Search results for "chaperone"

showing 10 items of 249 documents

Does Metformin Modulate Endoplasmic Reticulum Stress and Autophagy in Type 2 Diabetic Peripheral Blood Mononuclear Cells?

2018

Since type 2 diabetes (T2D) is associated with oxidative stress and metformin has been shown to exert a protective role against the said stress, we wondered whether metformin treatment might also modulate endoplasmic reticulum (ER) stress and autophagy in leukocytes of T2D patients. We studied 53 T2D patients (37 of whom had been treated with metformin 1700 mg for at least 1 year) and 30 healthy volunteers. Leukocytes from both groups of T2D patients exhibited increased protein levels of 78-kDa glucose-regulated protein (GRP78) with respect to controls, whereas activating transcription factor 6 (ATF6) was enhanced specifically in nonmetformin-treated T2D, and (s-xbp1) and phosphorylated euk…

Male0301 basic medicinemedicine.medical_specialtyendocrine system diseasesPhysiologyClinical BiochemistryAdministration OralType 2 diabetesBiologymedicine.disease_causeBiochemistry03 medical and health sciencesInternal medicineAutophagymedicineHumansEndoplasmic Reticulum Chaperone BiPMolecular BiologyGeneral Environmental ScienceDose-Response Relationship DrugATF6Endoplasmic reticulumAutophagynutritional and metabolic diseasesCell BiologyBECN1Middle AgedEndoplasmic Reticulum Stressmedicine.diseaseMetforminMetforminOxidative StressCross-Sectional Studies030104 developmental biologyEndocrinologyDiabetes Mellitus Type 2Leukocytes MononuclearUnfolded protein responseGeneral Earth and Planetary SciencesFemaleOxidative stressmedicine.drugAntioxidants & Redox Signaling
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Chaperone patterns in vernal keratoconjunctivitis are distinctive of cell and Hsp type and are modified by inflammatory stimuli

2016

Background Vernal keratoconjunctivitis (VKC) is a severe ocular allergy with pathogenic mechanism poorly understood and no efficacious treatment. The aims of the study were to determine quantities and distribution of Hsp chaperones in the conjunctiva of VKC patients and assess their levels in conjunctival epithelial and fibroblast cultures exposed to inflammatory stimuli. Methods Hsp10, Hsp27, Hsp40, Hsp60, Hsp70, Hsp90, Hsp105, and Hsp110 were determined in conjunctiva biopsies from nine patients and nine healthy age-matched normal subjects, using immunomorphology and qPCR. Conjunctival epithelial cells and fibroblasts were cultured and stimulated with IL-1β, histamine, IL-4, TNF-α, or UV-…

Male0301 basic medicinequantitative Hsp patternschemistry.chemical_compoundChaperonesHspchaperoneImmunology and AllergyChildCells CulturedHeat-Shock ProteinsConjunctivitis AllergicCulturedbiologyCD68conjunctival cells Hspconjunctival cellsImmunohistochemistrychaperones; conjunctival cells Hsp; quantitative Hsp patterns; vernal keratoconjunctivitis; Immunology; Immunology and Allergymedicine.anatomical_structureFemaleHistaminequantitative Hsp patternConjunctivaAdolescentCellsImmunologyTryptasevernal keratoconjunctivitiNO03 medical and health sciencesAllergicImmune systemHsp27Heat shock proteinmedicineHumansvernal keratoconjunctivitischaperones; conjunctival cells Hsp; quantitative Hsp patterns; vernal keratoconjunctivitis; Adolescent; Cells Cultured; Child; Conjunctivitis Allergic; Epithelial Cells; Female; Fibroblasts; Heat-Shock Proteins; Humans; Immunohistochemistry; Male; Molecular Chaperones; Immunology and Allergy; ImmunologyEpithelial CellsFibroblastsConjunctivitismedicine.diseaseeye diseases030104 developmental biologychemistryImmunologybiology.proteinChaperones; conjunctival cells Hsp; quantitative Hsp patterns; vernal keratoconjunctivitisVernal keratoconjunctivitisMolecular Chaperones
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The expression of HSP27 is associated with poor clinical outcome in intrahepatic cholangiocarcinoma.

