Search results for "UNFOLDED PROTEIN RESPONSE"

showing 10 items of 86 documents

Lafora disease fibroblasts exemplify the molecular interdependence between thioredoxin 1 and the proteasome in mammalian cells

2013

13 páginas, 8 figuras (que no aparecen en este documento, se pueden consultar en: http://www.sciencedirect.com/science/article/pii/S0891584913003274#ec0005)

Cell signalingProteasome Endopeptidase ComplexBlotting WesternFree radicalsBiologyBiochemistryLafora diseaseThioredoxin 1MiceThioredoxinsPhysiology (medical)medicineAnimalsHumansImmunoprecipitationLafora diseaseEndoplasmic Reticulum Chaperone BiPCell proliferationMicroscopy ConfocalProteasomeReverse Transcriptase Polymerase Chain ReactionEndoplasmic reticulumCell cycleFibroblastsSubcellular localizationmedicine.diseaseFlow CytometryCell biologyRare diseasesCytosolOxidative StressBiochemistryProteasomeLafora DiseaseUnfolded protein responseNIH 3T3 CellsAntioxidant enzymesOxidation-Reduction
researchProduct

Endoplasmic reticulum stress is involved in response of human laryngeal carcinoma cells to carboplatin but is absent in carboplatin resistant cells

2013

The major obstacle of successful tumor treatment with carboplatin (CBP) is the development of drug resistance. In the present study, we found that following treatment with CBP the amount of platinum which enters the human laryngeal carcinoma (HEp2)-derived CBP- resistant (7T) cells is reduced relative to the parental HEp2. As a consequence, the formation of reactive oxidative species (ROS) is reduced, the induction of endoplasmic reticulum (ER) stress is diminished, the amount of inter- and intrastrand cross-links is lower, and the induction of apoptosis is depressed. In HEp2 cells, ROS scavenger tempol, inhibitor of ER stress salubrinal, as well as gene silencing of ER stress marker CCAAT/…

Celllcsh:MedicineApoptosisCarboplatinSalubrinalapoptosis; carboplatin; drug resistance; endoplasmic reticulum stress; reactive oxidative species; tumor cellschemistry.chemical_compound0302 clinical medicineBlotting Southwesternlcsh:Science0303 health sciencesMultidisciplinaryThioureaGeologyEndoplasmic Reticulum Stress3. Good healthmedicine.anatomical_structure030220 oncology & carcinogenesisSignal transductionSignal TransductionResearch ArticleProgrammed cell deathCell SurvivalBlotting WesternBiologyReal-Time Polymerase Chain ReactionCyclic N-Oxides03 medical and health sciencesCell Line TumormedicineHumansGene SilencingLaryngeal NeoplasmsBiology030304 developmental biologyDNA PrimersPlatinumEndoplasmic reticulumlcsh:RCarcinomaMolecular biologychemistryCell cultureApoptosisCinnamatesDrug Resistance NeoplasmUnfolded protein responseCancer researchlcsh:QSpin LabelsReactive Oxygen Species
researchProduct

Reply to Dr Michaudet al.

2015

There is no abstract

Cholagogues and Cholereticsbusiness.industryEndoplasmic reticulumAmyotrophic Lateral SclerosisTaurochenodeoxycholic acidTauroursodeoxycholic acidMitochondrionPharmacologyEndoplasmic Reticulummedicine.diseaseTaurochenodeoxycholic Acidchemistry.chemical_compoundNeurologychemistryImmunologyUnfolded Protein ResponsemedicineUnfolded protein responseAnimalsHumansTUDCA ALSSettore MED/26 - NeurologiaNeurology (clinical)Amyotrophic lateral sclerosisbusinessEuropean Journal of Neurology
researchProduct

ER stress in human hepatic cells treated with Efavirenz: Mitochondria again

2013

Background & Aims ER stress is associated with a growing number of liver diseases, including drug-induced hepatotoxicity. The non-nucleoside analogue reverse transcriptase inhibitor Efavirenz, a cornerstone of the multidrug strategy employed to treat HIV1 infection, has been related to the development of various adverse events, including metabolic disturbances and hepatic toxicity, the mechanisms of which remain elusive. Recent evidence has pinpointed a specific mitochondrial effect of Efavirenz in human hepatic cells. This study assesses the induction of ER stress by Efavirenz in the same model and the implication of mitochondria in this process. Methods Primary human hepatocytes and Hep3B…

