Search results for "chaperone"

showing 10 items of 249 documents

Does SARS-CoV-2 Trigger Stress-InducedAutoimmunity by Molecular Mimicry? A Hypothesis.

2020

Viruses can generate molecular mimicry phenomena within their hosts. Why shouldsevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2) not be considered one of these?Information in this short review suggests that it might be so and, thus, encourages research aimingat testing this possibility. We propose, as a working hypothesis, that the virus induces antibodiesand that some of them crossreact with host’s antigens, thus eliciting autoimmune phenomena withdevasting consequences in various tissues and organs. If confirmed, by in vitro and in vivo tests,this could drive researchers to find effective treatments against the virus.

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)virusesantistress proteinslcsh:Medicinecrossreactive antibodiesWorking hypothesismedicine.disease_causeIn vivo testsViruscell stre03 medical and health sciences0302 clinical medicinecell stressAntigenmedicinemolecular mimicry030304 developmental biologyantistress protein0303 health sciencesbiologybusiness.industrySARS-CoV-2lcsh:Rmolecular chaperonesCOVID-19General Medicinemolecular chaperoneIn vitroMolecular mimicryImmunologybiology.proteinCommentaryAntibodybusiness030217 neurology & neurosurgeryJournal of clinical medicine
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The Mitochondrial Targeting Chaperone 14-3-3ε Regulates a RIG-I Translocon that Mediates Membrane Association and Innate Antiviral Immunity

2012

SummaryRIG-I is a cytosolic pathogen recognition receptor that initiates immune responses against RNA viruses. Upon viral RNA recognition, antiviral signaling requires RIG-I redistribution from the cytosol to membranes where it binds the adaptor protein, MAVS. Here we identify the mitochondrial targeting chaperone protein, 14-3-3ε, as a RIG-I-binding partner and essential component of a translocation complex or “translocon” containing RIG-I, 14-3-3ε, and the TRIM25 ubiquitin ligase. The RIG-I translocon directs RIG-I redistribution from the cytosol to membranes where it mediates MAVS-dependent innate immune signaling during acute RNA virus infection. 14-3-3ε is essential for the stable inte…

TRIM25Cancer ResearchUbiquitin-Protein Ligasesviruseschemical and pharmacologic phenomenaHepacivirusMicrobiologyAntiviral AgentsModels BiologicalArticleCell LineDEAD-box RNA HelicasesTripartite Motif Proteins03 medical and health sciences0302 clinical medicineVirologyImmunology and Microbiology(all)Protein Interaction MappingHumansReceptors ImmunologicDEAD Box Protein 58Molecular Biology030304 developmental biology0303 health sciencesInnate immune systembiologyRIG-IRNAMembrane Proteinsvirus diseasesRNA virusbiochemical phenomena metabolism and nutritionbiology.organism_classificationTranslocon3. Good healthCell biology14-3-3 Proteins030220 oncology & carcinogenesisChaperone (protein)biology.proteinDEAD Box Protein 58Parasitologybiological phenomena cell phenomena and immunityMolecular ChaperonesProtein BindingTranscription FactorsCell Host & Microbe
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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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Discovery and validation of small-molecule heat-shock protein 90 inhibitors through multimodality molecular imaging in living subjects.

2012

Up-regulation of the folding machinery of the heat-shock protein 90 (Hsp90) chaperone protein is crucial for cancer progression. The two Hsp90 isoforms (α and β) play different roles in response to chemotherapy. To identify isoform-selective inhibitors of Hsp90(α/β)/cochaperone p23 interactions, we developed a dual-luciferase (Renilla and Firefly) reporter system for high-throughput screening (HTS) and monitoring the efficacy of Hsp90 inhibitors in cell culture and live mice. HTS of a 30,176 small-molecule chemical library in cell culture identified a compound, N -(5-methylisoxazol-3-yl)-2-[4-(thiophen-2-yl)-6-(trifluoromethyl)pyrimidin-2-ylthio]acetamide (CP9), that binds to Hsp90(α/β) an…