2007

Abstract Background The heat shock proteins (HSPs) 27-kDa (HSP27) and 72-kDa (HSP72), are ubiquitous chaperone molecules inducible in cells exposed to different stress conditions. Increased level of HSPs are reported in several human cancers, and found to be associated with the resistance to some anticancer treatments and poor prognosis. However, there is no study of the relationship between HSPs expression and patient's prognosis in intrahepatic cholangiocarcinoma (IHCCA). In this exploratory retrospective study, we investigated the expressions of HSP27 and HSP72 as potential prognostic factors in IHCCA. Methods Thirty-one paraffin-embedded samples were analyzed by immunohistochemical meth…

MaleCancer ResearchHSP27 Heat-Shock ProteinsMitosisHSP72 Heat-Shock ProteinsBile Duct Neoplasmlcsh:RC254-282CholangiocarcinomaImmunoenzyme TechniquesNecrosisLymphocytes Tumor-InfiltratingHsp27Surgical oncologyHeat shock proteinGeneticsBiomarkers TumorMedicineHumansNeoplasm InvasivenessSurvival rateIntrahepatic CholangiocarcinomaHeat-Shock ProteinsAgedCell ProliferationRetrospective Studiesbiologybusiness.industryRetrospective cohort studyMiddle Agedlcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogensPrognosisNeoplasm ProteinsSurvival RateBile Ducts IntrahepaticOncologyBile Duct NeoplasmsImmunologybiology.proteinCancer researchFemaleStem cellbusinessMolecular ChaperonesResearch ArticleBMC cancer
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Castration-Induced Downregulation of SPARC in Stromal Cells Drives Neuroendocrine Differentiation of Prostate Cancer.

2021

Abstract Fatal neuroendocrine differentiation (NED) of castration-resistant prostate cancer is a recurrent mechanism of resistance to androgen deprivation therapies (ADT) and antiandrogen receptor pathway inhibitors (ARPI) in patients. The design of effective therapies for neuroendocrine prostate cancer (NEPC) is complicated by limited knowledge of the molecular mechanisms governing NED. The paucity of acquired genomic alterations and the deregulation of epigenetic and transcription factors suggest a potential contribution from the microenvironment. In this context, whether ADT/ARPI induces stromal cells to release NED-promoting molecules and the underlying molecular networks are unestablis…

MaleCancer ResearchStromal cellAnimals Biomarkers Tumor Cell Differentiation Cell Line Tumor Coculture Techniques Endoplasmic Reticulum Chaperone BiP Epigenesis Genetic Gene Expression Regulation Neoplastic Humans Male Mice Mice Inbred C57BL Neuroendocrine Cells Osteonectin Prostatic Neoplasms Stromal Cells Transgenes Tumor Microenvironment Down-RegulationDown-RegulationContext (language use)Settore MED/08 - Anatomia PatologicaNeuroendocrine differentiationEpigenesis GeneticProstate cancerMiceStromaDownregulation and upregulationNeuroendocrine CellsCell Line TumormedicineBiomarkers TumorTumor MicroenvironmentSettore MED/05 - Patologia ClinicaAnimalsHumansOsteonectinEpigeneticsTransgenesEndoplasmic Reticulum Chaperone BiPbusiness.industryMatricellular proteinProstatic NeoplasmsCell Differentiationmedicine.diseaseCoculture TechniquesGene Expression Regulation NeoplasticMice Inbred C57BLOncologyCancer researchStromal CellsbusinessCancer research
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X-linked primary ciliary dyskinesia due to mutations in the cytoplasmic axonemal dynein assembly factor PIH1D3

