Search results for "Heat-shock proteins"

showing 10 items of 310 documents

The HSP90 inhibitor, 17AAG, protects the intestinal stem cell niche and inhibits graft versus host disease development.

2016

IF 7.932; International audience; Graft versus host disease (GvHD), which is the primary complication of allogeneic bone marrow transplantation, can alter the intestinal barrier targeted by activated donor T-cells. Chemical inhibition of the stress protein HSP90 was demonstrated in vitro to inhibit T-cell activation and to modulate endoplasmic reticulum (ER) stress to which intestinal cells are highly susceptible. Since the HSP90 inhibitor 17-allylamino-demethoxygeldanamycin (17AAG) is developed in clinics, we explored here its ability to control intestinal acute GvHD in vivo in two mouse GvHD models (C57BL/6 -> BALB/c and FVB/N -> Lgr5-eGFP), ex vivo in intestine organoids and in vitro in …

0301 basic medicineX-Box Binding Protein 1Cancer ResearchLactams MacrocyclicRNA SplicingT-CellsGraft vs Host Disease[SDV.CAN]Life Sciences [q-bio]/Cancer[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiology[ SDV.CAN ] Life Sciences [q-bio]/CancerHsp90 inhibitor03 medical and health sciencesMiceSensitivityInflammatory-Bowel-diseaseGeneticsmedicineBenzoquinonesAnimals[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyNeural progenitor cellsHSP90 Heat-Shock ProteinsIntestinal MucosaStem Cell Niche[ SDV.GEN.GH ] Life Sciences [q-bio]/Genetics/Human genetics[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyMolecular BiologyLeukemia[ SDV.BC ] Life Sciences [q-bio]/Cellular BiologyBone-Marrow-TransplantationMoleculesmedicine.diseaseStem cell niche3. Good healthIre1-AlphaIntestinesMice Inbred C57BL030104 developmental biologyGraft-versus-host diseaseEr Stress[SDV.GEN.GH]Life Sciences [q-bio]/Genetics/Human geneticsCytoprotectionImmunologyMultiple-MyelomaFemaleOncogene
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Impact of polymer-modified gold nanoparticles on brain endothelial cells: exclusion of endoplasmic reticulum stress as a potential risk factor

2016

A library of polymer-coated gold nanoparticles (AuNPs) differing in size and surface modifications was examined for uptake and induction of cellular stress responses in the endoplasmic reticulum (ER stress) in human brain endothelial cells (hCMEC/D3). ER stress is known to affect the physiology of endothelial cells (ECs) and may lead to inflammation or apoptosis. Thus, even if applied at non-cytotoxic concentrations ER stress caused by nanoparticles should be prevented to reduce the risk of vascular diseases and negative effects on the integrity of barriers (e.g. blood-brain barrier). We exposed hCMEC/D3 to twelve different AuNPs (three sizes: 18, 35, and 65 nm, each with four surface-modif…

0301 basic medicineXBP1BiPCell SurvivalPolymersBiomedical EngineeringMetal NanoparticlesApoptosis02 engineering and technologyBiologyEndoplasmic ReticulumToxicologyArticleCell LineProinflammatory cytokine03 medical and health sciencescell stressDownregulation and upregulationRisk FactorsHeat shock proteinAnimalsHumansHSP70 Heat-Shock ProteinsParticle SizeHeat-Shock ProteinsATF6Endoplasmic reticulumInterleukin-8ATF4Endothelial CellsMembrane Proteinsunfolded protein responseEndoplasmic Reticulum Stress021001 nanoscience & nanotechnologyQPActivating Transcription Factor 4Cell biology030104 developmental biologyBlood-Brain Barriertight junction proteinsImmunologyUnfolded protein responseGold0210 nano-technologyTranscription Factor CHOPNanotoxicology
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Viable But Not Culturable (VBNC) state of Brettanomyces bruxellensis in wine: New insights on molecular basis of VBNC behaviour using a transcriptomi…

