Search results for " Heat"

showing 10 items of 830 documents

Brief Report: Functional Interaction of Endoplasmic Reticulum Aminopeptidase 2 and HLA-B27 Activates the Unfolded Protein Response.

2017

Objective: The basic mechanisms underlying the pathogenesis of ankylosing spondylitis (AS) remain unresolved. We previously reported an association of the single-nucleotide polymorphism (SNP) rs2549782 in the endoplasmic reticulum aminopeptidase 2 gene (ERAP2) with AS. It is known that patients homozygous for the G allele (GG) of another ERAP2 SNP, rs2248374, lack expression of ERAP2 (ERAP2 null). The present study utilized this information to study the impact of ERAP2 deficiency on HLA–B27 expression in patients with AS, specifically focusing on the functional interaction of ERAP2 and HLA–B27 in peripheral blood mononuclear cells (PBMCs) from patients with AS and assessing the effects …

0301 basic medicineMaleX-Box Binding Protein 1Aminopeptidases0302 clinical medicineImmunology and AllergyRNA Small InterferingEndoplasmic Reticulum Chaperone BiPHLA-B27 AntigenHeat-Shock ProteinsAlleleBlottingReverse Transcriptase Polymerase Chain ReactionHeat-Shock ProteinSingle NucleotideMiddle AgedFlow CytometryCCAAT-Enhancer-Binding Protein3. Good healthUp-RegulationFemaleWesternHumanAnkylosingAdultAminopeptidaseMononuclearImmunologyBlotting WesternSingle-nucleotide polymorphismBiologyMajor histocompatibility complexSmall InterferingPolymorphism Single NucleotideAdult; Alleles; Aminopeptidases; Blotting Western; CCAAT-Enhancer-Binding Proteins; Cell Line; Female; Flow Cytometry; HLA-B27 Antigen; Heat-Shock Proteins; Humans; Leukocytes Mononuclear; Male; Middle Aged; Polymorphism Single Nucleotide; RNA Small Interfering; Reverse Transcriptase Polymerase Chain Reaction; Spondylitis Ankylosing; Unfolded Protein Response; Up-Regulation; X-Box Binding Protein 1; Immunology and Allergy; Rheumatology; ImmunologyCell Line03 medical and health sciencesDownregulation and upregulationRheumatologyHumansSpondylitis AnkylosingAllelePolymorphismAlleles030203 arthritis & rheumatologySpondylitiHLA-B27LeukocyteEndoplasmic reticulum aminopeptidase 2X-Box Binding Protein 1Molecular biologySettore MED/16 - Reumatologia030104 developmental biologyUnfolded protein responsebiology.proteinCCAAT-Enhancer-Binding ProteinsLeukocytes MononuclearUnfolded Protein ResponseRNAArthritisrheumatology (Hoboken, N.J.)
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HSP110 T17 simplifies and improves the microsatellite instability testing in patients with colorectal cancer

2016

IF 5.65; International audience; Background Every colorectal cancer (CRC) patient should be tested for microsatellite instability (MSI, a marker for defective DNA mismatch repair) as a first screen for Lynch syndrome (LS). In this study, we investigated whether it may be possible to improve the detection of MSI in CRC. We examined whether the HT17 DNA repeat (critical for correct splicing of the chaperone HSP110) might constitute a superior marker for diagnosis of the MSI phenotype in patients with CRC compared with the standard panel of markers (pentaplex).Methods The HT17 polymorphism was analysed in germline DNA from 1037 multi-ethnic individuals. We assessed its sensitivity and specific…

