Search results for "chaperon"

showing 10 items of 358 documents

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
researchProduct

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
researchProduct

Heat shock protein 60 levels in tissue and circulating exosomes in human large bowel cancer before and after ablative surgery.

2015

BACKGROUND: Heat shock protein 60 (Hsp60) is a chaperonin involved in tumorigenesis, but its participation in tumor development and progression is not well understood and its value as a tumor biomarker has not been fully elucidated. In the current study, the authors presented evidence supporting the theory that Hsp60 has potential as a biomarker as well as a therapeutic target in patients with large bowel cancer. METHODS: The authors studied a population of 97 subjects, including patients and controls. Immunomorphology, Western blot analysis, and quantitative real-time polymerase chain reaction were performed on tissue specimens. Exosomes were isolated from blood and characterized by electr…

MaleCancer ResearchMacrophageBlotting WesternNatural killer cellEnzyme-Linked Immunosorbent AssayAdenocarcinomaExosomesReal-Time Polymerase Chain ReactionMitochondrial ProteinsHeat shock protein 60 (Hsp60)Biomarkers TumorHumansColon adenocarcinomaAgedColon adenocarcinoma; Exosomes; Heat shock protein 60 (Hsp60); Macrophages; Natural killer cells; Plasma cell membrane; Theranostics; Cancer Research; OncologyAged 80 and overPlasma cell membraneChaperonin 60Middle AgedImmunohistochemistryExosomeTheranosticOncologyColonic NeoplasmsFemaleCancer
researchProduct

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
researchProduct

Gene expression in mouse spermatogenesis during ontogenesis

2006

In this study, we evaluated the expression of genes probably involved in spermatogenesis in the mouse. We examined cytosolic chaperonin theta subunit (CCTtheta), Ngg1 interacting factor 3 like 1 binding protein 1 (NIF3L1 BP1) and apolipoprotein H (ApoH) expression during mouse onto-geny using RT-PCR. Testicular tissue was obtained from mice 3, 6, 8, 10, 12, 14, 18, 20 and 40 (adult) days after birth. For each mouse, one testis was used for histological examination, whereas RNA was extracted from the controlateral testis for expression analysis. RT-PCR analysis showed that CCTtheta gene expression was low until day 10, but increased drastically afterwards. At this age, spermatocytes started …

MaleChaperoninsSpermiogenesisMouse testis ontogenesisBiologyMiceGene expressionTestisGeneticsmedicineAnimalsRNA MessengerSpermatogenesisGeneGene expression; Mouse testis ontogenesis; SpermatogenesisGlycoproteinsReverse Transcriptase Polymerase Chain ReactionGene Expression Regulation DevelopmentalProteinsGeneral MedicineCell cycleMolecular biologyCell biologyChromatinmedicine.anatomical_structurebeta 2-Glycoprotein IGene expressionSpermatogenesisApolipoprotein HCo-Repressor ProteinsGerm cell: gene expression mouse testis ontogenesis spermatogenesisChaperonin Containing TCP-1Transcription Factors
researchProduct

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
researchProduct

Mild Aerobic Exercise Training Hardly Affects the Diaphragm of mdx Mice

2016

In the mdx mice model of Duchenne Muscular Dystrophy (DMD), mild endurance exercise training positively affected limb skeletal muscles, whereas few and controversial data exist on the effects of training on the diaphragm. The diaphragm was examined in mdx (C57BL/10ScSn-Dmdmdx) and wild-type (WT, C57BL/10ScSc) mice under sedentary conditions (mdx-SD, WT-SD) and during mild exercise training (mdx-EX, WT-EX). At baseline, and after 30 and 45 days (training: 5 d/wk for 6 weeks), diaphragm muscle morphology and Cx39 protein were assessed. In addition, tissue levels of the chaperonins Hsp60 and Hsp70 and the p65 subunit of nuclear factor-kB (NF-kB) were measured in diaphragm, gastrocnemius, and q…

MaleDuchenne muscular dystrophychaperoninTime FactorsDiaphragmSettore MED/10 - Malattie Dell'Apparato RespiratorioSettore BIO/09 - FisiologiaConnexinsMitochondrial ProteinsNecrosisendurance trainingAnimalsGenetic Predisposition to DiseaseHSP70 Heat-Shock Proteinsstress markersMuscle StrengthNF-kBSettore BIO/16 - Anatomia UmanaTranscription Factor RelAChaperonin 60Settore CHIM/06 - Chimica OrganicaExercise TherapyMuscular Dystrophy DuchenneDisease Models AnimalPhenotypeMice Inbred mdxPhysical Endurance
researchProduct

