Search results for "P[6]"

showing 10 items of 252 documents

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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CEP63 deficiency promotes p53-dependent microcephaly and reveals a role for the centrosome in meiotic recombination

2015

Artículo escrito por un elevado número de autores, solo se referencian el que aparece en primer lugar, el nombre del grupo de colaboración, si le hubiere, y los autores pertenecientes a la UAM

MaleProgrammed cell deathMicrocephalyGeneral Physics and AstronomyCell Cycle ProteinsDwarfismBiologyReal-Time Polymerase Chain ReactionArticleGeneral Biochemistry Genetics and Molecular BiologyMice03 medical and health sciences0302 clinical medicineChromosome structureSpermatocytesmedicineAnimalscentrioleHomologous Recombination030304 developmental biologyRecombination GeneticfertilityGeneticsCentrosomeMeiotic recombination0303 health sciencesMultidisciplinarySperm CountProtein cep63FaciesGeneral Chemistrymedicine.diseaseBiología y Biomedicina / BiologíaImmunohistochemistryNeural stem cell3. Good healthCEP63MeiosisSeckel syndromeCentrosomeMicrocephalyTumor Suppressor Protein p53Homologous recombinationmicrocephaly ; DNA damage ; centrosome ; meiosis030217 neurology & neurosurgeryDNA Damage
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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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Immunoproteasome LMP2 60HH Variant Alters MBP Epitope Generation and Reduces the Risk to Develop Multiple Sclerosis in Italian Female Population

2010

BackgroundAlbeit several studies pointed out the pivotal role that CD4+T cells have in Multiple Sclerosis, the CD8+ T cells involvement in the pathology is still in its early phases of investigation. Proteasome degradation is the key step in the production of MHC class I-restricted epitopes and therefore its activity could be an important element in the activation and regulation of autoreactive CD8+ T cells in Multiple Sclerosis.Methodology/principal findingsImmunoproteasomes and PA28-alphabeta regulator are present in MS affected brain area and accumulated in plaques. They are expressed in cell types supposed to be involved in MS development such as neurons, endothelial cells, oligodendroc…

MaleT cells proteasomes multiple sclerosis parietal lobeMuscle ProteinsImmunoproteasomeEpitopeEpitopesGene FrequencyRisk FactorsCytotoxic T cellFunding: This work was financed in part by the grant Giovani Ricercatori 2007 from Italian Ministry of Health to MM DG and FMB by a grant from the European Commission Integrated Project PROTEOMAGE (FP6) to CF by the finalized projects of Fondazione Italiana Sclerosi Multipla (FISM) cod. 2003/R26 and BioPharmaNet to CF and 2002/R/40 and 2005/R/10 2008/R/11 (Genoa) to SD'A by the University of Bologna (FRO) to MPF by the Regione Piemonte (Ricerca Sanitaria Finalizzata Project and Ricerca Sanitaria Applicata-CIPE Project) to SD'A by Associazione Amici del Centro Dino Ferrari and IRCCS Ospedale Maggiore Policlinico Milano to DG and by the grants Sonderforschungsbereich (SFB-507 SFB-421) to PMK and US the grants TR43 and Neurocure to PMK. MM benefited from the A.V. Humboldt PostDoc fellowship. The funders had no role in study design data collection and analysis decision to publish or preparation of the manuscript.MultidisciplinaryMicrogliaQRBrainMiddle AgedImmunohistochemistryCysteine EndopeptidasesOligodendrogliamedicine.anatomical_structureItalyImmunoproteasome; multiple sclerosis; italian populationmultiple sclerosiImmunology/Antigen Processing and RecognitionMedicineFemaleMicrogliaNeuroscience/Neurobiology of Disease and RegenerationResearch ArticleProtein BindingAdultProteasome Endopeptidase ComplexMultiple SclerosisGenotypeScienceMolecular Sequence DataImmunology/AutoimmunityBiologySex FactorsMHC class IHLA-A2 AntigenmedicineHumansAmino Acid SequenceAlleleHLA-A AntigensMultiple sclerosisMacrophagesMyelin Basic Proteinmedicine.diseaseMyelin basic proteinImmunologybiology.proteinitalian populationCD8PLoS ONE
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Obesity causes PGC‐1α deficiency in the pancreas leading to marked IL‐6 upregulation via NF‐κB in acute pancreatitis

2019

Obesity is associated with local and systemic complications in acute pancreatitis. PPARγ coactivator 1α (PGC-1α) is a transcriptional coactivator and master regulator of mitochondrial biogenesis that exhibits dysregulation in obese subjects. Our aims were: (1) to study PGC-1α levels in pancreas from lean or obese rats and mice with acute pancreatitis; and (2) to determine the role of PGC-1α in the inflammatory response during acute pancreatitis elucidating the signaling pathways regulated by PGC-1α. Lean and obese Zucker rats and lean and obese C57BL6 mice were used first; subsequently, wild-type and PGC-1α knockout (KO) mice with cerulein-induced pancreatitis were used to assess the inflam…