0301 basic medicineOncologymedicine.medical_specialtyGenotypeColorectal cancerPopulationMismatch RepairBiologyGuidelinesBioinformaticsDNA Mismatch RepairColon-Cancer03 medical and health sciences0302 clinical medicineMolecular geneticsInternal medicineDiagnostic-TestsGenotypeGeneticsmedicineBiomarkers TumorHumansChemotherapyHSP110 Heat-Shock Proteinseducation[ SDV.GEN.GH ] Life Sciences [q-bio]/Genetics/Human geneticsGenotypingneoplasmsGenetics (clinical)Tumorseducation.field_of_studyPentaplex PcrMicrosatellite instabilityDNAmedicine.diseaseColorectal Neoplasms Hereditary NonpolyposisLynch syndromedigestive system diseases3. Good healthMononucleotide Repeats030104 developmental biology[SDV.GEN.GH]Life Sciences [q-bio]/Genetics/Human genetics030220 oncology & carcinogenesisDNA mismatch repairMicrosatellite InstabilityLynch-SyndromeColorectal NeoplasmsMutations
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Innovative technologies for food preservation

2018

Abstract Several techniques have been developed during the 20th century in order to preserve foods. These innovative technologies vary considerably and embrace physical technologies (e.g., high hydrostatic pressure and high-pressure homogenization), electromagnetic technologies (e.g., pulsed electric fields, ohmic heating, microwaves, radio-frequency, and UV-light), acoustic technologies (e.g., ultrasound and shockwaves), and others such as membrane filtration and dense phase CO 2 . In this chapter, the theoretical background and definition of the technologies are explained together with a description of the equipment, main technological/processing parameters, and some advantages and limita…

0301 basic medicineOther Engineering and Technologies030109 nutrition & dieteticsMaterials sciencebusiness.industryHydrostatic pressureMechanical engineeringHigh-pressure homogenization04 agricultural and veterinary sciences040401 food scienceElectromagnetic03 medical and health sciences0404 agricultural biotechnologyHigh pressure homogenizationHigh hydrostatic pressureOhmic heatingUltrasoundDense phaseEngineering and TechnologyProcess engineeringbusinessPulsed electric fieldsMicrowavesMembrane filtration
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Chaperoning the Mononegavirales: Current Knowledge and Future Directions

2018

This article belongs to the Special Issue Breakthroughs in Viral Replication.

0301 basic medicineProtein Foldingrespiratory syncytial viruslcsh:QR1-502ReviewRespiratory syncytial virusVirus Replicationmedicine.disease_causelcsh:MicrobiologyHsp70Ebola virusantiviralsChaperonesMononegaviralesOrder MononegaviralesbiologyAntivirals<i>Mononegavirales</i>Hsp90Respiratory Syncytial VirusesInfectious DiseasesMumps virusHost-Pathogen InteractionsProtein foldingHsp90biology_otherComputational biologyAntiviral Agents03 medical and health sciencesEmerging infectionsVirologymedicineHumanschaperonesHSP70 Heat-Shock Proteinsrabies virusHSP90 Heat-Shock ProteinsEbola virusObligatebiology.organism_classificationCCT030104 developmental biologyMeasles virusRabies virusChaperone (protein)measles virusbiology.proteinmumps virusMononegaviralesMolecular ChaperonesViruses
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Breaking BAG: The Co-Chaperone BAG3 in Health and Disease.

2016

Human BAG ( B cl-2-associated a thano g ene) proteins form a family of antiapoptotic proteins that currently consists of six members (BAG1–6) all sharing the BAG protein domain from which the name arises. Via this domain, BAG proteins bind to the heat shock protein 70 (Hsp70), thereby acting as a co-chaperone regulating the activity of Hsp70. In addition to their antiapoptotic activity, all human BAG proteins have distinct functions in health and disease, and BAG3 in particular is the focus of many investigations. BAG3 has a modular protein domain composition offering the possibility for manifold interactions with other proteins. Various BAG3 functions are implicated in disorders including …

0301 basic medicineProtein domainCellular homeostasisBiologyToxicologyBAG303 medical and health sciencesMuscular DiseasesNeoplasmsmedicineAutophagyAnimalsHumansHSP70 Heat-Shock ProteinsAdaptor Proteins Signal TransducingPharmacologyAutophagyNeurodegenerationNeurodegenerative Diseasesmedicine.diseaseCell biologyHsp70Co-chaperone030104 developmental biologyProteasomeApoptosis Regulatory ProteinsTrends in pharmacological sciences
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Heat shock protein-90 toward theranostics: a breath of fresh air in idiopathic pulmonary fibrosis.