2016

International audience; The spoilage potential of Brettanomyces bruxellensis in wine is strongly connected with the aptitude of this yeast to enter in a Viable But Non Culturable (VBNC) state when exposed to the harsh wine conditions. In this work, we characterized the VBNC behaviour of seven strains of B. bruxellensis representing a regional intraspecific biodiversity, reporting conclusive evidence for the assessment of VBNC as a strain-dependent character. The VBNC behaviour was monitored by fluorescein diacetate staining/flow cytometry for eleven days after addition of 0.4, 0.6, 0.8, 1 and 1.2 mg/L of molecular SO2 (entrance in the VBNC state) and after SO2 removal (exit from the VBNC st…

0301 basic medicine[ SDV.AEN ] Life Sciences [q-bio]/Food and NutritionColony Count MicrobialExpressionSaccharomyces-cerevisiaeTranscriptometranscriptomicsHomeostasisSulfur DioxideHeat-Shock Proteinsmedicine.diagnostic_testViabilityCarbohydrate MetabolismOxidation-ReductionVolatile phenol production030106 microbiologyBrettanomyces bruxellensisBrettanomycesBiologyFlow cytometryMicrobiology03 medical and health sciencesPhenolsHeat shock proteinsulphitemedicineSulfiteswineGeneRna-seqBrettanomyces; spoilage; sulphite; transcriptomics; Viable But Not Culturable (VBNC); wine; food science; microbiologyWineMicrobial ViabilityGene Expression ProfilingspoilagemicrobiologyDNA replicationNonculturable bacteriabiology.organism_classificationCampylobacter-jejuniSulfur-dioxideYeastYeastCulture MediaOxidative StressFood MicrobiologyViable But Not Culturable (VBNC)food science[SDV.AEN]Life Sciences [q-bio]/Food and NutritionSettore AGR/16 - Microbiologia Agraria
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The Antisense RNA Approach: a New Application for In Vivo Investigation of the Stress Response of Oenococcus oeni, a Wine-Associated Lactic Acid Bact…

2015

ABSTRACT Oenococcus oeni is a wine-associated lactic acid bacterium mostly responsible for malolactic fermentation in wine. In wine, O. oeni grows in an environment hostile to bacterial growth (low pH, low temperature, and ethanol) that induces stress response mechanisms. To survive, O. oeni is known to set up transitional stress response mechanisms through the synthesis of heat stress proteins (HSPs) encoded by the hsp genes, notably a unique small HSP named Lo18. Despite the availability of the genome sequence, characterization of O. oeni genes is limited, and little is known about the in vivo role of Lo18. Due to the lack of genetic tools for O. oeni , an efficient expression vector in O…

0301 basic medicine[SDV.BIO]Life Sciences [q-bio]/Biotechnology[ SDV.AEN ] Life Sciences [q-bio]/Food and Nutrition030106 microbiologyLactobacillus-plantarumWineEscherichia-coliApplied Microbiology and Biotechnologymolecular characterization03 medical and health sciencesGrowth-phaseBacterial ProteinsMembrane stabilizationHeat shock protein[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]Antisense TechnologyGene expression[SDV.IDA]Life Sciences [q-bio]/Food engineeringMalolactic fermentationEnvironmental MicrobiologyRNA AntisenseGene-expressionLactic AcidHeat-Shock ProteinsOenococcusOenococcus oeniLeuconostoc-oenosEcologybiologyEthanolLactococcus lactisMalolactic fermentation[ SDV.BIO ] Life Sciences [q-bio]/BiotechnologyGene Expression Regulation Bacterialbiology.organism_classification[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/BacteriologyAntisense RNABiochemistryLactococcus-lactisHeat-shock-proteinFermentationOenococcusFood ScienceBiotechnology
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The Severity of Acute Stress Is Represented by Increased Synchronous Activity and Recruitment of Hypothalamic CRH Neurons

2016

The hypothalamo-pituitary-adrenocortical (HPA) axis regulates stress physiology and behavior. To achieve an optimally tuned adaptive response, it is critical that the magnitude of the stress response matches the severity of the threat. Corticotropin-releasing hormone (CRH) released from the paraventricular nucleus of the hypothalamus is a major regulator of the HPA axis. However, how CRH-producing neurons in an intact animal respond to different stressor intensities is currently not known. Using two-photon calcium imaging on intact larval zebrafish, we recorded the activity of CRH cells, while the larvae were exposed to stressors of varying intensity. By combining behavioral and physiologic…