Thymidine kinase activityProtein FoldingImmunoprecipitationLactams MacrocyclicBlotting WesternMice NudeThiophenesBiologyThioacetamideTritiumSmall Molecule LibrariesMiceco-chaperone p23Luciferases FireflyHeat shock proteinCell Line TumorNeoplasmsAcetamidesDrug DiscoveryBenzoquinonesAnimalsHumansImmunoprecipitationProtein IsoformsLuciferaseHSP90 Heat-Shock ProteinsLuciferases RenillaProstaglandin-E SynthasesMultidisciplinaryCell growthImidazolesbioluminescence imagingHsp90Small moleculeMolecular biologydrug developmentHigh-Throughput Screening Assayssmall-molecule inhibitorsIntramolecular OxidoreductasesLeadPNAS PlusCell culturePositron-Emission TomographyPyrazinesbiology.proteinPET/computed tomography imagingTomography X-Ray ComputedProceedings of the National Academy of Sciences of the United States of America
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Nerve growth factor and epidermal growth factor stimulate clusterin gene expression in PC12 cells

1999

Clusterin (apolipoprotein J) is an extracellular glycoprotein that might exert functions in development, cell death and lipid transport. Clusterin gene expression is elevated at sites of tissue remodelling, such as differentiation and apoptosis; however, the signals responsible for this regulation have not been identified. We use here the clusterin gene as a model system to examine expression in PC12 cells under the control of differentiation and proliferation signals produced by nerve growth factor (NGF) and by epidermal growth factor (EGF) respectively. NGF induced clusterin mRNA, which preceded neurite outgrowth typical of neuronal differentiation. EGF also activated the clusterin mRNA, …

Transcriptional ActivationProgrammed cell deathNeuriteMolecular Sequence DataResponse ElementsTransfectionBinding CompetitivePC12 CellsBiochemistryEpidermal growth factorConsensus SequenceNeuritesAnimalsNerve Growth FactorsRNA MessengerCloning MolecularPromoter Regions GeneticMolecular BiologyGlycoproteinsSequence DeletionNeuronsRegulation of gene expressionMessenger RNABase SequenceEpidermal Growth FactorClusterinbiologyKinaseCell DifferentiationDNACell BiologyMolecular biologyeye diseasesRatsTranscription Factor AP-1ClusterinNerve growth factorbiology.proteinsense organsCell DivisionMolecular ChaperonesSignal TransductionResearch ArticleBiochemical Journal
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Improved Expression of His6-Tagged Strictosidine Synthase cDNA for Chemo-Enzymatic Alkaloid Diversification

2010

Strictosidine synthase (STR1) catalyzes the stereoselective formation of 3alpha(S)-strictosidine from tryptamine and secologanin. Strictosidine is the key intermediate in the biosynthesis of 2,000 plant monoterpenoid indole alkaloids, and it is a key precursor of enzyme-mediated synthesis of alkaloids. An improved expression system is described which leads to optimized His(6)-STR1 synthesis in Escherichia coli. Optimal production of STR1 was achieved by determining the impact of co-expression of chaperones pG-Tf2 and pG-LJE8. The amount and activity of STR1 was doubled in the presence of chaperone pG-Tf2 alone. His(6)-STR1 immobilized on Ni-NTA can be used for enzymatic synthesis of stricto…

TryptamineStrictosidine synthaseCatharanthusStereochemistryRecombinant Fusion ProteinsIridoid GlucosidesBioengineeringBiochemistryEnzyme catalysischemistry.chemical_compoundAlkaloidsBiosynthesisCarbon-Nitrogen LyasesHistidineIridoidsVinca AlkaloidsMolecular Biologychemistry.chemical_classificationbiologyGeneral ChemistryGeneral MedicineTryptaminesEnzymechemistryBiochemistryChaperone (protein)StrictosidineBiocatalysisbiology.proteinMolecular MedicineSecologaninOligopeptidesMolecular ChaperonesChemistry & Biodiversity
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Progression of colorectal cancers correlates with overexpression and loss of polarization of expression of the htid-1 tumor suppressor.

2007

Recently, we identified htid-1, the human counterpart of the Drosophila tumor suppressor gene lethal(2)tumorous imaginal discs [l(2)tid], as a direct molecular ligand of the adenomatous polyposis coli (APC) tumor suppressor. The gene encodes three cytosolic (Tid50, Tid48 and Tid46) and three mitochondrial (Tid43, Tid40 and Tid38) proteins. In the colorectal epithelium the cytosolic forms hTid50/hTid48 interact under physiological conditions with the N-terminal region of APC. This complex which associates with additional proteins such as Hsp70, Hsc70, Actin, Dvl and Axin defines a novel physiological state of APC unrelated to beta-catenin degradation. Here we show that the expression of the …