MaleTaurocholic Acid0301 basic medicinemedicine.medical_specialtyPGC-1αPathology and Forensic Medicine03 medical and health sciencesDownregulation and upregulationInternal medicineAnimalsMedicineObesityPhosphorylationInterleukin 6PancreasCeruletideMice KnockoutIL-6biologyp65Interleukin-6business.industryNF-kappa BTranscription Factor RelAmedicine.diseasePeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaRats ZuckerUp-Regulation3. Good healthMice Inbred C57BLDisease Models Animal030104 developmental biologyEndocrinologymedicine.anatomical_structureMitochondrial biogenesisPancreatitisbiology.proteinPancreatitisAcute pancreatitisPPARGC1AbusinessPancreasCeruletideSignal TransductionThe Journal of Pathology
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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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Cross-linguistic variation in the neurophysiological response to semantic processing: Evidence from anomalies at the borderline of awareness

2014

The N400 event-related brain potential (ERP) has played a major role in the examination of how the human brain processes meaning. For current theories of the N400, classes of semantic inconsistencies which do not elicit N400 effects have proven particularly influential. Semantic anomalies that are difficult to detect are a case in point ("borderline anomalies", e.g. "After an air crash, where should the survivors be buried?"), engendering a late positive ERP response but no N400 effect in English (Sanford, Leuthold, Bohan, & Sanford, 2011). In three auditory ERP experiments, we demonstrate that this result is subject to cross-linguistic variation. In a German version of Sanford and colleagu…

Malegenetic structuresElectroencephalographyBrain mappingLate positivityDevelopmental psychologyGermanBehavioral NeuroscienceSurveys and QuestionnairesCross-linguistic differencesPsychologySemantic memoryN400Control (linguistics)Evoked PotentialsBrain Mappingmedicine.diagnostic_testBorderline anomaliesElectroencephalographyExperimental PsychologyAwarenessSemanticsVariation (linguistics)Bidirectional coding accountlanguageFemaleCognitive SciencesBottom-upPsychologypsychological phenomena and processesCognitive psychologyAdultAdolescentCognitive NeuroscienceExperimental and Cognitive PsychologySemanticsbehavioral disciplines and activitiesArticleYoung AdultClinical ResearchmedicineHumansP600Language processingShallow processingNeurosciencesLinguisticsTranslatingTop-downN400language.human_languageAcoustic StimulationNeuropsychologia
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Hsp60 and heme oxygenase-1 (Hsp32) in acute myocardial infarction

2011

Heat shock proteins (Hsps) are produced in response to various stressors, including ischemia-reperfusion, and they can exit cells and reach the blood. In this pilot study, we determined serum levels of Hsp60 and heme-oxygenase-1 (HO-1; also named Hsp32) in subjects with acute myocardial infarction (AMI) to assess their clinical significance and potential prognostic value. We also performed a bioinformatics analysis of the 2 molecules in search of structural clues on the mechanism of their release from cells. We studied 40 patients consecutively admitted for AMI (male:female patient ratio = 20:20, mean age: 64 ± 13 years) and 40 matched controls. A blood sample was drawn for biochemical anal…

Malemedicine.medical_specialtyPathologyStatistics as TopicMyocardial InfarctionPilot ProjectsCreatineGastroenterologyCoronary artery diseasePathogenesischemistry.chemical_compoundPredictive Value of TestsPhysiology (medical)Internal medicinemedicineHumansClinical significancecardiovascular diseasesMyocardial infarctionacute myocardial infarction heme oxyenase-1 Hsp Hsp60AgedAged 80 and overbiologybusiness.industrySettore BIO/16 - Anatomia UmanaBiochemistry (medical)C-reactive proteinPublic Health Environmental and Occupational HealthCase-control studyComputational BiologyChaperonin 60General MedicineMiddle Agedmedicine.diseaseTroponinchemistryCase-Control Studiesbiology.proteinFemalebusinessHeme Oxygenase-1Follow-Up Studies
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Quaternary structures of GroEL and naïve-Hsp60 chaperonins in solution: a combined SAXS-MD study

2015

The quaternary structures of bacterial GroEL and human naïve-Hsp60 chaperonins in physiological conditions have been investigated by an innovative approach based on a combination of synchrotron Small Angle X-ray Scattering (SAXS) in-solution experiments and molecular dynamics (MD) simulations. Low-resolution SAXS experiments over large and highly symmetric oligomers are analyzed on the basis of the high-resolution structure of the asymmetric protein monomers, provided by MD. The results reveal remarkable differences between the solution and the crystallographic structure of GroEL and between the solution structures of GroEL and of its human homologue Hsp60.

Materials scienceSettore BIO/16 - Anatomia UmanaSmall-angle X-ray scatteringGeneral Chemical EngineeringChemistry (all)Settore CHIM/06 - Chimica OrganicaGeneral ChemistryCrystal structureGroELSynchrotronlaw.inventionChaperoninChemistry (all); Chemical Engineering (all) Molecular Dynamics Heat Shock Proteins Small Angle X-ray Scatteringchemistry.chemical_compoundCrystallographyMolecular dynamicsMonomerchemistrySettore CHIM/03 - Chimica Generale E InorganicalawHSP60Chemical Engineering (all) Molecular Dynamics Heat Shock Proteins Small Angle X-ray ScatteringRSC Advances
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