Search results for "UNFOLDED PROTEIN RESPONSE"

showing 10 items of 86 documents

2-Hydroxyoleic Acid Induces ER Stress and Autophagy in Various Human Glioma Cell Lines

2012

Background: 2-Hydroxyoleic acid is a synthetic fatty acid with potent anti-cancer activity which does not induce undesired side effects. However, the molecular and cellular mechanisms by which this compound selectively kills human glioma cancer cells without killing normal cells is not fully understood. The present study was designed to determine the molecular bases underlying the potency against 1321N1, SF-767 and U118 human glioma cell lines growth without affecting non cancer MRC-5 cells. Methodology/Principal Findings: The cellular levels of endoplasmic reticulum (ER) stress, unfolded protein response (UPR) and autophagy markers were determined by quantitative RT-PCR and immunoblotting …

Tetrazolium SaltsOleic AcidsEndoplasmic ReticulumBiochemistry2-Hydroxyoleic AcidDrug DiscoveryMolecular Cell BiologyNeurological TumorsLungProtein MetabolismCellular Stress ResponsesMultidisciplinaryCell DeathBrain NeoplasmsQFatty AcidsRGliomaLipidsSignaling CascadesCell biologyOncologyMedicineSignal transductionResearch ArticleBiotechnologySignal TransductionCell SurvivalScienceAntineoplastic AgentsBiologyStress Signaling CascadeCell LineGliomaCell Line TumormedicineAutophagyHumansBiologyAutophagyProteinsCancers and NeoplasmsFibroblastsmedicine.diseaseChaperone ProteinsThiazolesMetabolismCell cultureApoptosisCancer cellUnfolded protein responsePLoS ONE
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Protective effect of paraoxonase-2 against endoplasmic reticulum stress-induced apoptosis is lost upon disturbance of calcium homoeostasis

2008

PON2 (paraoxonase-2) is a ubiquitously expressed antioxidative protein which is largely found in the ER (endoplasmic reticulum). Addressing the cytoprotective functions of PON2, we observed that PON2 overexpression provided significant resistance to ER-stress-induced caspase 3 activation when the ER stress was induced by interference with protein modification (by tunicamycin or dithiothreitol), but not when ER stress was induced by disturbance of Ca2+ homoeostasis (by thapsigargin or A23187). When analysing the underlying molecular events, we found an activation of the PON2 promoter in response to all tested ER-stress-inducing stimuli. However, only tunicamycin and dithiothreitol resulted i…

ThapsigarginRNA StabilityApoptosisCaspase 3Protein degradationEndoplasmic ReticulumBiochemistryGene Expression Regulation EnzymologicCell Linechemistry.chemical_compoundStress PhysiologicalHomeostasisHumansEnzyme InhibitorsPromoter Regions Genetic3' Untranslated RegionsMolecular BiologyCalcimycinIonophoresbiologyAryldialkylphosphataseCalpainTunicamycinEndoplasmic reticulumCalpainCell BiologyTunicamycinCell biologyDithiothreitolchemistryApoptosisbiology.proteinUnfolded protein responseThapsigarginCalcium5' Untranslated RegionsBiochemical Journal
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Tributyltin(Iv) butyrate: A novel epigenetic modifier with er stress-and apoptosis-inducing properties in colon cancer cells

2021

Organotin(IV) compounds are a class of non-platinum metallo-conjugates exhibiting antitumor activity. The effects of different organotin types has been related to several mechanisms, including their ability to modify acetylation protein status and to promote apoptosis. Here, we focus on triorganotin(IV) complexes of butyric acid, a well-known HDAC inhibitor with antitumor properties. The conjugated compounds were synthesized and characterised by FTIR spectroscopy, multi-nuclear (1H, 13C and 119Sn) NMR, and mass spectrometry (ESI-MS). In the triorganotin(IV) complexes, an anionic monodentate butyrate ligand was observed, which coordinated the tin atom on a tetra-coordinated, monomeric enviro…

