Search results for "HEAT-SHOCK PROTEINS"

showing 10 items of 310 documents

Human molecular chaperones share with SARS-CoV-2 antigenic epitopes potentially capable of eliciting autoimmunity against endothelial cells: possible…

2020

Severe acute respiratory syndrome corona virus 2 (SARS-CoV-2), the cause of COVID-19 disease, has the potential to elicit autoimmunity because mimicry of human molecular chaperones by viral proteins. We compared viral proteins with human molecular chaperones, many of which are heat shock proteins, to determine if they share amino acid-sequence segments with immunogenic-antigenic potential, which can elicit cross-reactive antibodies and effector immune cells with the capacity to damage-destroy human cells by a mechanism of autoimmunity. We identified the chaperones that can putatively participate in molecular mimicry phenomena after SARS-CoV-2 infection, focusing on those for which endotheli…

0301 basic medicineMolecular chaperonesShort CommunicationPneumonia ViralAutoimmunityBiologymedicine.disease_causeAutoantigensBiochemistryEpitopeAutoimmunity03 medical and health sciencesBetacoronavirusViral Proteins0302 clinical medicineImmune systemEndothelialitisAntigenHeat shock proteinmedicineHumansSevere acute respiratory syndrome coronavirus 2Amino Acid SequenceDatabases ProteinPandemicsHeat-Shock ProteinsEffectorImmunodominant EpitopesSARS-CoV-2Settore BIO/16 - Anatomia UmanaEndothelial CellsCOVID-19Cell BiologyCell biologyEndothelial stem cellMolecular mimicry030104 developmental biologyCoronavirus Infections030217 neurology & neurosurgeryMolecular mimicryCell Stress and Chaperones
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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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Activin Receptor Ligand Blocking and Cancer Have Distinct Effects on Protein and Redox Homeostasis in Skeletal Muscle and Liver

2019

Muscle wasting in cancer cachexia can be alleviated by blocking activin receptor type 2 (ACVR2) ligands through changes in protein synthesis/degradation. These changes in cellular and protein metabolism may alter protein homeostasis. First, we elucidated the acute (1–2 days) and 2-week effects of blocking ACVR2 ligands by soluble activin receptor 2B (sACVR2B-Fc) on unfolded protein response (UPR), heat shock proteins (HSPs) and redox balance in a healthy mouse skeletal muscle. Second, we examined UPR, autophagy and redox balance with or without sACVR2B-Fc administration in muscle and liver of C26 tumor-bearing mice. The indicators of UPR and HSPs were not altered 1–2 days after a single sAC…

0301 basic medicinePhysiologyProtein metabolismlihaksetMyostatinlcsh:PhysiologyMuscle hypertrophyACTIVATIONchemistry.chemical_compound0302 clinical medicineENDOPLASMIC-RETICULUM STRESSCACHEXIAglutathioneta315Original ResearchIIB RECEPTORbiologylcsh:QP1-981Chemistry1184 Genetics developmental biology physiologyactivinActivin receptorMOUSE MODELunfolded protein response3. Good healthmedicine.anatomical_structure030220 oncology & carcinogenesismyostatinsyöpätauditautofagiacancer cachexiamedicine.medical_specialtyendocrine systemautophagyoxidative stress/redoxta3111liverCachexia03 medical and health sciencesPhysiology (medical)Internal medicinemedicineHEAT-SHOCK PROTEINSskeletal muscleglutationioksidatiivinen stressiECCENTRIC EXERCISEmaksaSkeletal muscleGlutathionemedicine.diseaseMUSCULAR-DYSTROPHY030104 developmental biologyEndocrinologybiology.proteinOXIDATIVE DAMAGE3111 BiomedicineproteiinitlihassurkastumasairaudetACVR2BFrontiers in Physiology
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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: a hot topic in idiopathic pulmonary fibrosis

2017

HSP90 inhibition could be an exciting new treatment strategy for IPF http://ow.ly/HfKY306uvxw

0301 basic medicinePulmonary and Respiratory MedicinePathologymedicine.medical_specialtyPulmonary Fibrosis03 medical and health sciencesIdiopathic pulmonary fibrosis0302 clinical medicineHeat shock proteinPulmonary fibrosismedicineHumansHeat-Shock Proteinsbiologybusiness.industrymedicine.diseaseImmunohistochemistryHsp90Idiopathic Pulmonary Fibrosis030104 developmental biology030228 respiratory systemImmunologybiology.proteinImmunohistochemistryTreatment strategybusinessEuropean Respiratory Journal
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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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Effects of muscular dystrophy, exercise and blocking activin receptor IIB ligands on the unfolded protein response and oxidative stress

2016

Protein homeostasis in cells, proteostasis, is maintained through several integrated processes and pathways and its dysregulation may mediate pathology in many diseases including Duchenne muscular dystrophy (DMD). Oxidative stress, heat shock proteins, endoplasmic reticulum (ER) stress and its response, i.e. unfolded protein response (UPR), play key roles in proteostasis but their involvement in the pathology of DMD are largely unknown. Moreover, exercise and activin receptor IIB blocking are two strategies that may be beneficial to DMD muscle, but studies to examine their effects on these proteostasis pathways are lacking. Therefore, these pathways were examined in the muscle of mdx mice, …

0301 basic medicineX-Box Binding Protein 1Activin Receptors Type IIEukaryotic Initiation Factor-2MyostatinUPRBiochemistryMiceeIF-2 KinaseThioredoxinsSirtuin 1ENDOPLASMIC-RETICULUM STRESSDISULFIDE-ISOMERASEPhosphorylationta315Endoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsIN-VIVOta3141Activin receptorMOUSE MODELER STRESSEndoplasmic Reticulum Stress3. Good healthmedicine.anatomical_structuremyostatinPRESERVES MUSCLE FUNCTIONER-stressSKELETAL-MUSCLEmdxSignal TransductionEXPRESSIONmedicine.medical_specialtyXBP1MDX MICEBiologyProtein Serine-Threonine Kinases03 medical and health sciencesPhysiology (medical)Internal medicineHeat shock proteinPhysical Conditioning AnimalEndoribonucleasesmedicineAnimalsHumansRNA MessengerMuscle SkeletalSkeletal muscleMyostatinGENEActivating Transcription Factor 6Immunoglobulin Fc FragmentsMuscular Dystrophy DuchenneDisease Models Animal030104 developmental biologyProteostasisEndocrinologyGene Expression RegulationUnfolded protein responsebiology.proteinMice Inbred mdxProteostasisUnfolded Protein Response3111 BiomedicineCarrier ProteinsACVR2B
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