2017

Heat shock proteins are potential biomarkers and therapeutic targets in idiopathic pulmonary fibrosis http://ow.ly/fHVP30hJUOl

0301 basic medicinePulmonary and Respiratory MedicinePathologymedicine.medical_specialtyTheranostic NanomedicinePulmonary FibrosisRespiratory SystemHSP90 Heat-Shock ProteinsTheranostic Nanomedicine03 medical and health sciencesIdiopathic pulmonary fibrosisFresh airHeat shock proteinPulmonary fibrosisMedicineHumansHSP90 Heat-Shock ProteinsRespiratory systemMyofibroblastsHeat-Shock Proteinsbusiness.industrymedicine.diseaseIdiopathic Pulmonary Fibrosis030104 developmental biologyPotential biomarkersbusinessThe European respiratory journal
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BAG2 Interferes with CHIP-Mediated Ubiquitination of HSP72

2016

The maintenance of cellular proteostasis is dependent on molecular chaperones and protein degradation pathways. Chaperones facilitate protein folding, maturation, and degradation, and the particular fate of a misfolded protein is determined by the interaction of chaperones with co-chaperones. The co-factor CHIP (C-terminus of HSP70-inteacting protein, STUB1) ubiquitinates chaperone substrates and directs proteins to the cellular degradation systems. The activity of CHIP is regulated by two co-chaperones, BAG2 and HSPBP1, which are potent inhibitors of the E3 ubiquitin ligase activity. Here, we examined the functional correlation of HSP72, CHIP, and BAG2, employing human primary fibroblasts.…

0301 basic medicineTime FactorsUbiquitin-Protein LigasesImmunoblottingHSP72 Heat-Shock ProteinsUbiquitin-conjugating enzymeProtein degradationArticleCatalysisCell Linelcsh:ChemistryInorganic Chemistry03 medical and health sciencesUbiquitinddc:570Humansaging; BAG2; CHIP; HSP72; proteostasis; ubiquitinationPhysical and Theoretical ChemistryHSP72lcsh:QH301-705.5Molecular BiologyCellular SenescenceSpectroscopySTUB1proteostasisBAG2biologyCHIPagingOrganic ChemistryUbiquitinationGeneral MedicineComputer Science ApplicationsUbiquitin ligaseCell biology030104 developmental biologyProteostasislcsh:Biology (General)lcsh:QD1-999Chaperone (protein)biology.proteinRNA InterferenceProtein foldingMolecular ChaperonesInternational Journal of Molecular Sciences
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Heat shock protein 70 dampens the inflammatory response of human PDL cells to mechanical loading in vitro

2019

BACKGROUND AND OBJECTIVE Previously, we demonstrated an inflammatory response of human PDL (hPDL) cells to mechanical loading. The cellular reaction was dampened by heat pre-treatment suggesting a protective role for heat shock proteins (HSP) during stress-induced ischemia. Here we explored if HSP70, which has already been documented in the pressure zone of tooth movement, might be regulatorily involved in the attenuation of the inflammatory response. MATERIALS AND METHODS Fifth passage hPDL cells were mechanically loaded in the presence of the HSP70 inhibitor VER155008. Cell morphology, HSP70 expression, viability, IL-6 and IL-8 expression were determined by means of microscopy, realtime-P…

0301 basic medicineTooth Movement TechniquesPeriodontal LigamentInflammatory responseIschemiaOsteoclastsCell morphology03 medical and health sciences0302 clinical medicineHeat shock proteinmedicineHumansHSP70 Heat-Shock ProteinsCells CulturedInflammationChemistry030206 dentistryAdhesionmedicine.diseaseIn vitroHsp70Cell biologyCell stress030104 developmental biologyPeriodonticsStress MechanicalJournal of Periodontal Research
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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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