CyclopropanesEfavirenzXBP1Anti-HIV AgentsMitochondria LiverMitochondrionBiologyPharmacologyModels BiologicalCell Linechemistry.chemical_compoundMicroscopy Electron TransmissionDownregulation and upregulationHumansSide effectsEndoplasmic Reticulum Chaperone BiPCells CulturedHepatologyEndoplasmic reticulumHepatotoxicityATF4HIVEndoplasmic Reticulum StressHIV Reverse TranscriptaseBenzoxazinesMitochondriachemistryAlkynesHepatocytesHepatic stellate cellUnfolded protein responseReverse Transcriptase InhibitorsThapsigarginCalciumEfavirenzER stressBiomarkersJournal of Hepatology
researchProduct

High levels of the molecular chaperone Mdg1/ERdj4 reflect the activation state of endothelial cells

2003

Mdg1/ERdj4, a mammalian chaperone that belongs to the HSP40 protein family, has been reported to be located in the endoplasmic reticulum (ER), is induced by ER stress, and protects ER stressed cells from apoptosis. Here we show that under normal physiological conditions, Mdg1/ERdj4 is expressed at various levels in the vasculature due to different activation states of the endothelium. To elucidate the stimuli that induce ER stress and thus upregulate Mdg1/ERdj4, we investigated the effect of several endothelium specific stressors on its expression. Mdg1/ERdj4 mRNA is induced by activated macrophages, by nitric oxide (NO) and heat shock, and during terminal cell differentiation, whereas shea…

EndotheliumCell SurvivalCellular differentiationApoptosisCell CommunicationEndoplasmic ReticulumNitric OxideMiceStress PhysiologicalmedicineAnimalsHumansRNA MessengerHeat shockEndoplasmic Reticulum Chaperone BiPbiologyMacrophagesEndoplasmic reticulumMembrane ProteinsProteinsCell BiologyHSP40 Heat-Shock ProteinsCoculture TechniquesUp-RegulationHsp70Cell biologyProtein Transportmedicine.anatomical_structureApoptosisChaperone (protein)biology.proteinUnfolded protein responseEndothelium VascularStress MechanicalCarrier ProteinsCell NucleolusHeat-Shock ResponseHeLa CellsMolecular ChaperonesExperimental Cell Research
researchProduct

The Evolutionary Conserved Transmembrane BAX Inhibitor Motif (TMBIM) Containing Protein Family Members 5 and 6 Are Essential for the Development and …

2021

Frontiers in cell and developmental biology 9, 666484 (2021). doi:10.3389/fcell.2021.666484 special issue: "Cell Death and Survival / You-Wen He, Speciality Chief Editor; Craig Michael Walsh, Speciality Chief Editor; Arm Ruhul Amin, Associate Editor; Gustavo P. Amarante-Mendes, Associate Editor"

Gene knockdowncalciumProtein familylifeguardQH301-705.5Cell BiologyBiologyMitochondrionbiology.organism_classificationTransmembrane proteinGHITMCell biologymitochondriaMICS1RNA interferenceGRINAUnfolded protein responseDrosophila melanogasterBiology (General)ER stressDevelopmental Biology
researchProduct

Thermal aggregation of glycated bovine serum albumin

2010

International audience; Aggregation and glycation processes in proteins have a particular interest in medicine fields and in food technology. Serum albumins are model proteins which are able to self-assembly in aggregates and also sensitive to a non-enzymatic glycation in cases of diabetes. In this work, we firstly reported a study on the glycation and oxidation effects on the structure of bovine serum albumin (BSA). The experimental approach is based on the study of conformational changes of BSA at secondary and tertiary structures by FTIR absorption and fluorescence spectroscopy, respectively. Secondly, we analysed the thermal aggregation process on BSA glycated with different glucose con…