2017

By moving essential body fluids and molecules, motile cilia and flagella govern respiratory mucociliary clearance, laterality determination and the transport of gametes and cerebrospinal fluid. Primary ciliary dyskinesia (PCD) is an autosomal recessive disorder frequently caused by non-assembly of dynein arm motors into cilia and flagella axonemes. Before their import into cilia and flagella, multi-subunit axonemal dynein arms are thought to be stabilized and pre-assembled in the cytoplasm through a DNAAF2–DNAAF4–HSP90 complex akin to the HSP90 co-chaperone R2TP complex. Here, we demonstrate that large genomic deletions as well as point mutations involving PIH1D3 are responsible for an X-li…

MaleCytoplasmProtein FoldingAxoneme[SDV]Life Sciences [q-bio][SDV.GEN] Life Sciences [q-bio]/Genetics[SDV.MHEP.PSR]Life Sciences [q-bio]/Human health and pathology/Pulmonology and respiratory tractouterGenes X-LinkedChilddefectsPhylogenyZebrafisharmsSequence DeletionvariantsIntracellular Signaling Peptides and ProteinsGenetic Diseases X-LinkedPedigreeMultidisciplinary Sciences[SDV] Life Sciences [q-bio]motilityChild PreschoolMicrotubule ProteinsSperm MotilityScience & Technology - Other TopicsFemaleAdultAdolescentinnerUK10K Rare Groupr2tp complexof-function mutationsArticleMicroscopy Electron TransmissionMD MultidisciplinaryExome SequencingAnimalsHumansPoint MutationCiliaHSP90 Heat-Shock Proteins[SDV.GEN]Life Sciences [q-bio]/GeneticsScience & TechnologyKartagener SyndromeInfant NewbornAxonemal DyneinsDisease Models AnimalHEK293 Cells[SDV.MHEP.PSR] Life Sciences [q-bio]/Human health and pathology/Pulmonology and respiratory tractidentifies mutationsproteinApoptosis Regulatory ProteinsSequence AlignmentMolecular ChaperonesNature Communications
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Defective nuclear localization of Hsp70 is associated with dyserythropoiesis and GATA-1 cleavage in myelodysplastic syndromes.

2012

Abstract Normal human erythroid cell maturation requests the transcription factor GATA-1 and a transient activation of caspase-3, with GATA-1 being protected from caspase-3–mediated cleavage by interaction with the chaperone heat shock protein 70 (Hsp70) in the nucleus. Erythroid cell dysplasia observed in early myelodysplastic syndromes (MDS) involves impairment of differentiation and excess of apoptosis with a burst of caspase activation. Analysis of gene expression in MDS erythroblasts obtained by ex vivo cultures demonstrates the down-regulation of a set of GATA-1 transcriptional target genes, including GYPA that encodes glycophorin A (GPA), and the up-regulation of members of the HSP70…

MaleErythroblasts[SDV]Life Sciences [q-bio]Biochemistry0302 clinical medicineTranscription (biology)hemic and lymphatic diseasesGene expressionErythropoiesisGATA1 Transcription FactorCells CulturedCaspaseComputingMilieux_MISCELLANEOUSOligonucleotide Array Sequence AnalysisAged 80 and over0303 health sciencesbiologyCaspase 3Reverse Transcriptase Polymerase Chain ReactionCell DifferentiationU937 CellsHematologyMiddle Agedmedicine.anatomical_structure030220 oncology & carcinogenesisFemaleAdultGreen Fluorescent ProteinsImmunoblottingImmunology03 medical and health sciencesErythroid CellsmedicineHumansHSP70 Heat-Shock ProteinsTranscription factorAged030304 developmental biologyCell NucleusGene Expression ProfilingCell BiologyMolecular biologyCell nucleusMicroscopy FluorescenceApoptosisMyelodysplastic SyndromesChaperone (protein)Mutationbiology.proteinNuclear localization sequence
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Convergent sets of data from in vivo and in vitro methods point to an active role of Hsp60 in chronic obstructive pulmonary disease pathogenesis.

