Search results for "Chaperonin 60"

showing 10 items of 82 documents

Human Hsp60 with Its Mitochondrial Import Signal Occurs in Solution as Heptamers and Tetradecamers Remarkably Stable over a Wide Range of Concentrati…

2014

It has been established that Hsp60 can accumulate in the cytosol in various pathological conditions, including cancer and chronic inflammatory diseases. Part or all of the cytosolic Hsp60 could be naive, namely, bear the mitochondrial import signal (MIS), but neither the structure nor the in solution oligomeric organization of this cytosolic molecule has still been elucidated. Here we present a detailed study of the structure and self-organization of naive cytosolic Hsp60 in solution. Results were obtained by different biophysical methods (light and X ray scattering, single molecule spectroscopy and hydrodynamics) that all together allowed us to assay a wide range of concentrations of Hsp60…

LightCancer Treatmentlcsh:MedicinePlasma protein bindingMitochondrionBiochemistrySmall-Angle ScatteringCell-free systemScatteringchemistry.chemical_compoundCytosolProtein structureBasic Cancer ResearchMacromolecular Structure AnalysisMedicine and Health SciencesScattering RadiationHsp60 Gro EL Recombinant proteinslcsh:ScienceAdenosine TriphosphatasesMultidisciplinaryAqueous solutionMolecular StructurePhysicsElectromagnetic RadiationHydrolysisRecombinant ProteinsMitochondriaChemistryMonomerOncologyBiochemistryPhysical SciencesInterdisciplinary PhysicsHSP60Research ArticleProtein BindingProtein Structureanimal structuresBiophysicschemical and pharmacologic phenomenaBiologycomplex mixturesMitochondrial ProteinsHumansProtein InteractionsMolecular BiologyInflammationChemical PhysicsCell-Free Systemlcsh:RfungiLight ScatteringBiology and Life SciencesProteinsProtein ComplexesChaperonin 60Chaperone ProteinsCytosolSpectrometry FluorescencechemistryMolecular Complexeslcsh:QPLoS ONE
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HSP60 and CpG-DNA-oligonucleotides differentially regulate LPS-tolerance of hepatic Kupffer cells

2004

Background/aims: Hepatic Kupffer cells (KC) are major regulators of the immune response to gut-derived bacterial products; uncontrolled activation of KC by bacterial components is of pathogenic relevance in alcoholic hepatitis and septic shock. Methods: We examined the role of bacterial lipopolysaccharide (LPS), bacterial and autologous HSP60 and bacterial DNA, which are recognized by innate Toll-like receptors, during activation of murine KC. Results: In cultivated KC, autologous HSP60 induced a state of LPS-hyporesponsiveness; bacterial DNA did not mitigate the response to subsequent LPS-challenge in vitro; in contrast, pre-treatment of mice with bacterial DNA even significantly increased…

LipopolysaccharidesMaleLipopolysaccharideKupffer CellsImmunologyGene ExpressionGalactosamineReceptors Cell SurfaceCell LineMicrobiologyMicechemistry.chemical_compoundImmune systemImmunityHeat shock proteinAnimalsImmunology and AllergyInterleukin 6Cells CulturedbiologyInterleukin-6Reverse Transcriptase Polymerase Chain ReactionTumor Necrosis Factor-alphaAlanine TransaminaseChaperonin 60Macrophage ActivationToll-Like Receptor 9DNA-Binding ProteinsToll-Like Receptor 4LiverOligodeoxyribonucleotideschemistryToll-Like Receptor 9Immunologybiology.proteinFemaleHSP60Tumor necrosis factor alphaLiver FailureImmunology Letters
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Heat shock protein 60 autoimmunity and early lipid lesions in cholesterol-fed C57BL/6JBom mice during Chlamydia pneumoniae infection

2004

Chronic Chlamydia pneumoniae infection and autoimmunity to heat shock protein 60 (Hsp60) have both been documented to be associated with atherosclerosis. Herein, we studied the effects of C. pneumoniae infection and a diet with a low-cholesterol supplement on the development of autoantibodies to mouse Hsp60 and early lipid lesions in the aortic valve of C57BL/6JBom mice. In addition, pulmonary infection was investigated. C57BL/6JBom mice were given one to three C. pneumoniae inoculations and fed either a regular diet or a diet enriched with 0.2% cholesterol. Autoantibody responses against mouse Hsp60 developed in both diet groups when the mice were infected with C. pneumoniae and in uninfec…

Lung DiseasesAutoimmunity030204 cardiovascular system & hematologymedicine.disease_causeCholesterol DietaryMice03 medical and health scienceschemistry.chemical_compound0302 clinical medicineHeat shock proteinmedicineAnimalsChlamydiaceae030304 developmental biologyFoam cell0303 health sciencesChlamydiabiologyCholesterolAutoantibodyChaperonin 60Chlamydia InfectionsChlamydophila pneumoniaebiology.organism_classificationmedicine.disease3. Good healthchemistryChlamydophila pneumoniaeAortic ValveImmunologylipids (amino acids peptides and proteins)Cardiology and Cardiovascular MedicineLipoproteinAtherosclerosis
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Upon oxidative stress, the antiapoptotic Hsp60/procaspase-3 complex persists in mucoepidermoid carcinoma cells.