Glycation End Products AdvancedGlycosylationHot TemperatureGlycoxidation02 engineering and technologyProtein aggregationBiochemistryProtein Structure SecondaryAnalytical Chemistrychemistry.chemical_compoundProtein structureGlycationSpectroscopy Fourier Transform InfraredScattering RadiationGlycated Serum AlbuminBovine serum albuminGlycation0303 health sciencesbiologyChemistryTryptophanSerum Albumin Bovine021001 nanoscience & nanotechnology3. Good healthSpectrophotometryProtein aggregation0210 nano-technologyOxidation-ReductionGlycosylationBiophysicsSerum albuminIn Vitro Techniques03 medical and health sciencesAnimalsMolecular BiologySerum Albumin030304 developmental biologyChromatographyAlbuminAlbuminLight scatteringSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Protein tertiary structureProtein Structure TertiaryKineticsFTIR spectroscopyGlucoseSpectrometry FluorescenceUnfolded Protein Responsebiology.proteinCattleProtein Multimerization[SDV.MHEP]Life Sciences [q-bio]/Human health and pathologyBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
researchProduct

Dataset related to article "The unfolded protein response in amyotrophic later sclerosis: results of a phase 2 trial"

2021

The data support the findings of the study "The Unfolded Protein Response in Amyotrophic Later Sclerosis: Results of a Phase 2 Trial". They include demographic and clinical data at baseline, and changes measured by the primary and secondary outcomes at 6 months

GuanabenzAmyotrophic Lateral SclerosisUnfolded Protein Responsephase 2 trial
researchProduct

The new murine hepatic 3A cell line responds to stress stimuli by activating an efficient Unfolded Protein Response (UPR)

2012

In the present study we have investigated the properties of a novel cell line (3A cells) obtained from the liver of 14.5. days post coitum (dpc) wild-type mouse embryo. 3A cells morphology was characterized by fluorescent localization of F-actin and β-catenin. The expression of specific genes and proteins essential to liver function in these cells was comparable or even more efficient then in the differentiated hepatocytic cell line MMH-D6. 3A cells also showed the capability to excrete molecules in extracellular spaces resembling functional bile canaliculi, glycogen storage activity and the ability to control retinol-binding protein 4 secretion in response to retinol deprivation. Their re…

Hepatocytes; ER stress; RBP4BiologyToxicologyCellular modelCell LineMicechemistry.chemical_compoundStress PhysiologicalExtracellularAnimalsHepatocyteSecretionActinbeta CateninAnimalReverse Transcriptase Polymerase Chain ReactionRBP4Gene Expression ProfilingTunicamycinDays post coitumCellular model; ER stress; Hepatocytes; RBP4; Actins; Animals; Cell Line; Fluorescein; Gene Expression Profiling; Glycogen; Liver; Retinol-Binding Proteins Plasma; Reverse Transcriptase Polymerase Chain Reaction; Stress Physiological; Tunicamycin; Unfolded Protein Response; beta Catenin; Mice; ToxicologyGeneral MedicineTunicamycinMolecular biologyActinsLiverchemistryCell cultureUnfolded Protein ResponseUnfolded protein responseER streFluoresceinLiver functionCellular modelRetinol-Binding Proteins PlasmaGlycogenToxicology in Vitro
researchProduct

Adaptive suppression of the ATF4–CHOP branch of the unfolded protein response by toll-like receptor signalling

2009

The endoplasmic reticulum (ER) unfolded protein response (UPR) restores equilibrium to the ER, but prolonged expression of the UPR effector CHOP (GADD153) is cytotoxic. We found that CHOP expression induced by ER stress was suppressed by prior engagement of toll-like receptor (TLR) 3 or 4 through a TRIF-dependent pathway. TLR engagement did not suppress phosphorylation of PERK or eIF-2alpha, which are upstream of CHOP, but phospho-eIF-2alpha failed to promote translation of the CHOP activator ATF4. In mice subjected to systemic ER stress, pretreatment with low dose lipopolysaccharide (LPS), a TLR4 ligand, suppressed CHOP expression and apoptosis in splenic macrophages, renal tubule cells an…

LipopolysaccharidesBiologyCHOPEndoplasmic ReticulumArticleMice03 medical and health sciences0302 clinical medicineStress Physiologicalhemic and lymphatic diseasesAnimalsHumansCells Cultured030304 developmental biologyMice Knockout0303 health sciencesToll-like receptorEndoplasmic reticulumToll-Like ReceptorsATF4Cell BiologyActivating Transcription Factor 4Cell biologyMice Inbred C57BLAdaptor Proteins Vesicular TransportTRIF030220 oncology & carcinogenesisUnfolded Protein ResponseUnfolded protein responseTLR4biological phenomena cell phenomena and immunitySignal transductionTranscription Factor CHOPSignal TransductionNature Cell Biology
researchProduct