2011

BackgroundIt is increasingly clear that some heat shock proteins (Hsps) play a role in inflammation. Here, we report results showing participation of Hsp60 in the pathogenesis of chronic obstructive pulmonary diseases (COPD), as indicated by data from both in vivo and in vitro analyses.Methods and resultsBronchial biopsies from patients with stable COPD, smoker controls with normal lung function, and non-smoker controls were studied. We quantified by immunohistochemistry levels of Hsp10, Hsp27, Hsp40, Hsp60, Hsp70, Hsp90, and HSF-1, along with levels of inflammatory markers. Hsp10, Hsp40, and Hsp60 were increased during progression of disease. We found also a positive correlation between th…

MaleSTRESSPulmonologyChronic Obstructive Pulmonary DiseasesNeutrophilsBiopsyGene ExpressionCD8-Positive T-Lymphocytesmedicine.disease_causeBiochemistryEpitheliumPulmonary function testingPathogenesisACTIVATIONPulmonary Disease Chronic ObstructiveMolecular Cell BiologyLungCOPDMultidisciplinaryReverse Transcriptase Polymerase Chain ReactionCOPD Hsp60QRCOPD heat shock proteins inflammationMiddle AgedImmunohistochemistrymedicine.anatomical_structureEXPERIMENTAL AUTOIMMUNE ENCEPHALOMYELITISMedicineFemalemedicine.symptomInflammation MediatorsSPINAL-CORDResearch ArticleEXPRESSIONanimal structuresCOPD; heat shock proteins; inflammationScienceImmunologyMolecular Sequence DataInflammationBronchichemical and pharmacologic phenomenaHEAT-SHOCK-PROTEIN EXPERIMENTAL AUTOIMMUNE ENCEPHALOMYELITIS ACUTE LUNG INJURY SPINAL-CORD CELL-DEATH KAPPA-B HEAT-SHOCK-PROTEIN-60 STRESS EXPRESSION ACTIVATIONKAPPA-BBiologyHEAT-SHOCK-PROTEINMicrobiologycomplex mixturesCell LineACUTE LUNG INJURYMolecular GeneticsIn vivoStress PhysiologicalHeat shock proteinmedicineGeneticsHumansCOPDRNA MessengerBiologyAgedLungMucous MembraneBase SequenceSettore BIO/16 - Anatomia UmanaMacrophagesfungiImmunityTranscription Factor RelAProteinsComputational BiologyChaperonin 60medicine.diseaseChaperone Proteinsrespiratory tract diseasesGene Expression RegulationCELL-DEATHHEAT-SHOCK-PROTEIN-60inflammationImmunologyheat shock proteinsClinical ImmunologyOxidative stressBiomarkers
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Molecular Cloning and mRNA Expression of Heat Shock Protein Genes and Their Response to Cadmium Stress in the Grasshopper Oxya chinensis

2015

Heat shock proteins (Hsps) are highly conserved molecular chaperones that are synthesized in response to stress. In this study, we cloned the full-length sequences of the Grp78 (glucose-regulated protein 78), Hsp70, Hsp90, and Hsp40 genes from the Chinese rice grasshopper Oxya chinensis. The full-length cDNA sequences of OcGrp78, OcHsp70, OcHsp90, and OcHsp40 contain open reading frames of 1947, 1920, 2172, and 1042 bp that encode proteins of 649, 640, 724, and 347 amino acids, respectively. Fluorescent real-time quantitative PCR (RT-qPCR) was performed to quantify the relative transcript levels of these Hsp genes in different tissues and developmental stages. The mRNAs encoding these four …

MaleZygotelcsh:MedicineGrasshoppersOpen Reading FramesStress PhysiologicalComplementary DNAHeat shock proteinGene expressionAnimalsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsRNA MessengerCloning Molecularlcsh:ScienceEndoplasmic Reticulum Chaperone BiPGeneHeat-Shock ProteinsRegulation of gene expressionMultidisciplinarybiologylcsh:RHSP40 Heat-Shock ProteinsHsp90Molecular biologyHsp70Real-time polymerase chain reactionGene Expression RegulationLarvabiology.proteinInsect ProteinsFemalelcsh:QResearch ArticleCadmiumSignal TransductionPLOS ONE
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Hsp60 expression, new locations, functions and perspectives for cancer diagnosis and therapy.