Tumor suppressor geneProtein familyAdenomatous polyposis coliColorectal cancerAntibodies NeoplasmRNA SplicingAdenomatous Polyposis Coli ProteinGeneticsmedicineHumansHSP70 Heat-Shock ProteinsRNA NeoplasmIntestinal MucosaDNA PrimersGeneticsOncogenebiologyTumor Suppressor ProteinsWnt signaling pathwayCell DifferentiationGeneral MedicineCell cycleHSP40 Heat-Shock Proteinsmedicine.diseaseGene Expression Regulation NeoplasticChaperone (protein)biology.proteinCancer researchDisease ProgressionColorectal NeoplasmsInternational journal of molecular medicine
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Heat shock protein-peptide complexes for use in vaccines

1996

Abstract The heat shock proteins gp96, HSP70, and HSP90 are complexed to a diverse array of cellular proteins and peptides as a consequence of their chaperone functions. There is good experimental evidence that vaccination with these heat shock protein-peptide complexes elicit immune responses against chaperoned peptide antigens. As shown with gp96, this requires internalization of the heat shock protein-peptide complexes by macrophages and processing of the chaperoned peptides for class I restricted presentation. Via this process, primarily CD8+ antigen-specific T cells are primed by gp96 vaccination. This might represent a general mechanism for priming of MHC-class I restricted T cells by…

VaccinesbiologyAntigen processingImmunologyAntigen presentationCell BiologyMHC restrictionMajor histocompatibility complexMolecular biologyHsp70Cell biologyAntigenAntigens NeoplasmNeoplasmsHeat shock proteinMHC class Ibiology.proteinAnimalsHumansImmunology and AllergyPeptidesHeat-Shock ProteinsMolecular ChaperonesJournal of Leukocyte Biology
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Membrane topology and post-translational modification of the Saccharomyces cerevisiae essential protein Rot1.

2007

ROT1 is an essential gene that has been related to cell wall biosynthesis, the actin cytoskeleton and protein folding. In order to help to understand its molecular function, we carried out a characterization of the Rot1 protein. It is primarily located at the endoplasmic reticulum-nuclear membrane facing the lumen. Rot1 migrates more slowly than expected, which might suggest post-translational modification. Our results indicate that Rot1 is a protein that is neither GPI-anchored nor O-glycosylated. In contrast, it is N-glycosylated. By a directed mutagenesis of several Asn residues, we identified that the protein is simultaneously glycosylated at N103, N107 and N139. Although the mutation o…

Vesicle-associated membrane protein 8Saccharomyces cerevisiae ProteinsMolecular Sequence DataBioengineeringmacromolecular substancesSaccharomyces cerevisiaeBiologyEndoplasmic ReticulumApplied Microbiology and BiotechnologyBiochemistryProtein structureSEC62Gene Expression Regulation FungalGeneticsAmino Acid SequenceCell MembraneMembrane ProteinsActin cytoskeletonCell biologyTransport proteinProtein Structure TertiaryTransmembrane domainProtein TransportBiochemistryMembrane topologyProtein foldingProtein Processing Post-TranslationalBiotechnologyMolecular ChaperonesYeast (Chichester, England)
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Treatment of Anderson-Fabry Disease

2020

Fabry disease is an X-linked disorder of glycosphingolipid metabolism that results in progressive accumulation of neutral glycosphingolipids, predominantly globotriaosylsphingosine (Gb3) in lysosomes, as well as other cellular compartments of several tissues, causing multi-organ manifestations (acroparesthesias, hypohidrosis, angiokeratomas, signs and symptoms of cardiac, renal, cerebrovascular involvement). Pathogenic mutations lead to a deficiency of the lysosomal enzyme alpha-galactosidase A (GLA). In the presence of high clinical suspicion, a careful physical examination and specific laboratory tests are required. Finally, the diagnosis of Fabry’s disease is confirmed by the demonstrat…

Viral vectorsMaleGenetic enhancementChaperone therapyPhysical examinationDiseaseKidneyViral vector03 medical and health sciencesGene therapy0302 clinical medicineDrug DiscoverymedicineHumansEnzyme Replacement Therapy030304 developmental biologyPharmacology0303 health sciencesmedicine.diagnostic_testbusiness.industryPharmacologicalGenetic TherapyEnzyme replacement therapymedicine.diseaseFabry diseasePharmacological chaperonealpha-GalactosidaseImmunologyFabry DiseaseFemaleStem cellbusiness030217 neurology & neurosurgerymedicine.drugCurrent Pharmaceutical Design
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