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MetabolomicsER stress inhibits liver fatty acid oxidation while unmitigated stress leads to anorexia-induced lipolysis and both liver and kidney steatosis
The unfolded protein response (UPR), induced by endoplasmic reticulum (ER) stress, regulates the expression of factors that restore protein folding homeostasis. However, in the liver and kidney, ER stress also leads to lipid accumulation, accompanied at least in the liver by transcriptional suppress...
2017-06-23 | MTBLS472 | MetaboLights
TranscriptomicsThe genetic architecture of the genome-wide transcriptional response to ER stress in the mouse
Endoplasmic reticulum (ER) stress occurs when misfolded proteins accumulate in the ER. The cellular response to ER stress involves complex transcriptional and translational changes, important to the survival of the cell. ER stress is a primary cause and a modifier of many human diseases. A first ste...
ORGANISM(S): Mus musculus 
2014-12-02 | E-GEOD-63756 | biostudies-arrayexpress
TranscriptomicsNuclear receptor LRH-1/NR5A2 is required and targetable for liver endoplasmic reticulum stress resolution.
Chronic endoplasmic reticulum (ER) stress results in toxicity that contributes to multiple human disorders. We report a stress resolution pathway initiated by the nuclear receptor LRH-1 that is independent of known unfolded protein response (UPR) pathways. Like mice lacking primary UPR components, h...
ORGANISM(S): Mus musculus 
2015-05-12 | E-GEOD-68718 | biostudies-arrayexpress
UnknownProtective effects of UFL1 against endoplasmic reticulum stress-induced autophagy in bovine mammary epithelial cells.
Ubiquitin-fold modifier 1 (UFM1)-specific ligase 1 (UFL1) is an important component of the UFM1 conjugation system, which is required for various cellular processes including protein translation, apoptosis, autophagy, and signal transduction. However, both, the expression of UFL1 in mammary cells an...
S-EPMC6883021 | biostudies-literature
UnknownGenome-wide screen identifies a novel p97/CDC-48-dependent pathway regulating ER-stress-induced gene transcription.
The accumulation of misfolded proteins in the endoplasmic reticulum (ER) activates the Unfolded Protein Response (UPR(ER)) to restore ER homeostasis. The AAA(+) ATPase p97/CDC-48 plays key roles in ER stress by promoting both ER protein degradation and transcription of UPR(ER) genes. Although the me...
S-EPMC4364872 | biostudies-literature
TranscriptomicsLack of de novo phosphatidylinositol synthesis leads to endoplasmic reticulum stress and hepatic steatosis in cdipt-deficient zebrafish
cdipt is an essential gene in the synthesis of phosphatidylinositol (PtdIns) in the zebrafish, Danio rerio. The zebrafish mutant cdipt^hi559Tg (ZL782) carries a retroviral insertion which inactivates cdipt. Homozygous mutants exhibit hepatocellular endoplasmic reticulum (ER) stress and non-alcoholic...
ORGANISM(S): Danio rerio 
2011-05-09 | E-GEOD-17711 | biostudies-arrayexpress
ProteomicsCell survival and adaptation to chronic endoplasmic reticulum stress in thyrocytes
The large secretory glycoprotein, thyroglobulin, is the primary translation product of thyroid follicular cells. This difficult-to-fold protein is readily susceptible to structural alterations that render the misfolded thyroglobulin unable to be exported from the endoplasmic reticulum (ER) a known c...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-02-25 | MSV000085006 | MassIVE
UnknownEndoplasmic reticulum stress and therapeutic strategies in metabolic, neurodegenerative diseases and cancer.
The accumulation of unfolded or misfolded proteins within the endoplasmic reticulum (ER), due to genetic determinants and extrinsic environmental factors, leads to endoplasmic reticulum stress (ER stress). As ER stress ensues, the unfolded protein response (UPR), comprising three signaling pathways-...
S-EPMC10956371 | biostudies-literature
TranscriptomicsThe eIF2 kinase PERK and the integrated stress response facilitate activation of ATF6 during endoplasmic reticulum stress
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 ...
ORGANISM(S): Mus musculus 
2012-01-20 | E-GEOD-29929 | biostudies-arrayexpress
UnknownFanning the Flames of Endoplasmic Reticulum (ER) Stress: Can Sphingolipid Metabolism Be Targeted to Enhance ER Stress-Associated Immunogenic Cell Death in Cancer?
The three arms of the unfolded protein response (UPR) surveil the luminal environment of the endoplasmic reticulum (ER) and transmit information through the lipid bilayer to the cytoplasm to alert the cell of stress conditions within the ER lumen. That same lipid bilayer is the site of de novo synth...
S-EPMC10877730 | biostudies-literature
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