Triorganotin(IV) butyratesPharmaceutical ScienceOrganic chemistryApoptosisButyrateArticleHistone DeacetylasesAnalytical ChemistryEpigenesis GeneticButyric acidchemistry.chemical_compoundQD241-441HDAC inhibitorsCell Line TumorSettore BIO/10 - BiochimicaDrug DiscoveryHumansPhysical and Theoretical ChemistrybiologyAcetylationLigand (biochemistry)Endoplasmic Reticulum StressColon cancerHistonechemistryBiochemistryHistone acetylationChemistry (miscellaneous)ApoptosisAcetylationSettore CHIM/03 - Chimica Generale E InorganicaColonic NeoplasmsTributyltinbiology.proteinUnfolded protein responseMolecular MedicineButyric AcidTrialkyltin CompoundsER stressProtein Processing Post-Translational
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Oxidative stress, a new hallmark in the pathophysiology of Lafora progressive myoclonus epilepsy

2015

12 páginas, 4 figuras, 1 tabla

Ubiquitin-Protein LigasesFree radicalsBiologymedicine.disease_causeBiochemistryAntioxidantsLafora diseasechemistry.chemical_compoundLaforinPhysiology (medical)medicineHumansLafora diseaseProteostasis DeficienciesGlycogenAutophagyProtein Tyrosine Phosphatases Non-ReceptorMalinmedicine.diseaseOxidative StressProteostasisLafora DiseaseBiochemistrychemistryProteasomeOxidative stressMutationProteostasisUnfolded protein responseCarrier ProteinsLaforinGlycogenOxidative stressFree Radical Biology and Medicine
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Endoplasmic Reticulum stress reduces COPII vesicle formation and modifies Sec23a cycling at ERESs

2013

AbstractExit from the Endoplasmic Reticulum (ER) of newly synthesized proteins is mediated by COPII vesicles that bud from the ER at the ER Exit Sites (ERESs). Disruption of ER homeostasis causes accumulation of unfolded and misfolded proteins in the ER. This condition is referred to as ER stress. Previously, we demonstrated that ER stress rapidly impairs the formation of COPII vesicles. Here, we show that membrane association of COPII components, and in particular of Sec23a, is impaired by ER stress-inducing agents suggesting the existence of a dynamic interplay between protein folding and COPII assembly at the ER.

Vesicular Transport ProteinsBiophysicsEndoplasmic ReticulumBiochemistryCell LineVesicular Transport ProteinGeneticStructural BiologyERESGeneticsVesicular Transport ProteinsHumansCOPIIEndoplasmic Reticulum StreMolecular BiologyCOPIIChemistryVesicleEndoplasmic reticulumSec23Cell BiologyCOP-Coated VesiclesSEC23AEndoplasmic Reticulum StressCell biologyBiophysicUnfolded protein responseER streProtein foldingCOP-Coated VesiclesER stressCOP-Coated VesicleHumanProtein BindingFEBS Letters
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Effect of Ligands on HP-Induced Unfolding and Oligomerization of β-Lactoglobulin

2020

ABSTRACTTo probe intermediate states during unfolding and oligomerization of proteins remains a major challenge. High pressure (HP) is a powerful tool for studying these problems, revealing subtle structural changes in proteins not accessible by other means of denaturation. Bovine β-lactoglobulin (BLG), the main whey protein, has a strong propensity to bind various bioactive molecules, such as retinol and resveratrol, two ligands with different affinity and binding sites. By combining in situ HP-small-angle neutron scattering (SANS) and HP-UV/visible absorption spectroscopy, we report the specific effects of these ligands on 3D conformational and local changes in BLG induced by HP. Dependin…

Whey proteinProtein Folding[SDV]Life Sciences [q-bio]BiophysicsAb initioLactoglobulins010402 general chemistryLigands01 natural sciences03 medical and health sciences0404 agricultural biotechnologyAnimalsDenaturation (biochemistry)[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyBinding site030304 developmental biology0303 health sciencesBinding SitesChemistry04 agricultural and veterinary sciencesArticlesLigand (biochemistry)040401 food science0104 chemical sciencesCovalent bondBiophysicsUnfolded protein responseProtein foldingCattleHydrophobic and Hydrophilic Interactions
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Depletion ofL-arginine induces autophagy as a cytoprotective response to endoplasmic reticulum stress in human T lymphocytes