0301 basic medicineendocrine systemmedicine.medical_specialtyHydrocortisoneCorticotropin-Releasing HormoneHypothalamusRegulatorMotor ActivityMembrane PotentialsAnimals Genetically Modified03 medical and health sciencesCorticotropin-releasing hormoneCalcium imagingStress PhysiologicalInternal medicineAvoidance LearningmedicineAnimalsZebrafishHeat-Shock ProteinsZebrafishHydrocortisoneNeuronsMembrane potentialbiologyGeneral NeuroscienceArticlesbiology.organism_classificationLuminescent Proteins030104 developmental biologymedicine.anatomical_structureEndocrinologyGene Expression Regulationnervous systemHypothalamusLarvaCalciumPsychologyNucleusNeurosciencehormones hormone substitutes and hormone antagonistsmedicine.drugThe Journal of Neuroscience
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Heat Shock Proteins in Alzheimer’s Disease: Role and Targeting

2018

Among diseases whose cure is still far from being discovered, Alzheimer’s disease (AD) has been recognized as a crucial medical and social problem. A major issue in AD research is represented by the complexity of involved biochemical pathways, including the nature of protein misfolding, which results in the production of toxic species. Considering the involvement of (mis)folding processes in AD aetiology, targeting molecular chaperones represents a promising therapeutic perspective. This review analyses the connection between AD and molecular chaperones, with particular attention toward the most important heat shock proteins (HSPs) as representative components of the human chaperome: Hsp60,…

0301 basic medicineheat shock proteinDiseaseReviewprotein TauHsp70lcsh:ChemistrychaperoneEnzyme Inhibitorslcsh:QH301-705.5SpectroscopybiologyGeneral MedicineHsp60Hsp90Computer Science Applicationsamyloid peptideModels AnimalHSP60Protein foldingAlzheimer’s diseaseheat shock proteins; chaperones; Alzheimer’s disease; amyloid peptide; protein Tau; Hsp60; Hsp70; Hsp90Tau proteintau ProteinsHsp90Computational biologyCatalysisInorganic ChemistryMitochondrial Proteins03 medical and health sciencesAlzheimer DiseaseHeat shock proteinAnimalsHumanschaperonesHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsPhysical and Theoretical ChemistryMolecular BiologyAmyloid beta-PeptidesSettore BIO/16 - Anatomia UmanaOrganic ChemistryChaperonin 60Settore CHIM/06 - Chimica OrganicaHsp70030104 developmental biologylcsh:Biology (General)lcsh:QD1-999heat shock proteinsbiology.protein
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Inhibition of cell migration and induction of apoptosis by a novel class II histone deacetylase inhibitor, MCC2344.

2020

Epigenetic modifiers provide a new target for the development of anti-cancer drugs. The eraser histone deacetylase 6 (HDAC6) is a class IIb histone deacetylase that targets various non-histone proteins such as transcription factors, nuclear receptors, cytoskeletal proteins, DNA repair proteins, and molecular chaperones. Therefore, it became an attractive target for cancer treatment. In this study, virtual screening was applied to the MicroCombiChem database with 1162 drug-like compounds to identify new HDAC6 inhibitors. Five compounds were tested in silico and in vitro as HDAC6 inhibitors. Both analyses revealed 1-cyclohexene-1-carboxamide, 2-hydroxy-4,4-dimethyl-N-1-naphthalenyl-6-oxo- (MC…

0301 basic medicinemedicine.drug_classDNA repairAntineoplastic AgentsApoptosisHistone Deacetylase 6MicrotubulesEpigenesis Genetic03 medical and health sciences0302 clinical medicineCell MovementTubulinNeoplasmsCyclohexenesmedicineAnimalsHumansNeoplasm InvasivenessEpigeneticsHSP90 Heat-Shock ProteinsTranscription factorZebrafishPharmacologyChemistryHistone deacetylase inhibitorCell migrationAcetylationHDAC6Xenograft Model Antitumor AssaysCell biologyHistone Deacetylase Inhibitors030104 developmental biologyCell culture030220 oncology & carcinogenesisMCF-7 CellsHistone deacetylaseApoptosis Regulatory ProteinsPharmacological research
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Autoantibodies in Spondyloarthritis, Focusing on Anti-CD74 Antibodies

