgesic often prescribed for postsurgical pain, has recently been shown to have anticancer effects on breast cancer cells. The use of tramadol in postoperative care has been associated with reduced recurrence and improved survival rates, but the mechanisms involved in its anticancer activity are not fully understood. This study explored how tramadol induces paraptosis, a form of nonapoptotic cell death, by focusing on endoplasmic reticulum (ER) stress and reactive oxygen species (ROS) pathways in breast cancer cells. The findings revealed that tramadol treatment increased ROS levels, triggering ER stress and activating the p-eIF2α/ATF4/CHOP signaling axis. This stress response led to cytoplasmic vacuolization and mitochondrial dysfunction, both of which are key features of paraptosis. Inhibiting ROS production or blocking the ATF4 pathway reduced tramadol-induced paraptosis, confirming the critical role of these mechanisms in breast cancer cells. In summary, tramadol induces paraptosis in breast cancer cells by activating ROS and ER stress, offering potential insight into its anticancer effects. These findings could have implications for improving both pain management and cancer treatment outcomes in breast cancer patients.
2025-11-15 | GSE282008 | GEO
Project description:CSB ablation induced apoptosis is mediated by Increased Endoplasmic Reticulum Stress Response: a gene expression study
| PRJNA325696 | ENA
Project description:Epithelial-to-Mesenchymal Transition (EMT) is a key process contributing to the aggressiveness of cancer cells. EMT is triggered by activation of different transcription factors collectively known as EMT-TFs. Different cellular cues and cell signalling networks activate EMT at transcriptional and posttranscriptional level in different biological and pathological situations. Among them, overexpression of LOXL2 (lysyl oxidase-like 2) induces EMT independent of its catalytic activity. Remarkably, perinuclear/cytoplasmic accumulation of LOXL2 is a poor prognosis marker of squamous cell carcinomas and is associated to basal breast cancer metastasis by mechanisms no yet fully understood. Here, we report that overexpression of LOXL2 promotes its accumulation in the Endoplasmic Reticulum where it interacts with HSPA5 leading to activation of the IRE1-XBP1-branch of the Unfolded Protein Response (UPR). LOXL2-dependent UPR activation induces the expression of several EMT-TFs: SNAI1, SNAI2, ZEB2 and TCF3 that are direct transcriptional targets of XBP1. Remarkably, inhibition of IRE1 blocks LOXL2-dependent upregulation of EMT-TFs thus hindering EMT induction. LOXL2 relationship to Endoplasmic Reticulum Stress
2017-05-11 | GSE90605 | GEO
Project description:Thioxotriazole copper(II) complex A0 kills cancer cells inducing endoplasmic reticulum stress and paraptotic cell death
| PRJNA115185 | ENA