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
researchProduct

Elevated blood Hsp60, its structural similarities and cross-reactivity with thyroid molecules, and its presence on the plasma membrane of oncocytes p…

2014

The role Hsp60 might play in various inflammatory and autoimmune diseases is under investigation, but little information exists pertaining to Hashimoto’s thyroiditis (HT). With the aim to fill this gap, in the present work, we directed our attention to Hsp60 participation in HT pathogenesis. We found Hsp60 levels increased in the blood of HT patients compared to controls. The chaperonin was immunolocalized in thyroid tissue specimens from patients with HT, both in thyrocytes and oncocytes (Hurthle cells) with higher levels compared to controls (goiter). In oncocytes, we found Hsp60 not only in the cytoplasm but also on the plasma membrane, as shown by double immunofluorescence performed on …

MaleIntegrinsmedicine.medical_treatmentThyroid Glandmedicine.disease_causeBiochemistryThyroiditisAutoimmunityHashimoto DiseaseThyroglobulin (TG)Hashimoto's thyroiditis (HT)Oxyphil CellsbiologyThyroid peroxidase (TPO)GoiterThyroidHsp60Immunohistochemistrymedicine.anatomical_structureFemaleAntibodyAdultmedicine.medical_specialtyendocrine systemanimal structuresMolecular Sequence Datachemical and pharmacologic phenomenaEnzyme-Linked Immunosorbent AssayHashimoto DiseaseCross Reactionscomplex mixturesIodide PeroxidaseThyroglobulinMitochondrial ProteinsYoung AdultThyroid peroxidaseInternal medicinemedicineHumansAmino Acid SequenceAutoantibodiesOriginal PaperfungiCell MembraneAutoantibodyComputational BiologyCell BiologyChaperonin 60medicine.diseaseHsp60 . Hashimoto's thyroiditis (HT) . Thyroglobulin (TG) . Thyroid peroxidase (TPO) . Autoantibodies . Oncocytes . Hurthle cells . Thyrocytes . Chaperonin . AutoimmunityEndocrinologyStructural Homology Proteinbiology.proteinLeukocytes MononuclearThyroglobulinCell stresschaperones
researchProduct

Hsp10 nuclear localization and changes in lung cells response to cigarette smoke suggest novel roles for this chaperonin

2014

Heat-shock protein (Hsp)10 is the co-chaperone for Hsp60 inside mitochondria, but it also resides outside the organelle. Variations in its levels and intracellular distribution have been documented in pathological conditions, e.g. cancer and chronic obstructive pulmonary disease (COPD). Here, we show that Hsp10 in COPD undergoes changes at the molecular and subcellular levels in bronchial cells from human specimens and derived cell lines, intact or subjected to stress induced by cigarette smoke extract (CSE). Noteworthy findings are: (i) Hsp10 occurred in nuclei of epithelial and lamina propria cells of bronchial mucosa from non-smokers and smokers; (ii) human bronchial epithelial (16HBE) a…

MaleMitochondrionChaperoninPulmonary Disease Chronic ObstructiveCytosolSmokeSettore BIO/10 - Biochimicabronchial epithelial cellChaperonin 10nuclear localizationlcsh:QH301-705.5LungCOPD; Hsp10; bronchial epithelial cells; lung fibroblasts; nuclear localizationbronchial epithelial cellsGeneral NeuroscienceSmokingTobacco ProductsMiddle Aged33ImmunohistochemistryNucleosomesRespiratory Function TestsCell biologymedicine.anatomical_structureFemaleHSP60IntracellularResearch Article1001Hsp10ImmunologyBronchiBiologyGeneral Biochemistry Genetics and Molecular BiologyMitochondrial ProteinsOrganellemedicineHumansCOPDComputer SimulationIsoelectric PointAgedCell NucleusSettore BIO/16 - Anatomia UmanaResearchlung fibroblastsEpithelial CellsChaperonin 60DNAFibroblastsrespiratory tract diseasesMolecular WeightCell nucleusCytosollcsh:Biology (General)Immunologylung fibroblastNuclear localization sequenceOpen Biology
researchProduct