2019

Spondyloarthritis (SpA) is an inflammatory rheumatic disease with diverse clinical presentation. The diagnosis of SpA remains a big challenge in daily clinical practice because of the limitation in specific biomarkers of SpA, more biomarkers are still needed for SpA diagnosis and disease activity monitoring. In the past, SpA was considered predominantly as auto-inflammatory disease vs. autoimmune disease. However, in recent years several researches demonstrated a broad autoantibody response in SpA patients. Study also indicated that mice lack of ZAP70 in T cell develop SpA featured inflammation. These studies indicated the autoimmune features of SpA and gave rise to the potential use of aut…

0301 basic medicinemusculoskeletal diseaseslcsh:Immunologic diseases. AllergyCD74autoantibodiesdiagnosisImmunologyAutoimmunityDiseaseAutoantigensAutoimmune DiseasesPathogenesis03 medical and health sciences0302 clinical medicineHypothesis and TheorySpondylarthritismedicineImmunology and AllergyHumansHeat-Shock ProteinsAutoimmune diseasebiologybusiness.industryChinese patientsAutoantibodyHistocompatibility Antigens Class IIspondyloarthritismedicine.diseaseClinical PracticeAntigens Differentiation B-LymphocyteProtein Phosphatase 2Cstomatognathic diseases030104 developmental biology14-3-3 ProteinsROC CurveImmunologybiology.proteinBiomarker (medicine)Antibodybusinessbeta 2-Microglobulinlcsh:RC581-607Biomarkers030215 immunologyanti-CD74 autoantibodyFrontiers in Immunology
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Pterostilbene in Cancer Therapy.

2021

Natural polyphenols are organic chemicals which contain phenol units in their structures and possess antitumor properties. However, a key problem is their short half-life and low bioavailability under in vivo conditions. Pterostilbene (3,5-dimethoxy-4′-hydroxystilbene; PT) is a phytoalexin originally isolated from the heartwood of red sandalwood. As recently reported by our group, PT was shown to be effective in the treatment of melanoma. Counterintuitively, PT is not effective (cytotoxic) against melanoma in vitro, and only under in vivo conditions does PT display its anticancer activity. This study elucidated that PT can be effective against melanoma through the inhibition of adrenocortic…

0301 basic medicinepterostilbenePterostilbenePhysiologymedicine.medical_treatmentClinical BiochemistryReviewPharmacologystilbenesBiochemistry03 medical and health scienceschemistry.chemical_compound0302 clinical medicineIn vivomedicinecanceroxidative stressMolecular BiologySensitizationpolyphenolsChemistryMelanomaheat-shock proteinslcsh:RM1-950CancerCell Biologymedicine.diseaseBioavailability030104 developmental biologymedicine.anatomical_structurelcsh:Therapeutics. Pharmacology030220 oncology & carcinogenesisCancer cellAdjuvantAntioxidants (Basel, Switzerland)
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Genomic organization and promoter characterization of the gene encoding a putative endoplasmic reticulum chaperone, ERp29

2002

Abstract ERp29 is a soluble protein localized in the endoplasmic reticulum (ER) of eukaryotic cells, which is conserved in all mammalian species. The N-terminal domain of ERp29 displays sequence and structural similarity to the protein disulfide isomerase despite the lack of the characteristic double cysteine motif. Although the exact function of ERp29 is not yet known, it was hypothesized that it may facilitate folding and/or export of secretory proteins in/from the ER. ERp29 is induced by ER stress, i.e. accumulation of unfolded proteins in the ER. To gain an insight into the mechanisms regulating ERp29 expression we have cloned and characterized the rat ERp29 gene and studied in details …

5' Flanking RegionRecombinant Fusion ProteinsMolecular Sequence DataCHO CellsBiologyCell LineMiceCricetinaeSequence Homology Nucleic AcidGene expressionTumor Cells CulturedGeneticsAnimalsHumansRNA MessengerLuciferasesPromoter Regions GeneticProtein disulfide-isomeraseGeneHeat-Shock ProteinsPhylogenyBase SequenceGene Expression ProfilingEndoplasmic reticulumPromoter3T3 CellsDNAExonsSequence Analysis DNAGeneral MedicineMolecular biologyIntronsRatsHousekeeping geneSecretory proteinGenesUnfolded protein responseFemaleTranscription Initiation SiteSequence AlignmentHeLa CellsGene
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