2008

Hsp60, a mitochondrial chaperonin highly conserved during evolution, has been found elevated in the cytosol of cancer cells, both in vivo and in vitro, but its role in determining apoptosis during oxidative stress (OS) has not yet been fully elucidated. The aim of the present work was to study the effects of OS on Hsp60 levels and its interactions with procaspase- 3 (p-C3) and p53 in tumor cells. NCI-H292 (mucoepidermoid carcinoma) cells were exposed to various concentrations of hydrogen peroxide (H2O2) for 24 hours. Cell viability was determined by Trypan blue and MTT assays. DNA damage was assessed by the Comet assay, and apoptosis was measured by the AnnexinV cytofluorimetric test. Expos…

Lung Neoplasmsanimal structuresHistologyCell SurvivalDNA damageBlotting WesternBiophysicsHsp60;procaspase-3;mucoepidermoid carcinomaGene ExpressionTetrazolium SaltsApoptosisBiologymedicine.disease_causechemistry.chemical_compoundCell Line TumormedicineHumansChaperonin Hsp60 Cpn60 procaspase-3 caspase- 3 DNA damage p53 apoptosis.Viability assaylcsh:QH301-705.5FormazansCaspase 3Settore BIO/16 - Anatomia UmanaChaperonin 60DNAHydrogen PeroxideTrypan BlueCell BiologyImmunohistochemistryMolecular biologyComet assayOxidative Stresslcsh:Biology (General)chemistryApoptosisCancer cellCarcinoma MucoepidermoidHSP60Trypan blueComet AssayTumor Suppressor Protein p53Oxidative stressDNA Damage
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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
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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
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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
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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
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Immunohistochemical evaluation of PCNA, p53, HSP60, HSP10 and MUC-2 presence and expression in prostate carcinogenesis

2003

Background: The study of the expression of different biological markers in non-neoplastic, pre-neoplastic and neoplastic lesions of prostate could help to better understand their role in carcinogenesis and to find new diagnostic and prognostic tools. Materials and Methods: In the present work we evaluated, by immunohistochemistry, the presence and the expression of PCNA, p53, HSP60, HSP10 and MUC-2 in a series of nodular hyperplasia, low- and high-grade prostatic intraepithelial lesions and adenocarcinomas. Results: Our data confirmed that: 1) PCNA expression could be related to the grade of progression of cancer; and that 2) p53 mutation could be a late event in prostate carcinogenesis. Mo…

MaleProstatic Intraepithelial NeoplasiaMucin-2Cancer ResearchGene Expression ProfilingMucinsProstatic HyperplasiaProstateProstatic NeoplasmsCarcinogenesis; Heat-shock proteins; Prostate; Cancer Research; OncologyCell DifferentiationChaperonin 60AdenocarcinomaGenes p53ImmunohistochemistryNeoplasm ProteinsHeat-shock proteinCell Transformation NeoplasticOncologyProliferating Cell Nuclear AntigenChaperonin 10Disease ProgressionHumansTumor Suppressor Protein p53Carcinogenesi
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Enhanced characterization of serum autoantibody reactivity following HSP 60 immunization in a rat model of experimental autoimmune glaucoma.

2010

Antibodies against heat shock proteins have been identified in sera of human glaucoma patients in several studies and immunization with heat shock protein 60 (HSP 60) causes retinal ganglion cell (RGC) loss in an animal model of experimental autoimmune glaucoma. The aim of this study was to observe the time course of increased anti-retina antibody appearance in the serum and characterize the identification of prominent autoantibodies that accompany HSP 60 immunization in a rat model of experimental autoimmune glaucoma.Eight weeks after immunization with HSP 60 retinal flatmounts were prepared and RGCs were counted in eight predefined areas and compared to controls. Serum collected before, a…

MaleRetinal Ganglion CellsPathologymedicine.medical_specialtyTime Factorsgenetic structuresGlaucomaDown-RegulationRetinaAutoimmune DiseasesCellular and Molecular Neurosciencechemistry.chemical_compoundAntigenHeat shock proteinmedicineAnimalsAutoantibodiesbiologyAutoantibodyRetinalGlaucomaChaperonin 60medicine.diseaseeye diseasesSensory SystemsRatsUp-RegulationBlotOphthalmologychemistryImmunizationRats Inbred LewImmunologybiology.proteinImmunizationsense organsAntibodyCurrent eye research
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