2012

PMCID: PMC3494587

X-Box Binding Protein 1Proteasome Endopeptidase ComplexProgrammed cell deathXBP1CD3 ComplexMAP Kinase Signaling SystemRNA SplicingT-LymphocytesT cellDown-RegulationApoptosisRegulatory Factor X Transcription FactorsUbiquitin-Activating EnzymesProtein Serine-Threonine KinasesBiologyArginineLymphocyte ActivationAutophagy-Related Protein 7Jurkat cellsJurkat CellsEndoribonucleasesAutophagymedicineHumansMolecular BiologyCell ProliferationTOR Serine-Threonine KinasesAutophagyMembrane ProteinsCell BiologyBECN1Endoplasmic Reticulum StressG1 Phase Cell Cycle CheckpointsBasic Research Paper3. Good healthCell biologyDNA-Binding Proteinsmedicine.anatomical_structureCytoprotectionApoptosisUnfolded protein responseBeclin-1MitogensApoptosis Regulatory ProteinsLysosomesProto-Oncogene Proteins c-aktTranscription FactorsAutophagy
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OP0204 Autophagy and Unfolded Protein Response: A Fine Balance that can Influence the Pathogenesis of Ankylosing Spondylitis and Inflammatory Bowel D…

2015

Background We have shown an increase in the unfolded protein response (UPR) with decreased ERAP1 or ERAP2 function in an in vitro system. Similarly UPR has been demonstrated to correlate with onset of disease in the HLA-B27 rat model. UPR has been difficult to demonstrate in the gut of AS patients but autophagy is upregulated. ERAP2 is associated with both AS and inflammatory bowel disease (IBD). Objectives Here we explore the moderating effect of autophagy on UPR. Specifically we study the impact of suppressing autophagy on UPR. Methods Lamina Propria Mononuclear cells (LPMC) were isolated from terminal ileal biopsies of 10 AS patients. Autophagy was suppressed with 2 agents anisomycin and…

XBP1biologymedicine.diagnostic_testImmunologyAutophagyMajor histocompatibility complexdigestive systemGeneral Biochemistry Genetics and Molecular BiologyCell biologyFlow cytometryPathogenesischemistry.chemical_compoundRheumatologychemistryDownregulation and upregulationbiology.proteinUnfolded protein responsemedicineImmunology and AllergyAnisomycinAnnals of the Rheumatic Diseases
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Mitochondria and T2D: Role of Autophagy, ER Stress, and Inflammasome.

2020

Type 2 diabetes (T2D) is one of the main current threats to human health. Both T2D and its numerous clinical complications are related to mitochondrial dysfunction and oxidative stress. Over the past decade, great progress has been made in extending our knowledge about the signaling events regulated by mitochondria. However, the links among mitochondrial impairment, oxidative stress, autophagy, endoplasmic reticulum (ER) stress, and activation of the inflammasome still need to be clarified. In light of this deficit, we aim to provide a review of the existing literature concerning the complicated crosstalk between mitochondrial impairment, autophagy, ER stress, and the inflammasome in the mo…

autophagyMitochondrial DiseasesInflammasomesEndocrinology Diabetes and Metabolism030209 endocrinology & metabolismMitochondrionmedicine.disease_causeInflammasome03 medical and health sciences0302 clinical medicineEndocrinologyinflammasomemedicineAutophagyAnimalsHumansbusiness.industryEndoplasmic reticulumAutophagyMolecular pathogenesisInflammasomeType 2 diabetesEndoplasmic Reticulum StressCell biologyMitochondriamitochondriaCrosstalk (biology)Oxidative StressDiabetes Mellitus Type 2Unfolded protein responsetype 2 diabetesbusinessOxidative stressmedicine.drugTrends in endocrinology and metabolism: TEM
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Hypusinated eIF5A is required for the translation of collagen.

2021

ABSTRACT Translation of mRNAs that encode peptide sequences with consecutive prolines (polyproline) requires the conserved and essential elongation factor eIF5A to facilitate the formation of peptide bonds. It has been shown that, upon eIF5A depletion, yeast ribosomes stall in polyproline motifs, but also in tripeptide sequences that combine proline with glycine and charged amino acids. Mammalian collagens are enriched in putative eIF5A-dependent Pro-Gly-containing tripeptides. Here, we show that depletion of active eIF5A in mouse fibroblasts reduced collagen type I α1 chain (Col1a1) content, which concentrated around the nuclei. Moreover, it provoked the upregulation of endoplasmic reticul…

chemistry.chemical_classificationEndoplasmic reticulumRNA-Binding ProteinsTranslation (biology)Cell BiologyTripeptideSaccharomyces cerevisiaeBiologyCell biologyAmino acidElongation factorCollagen type I alpha 1MicechemistryPeptide Initiation FactorsUnfolded protein responseAnimalsCollagenRibosomesPolyproline helixJournal of cell science
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