2008

Hsp60 in eukaryotes is considered typically a mitochondrial chaperone (also called Cpn60) but in the last few years it has become clear that it also occurs in the cytosol, the cell surface, the extracellular space, and in the peripheral blood. Studies with prokaryotic models have shown that Hsp60 plays a role in assisting nascent polypeptides to reach a native conformation, and that it interacts with Hsp10 (which also resides in the mitochondria and is also named Cpn10). In addition to its role in polypeptide folding in association with Hsp10, other functions and interacting molecules have been identified for Hsp60 in the last several years. Some of these newly identified functions are asso…

MalechaperoninCancer ResearchProtein Foldinganimal structuresChaperoninsCell SurvivalCelldifferential diagnosiGene ExpressionAntineoplastic AgentsApoptosisBiologyMitochondrionmedicine.disease_causeBioinformaticsDiagnosis Differentialtumor-cell survivalCell Line TumorNeoplasmstumor diagnosiExtracellularmedicineHumansHsp60 (Cpn60)chaperonotherapyPharmacologyClinical Oncologymonitoring response to treatmentanti-tumor immune responsefungiHsp60 (Cpn60); tumor-cell survival; apoptosis; tumor diagnosis; differential diagnosis; assessing prognosis; monitoring response to treatment; chaperonotherapy; anti-tumor immune response; chaperonin; protein foldingassessing prognosiChaperonin 60PrognosisapoptosiCell biologyCytosolmedicine.anatomical_structureOncologyChaperone (protein)biology.proteinMolecular MedicineHSP60FemaleCarcinogenesisSignal TransductionCancer biologytherapy
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The association of variants in PNPLA3 and GRP78 and the risk of developing hepatocellular carcinoma in an Italian population

2016

// Daniele Balasus 1, * , Michael Way 2, * , Caterina Fusilli 3 , Tommaso Mazza 3 , Marsha Y. Morgan 2 , Melchiorre Cervello 4 , Lydia Giannitrapani 1 , Maurizio Soresi 1 , Rosalia Agliastro 5 , Manlio Vinciguerra 2, 6 , Giuseppe Montalto 1, 4 1 Biomedical Department of Internal Medicine and Medical Specialties, University of Palermo, Palermo, Italy 2 Institute for Liver & Digestive Health, Division of Medicine, Royal Free Campus, University College London, London, UK 3 IRCCS Casa Sollievo della Sofferenza, Bioinformatics Unit, San Giovanni Rotondo (FG), Italy 4 Institute of Biomedicine and Molecular Immunology, National Research Council (C.N.R.), Palermo, Italy 5 Immunohematology and Trans…

Malehepatitis C virusSettore MED/09 - Medicina InternaGenome-wide association studyCohort StudiesLiver diseasesingle nucleotide polymorphisms0302 clinical medicineGene FrequencyRisk FactorsEpidemiologyhepatitis C viruEndoplasmic Reticulum Chaperone BiPSicilyHeat-Shock ProteinsLiver NeoplasmsTransfusion medicineHepatitis Chepatocellular carcinomaMiddle Aged3. Good healthOncologyrisk factor030220 oncology & carcinogenesisHepatocellular carcinomaCohort030211 gastroenterology & hepatologyFemaleResearch Papergenetic variantmedicine.medical_specialtyCarcinoma HepatocellularGenotypeSingle-nucleotide polymorphismPolymorphism Single Nucleotide03 medical and health sciencesInternal medicinemedicineHumansGenetic Predisposition to DiseaseAllelesAgedbusiness.industrygenetic variantsMembrane ProteinsLipasemedicine.diseasedigestive system diseasesSurgerybusiness
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