Search results for "chaperon"

showing 10 items of 358 documents

Hsp60 response in experimental and human temporal lobe epilepsy

2015

The mitochondrial chaperonin Hsp60 is a ubiquitous molecule with multiple roles, constitutively expressed and inducible by oxidative stress. In the brain, Hsp60 is widely distributed and has been implicated in neurological disorders, including epilepsy. A role for mitochondria and oxidative stress has been proposed in epileptogenesis of temporal lobe epilepsy (TLE). Here, we investigated the involvement of Hsp60 in TLE using animal and human samples. Hsp60 immunoreactivity in the hippocampus, measured by Western blotting and immunohistochemistry, was increased in a rat model of TLE. Hsp60 was also increased in the hippocampal dentate gyrus neurons somata and neuropil and hippocampus proper …

AdultMalePathologymedicine.medical_specialtyanimal structuresHippocampuschemical and pharmacologic phenomenaBiologyHippocampal formationHippocampuscomplex mixturesEpileptogenesisArticleTemporal lobeYoung AdultEpilepsymedicineNeuropilAnimalsHumansTemporal lobe epilepsyMultidisciplinaryHippocampus properDentate gyrusfungiChaperonin 60Middle Agedmedicine.diseaseImmunohistochemistryRatsmedicine.anatomical_structureEpilepsy Temporal Lobenervous systemDentate GyrusFemale
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Different immunohistochemical levels of Hsp60 and Hsp70 in a subset of brain tumors and putative role of Hsp60 in neuroepithelial tumorigenesis

2013

In this work we analysed, by immunohistochemistry, a series of brain tumors to detect the levels and cellular distribution of Hsp60 and Hsp70. We found that Hsp60 levels were significantly higher than those of Hsp70 in neuroepithelial tumors, while levels of both molecules were not significantly different from each other in meningeal neoplasms. In particular, Hsp60 immunopositivity was present mainly at the cytoplasmic level, while Hsp70 immunopositivity was found both in the cytoplasm and in the nucleus of tumor cells. The levels of these molecules in healthy control cells were always very low. Finally, Hsp60 and Hsp70 levels did not correlate with the different types (WHO grade) of neopla…

AdultMalePathologymedicine.medical_specialtyanimal structuresHistologyAdolescentNeuroepithelial CellsBiophysicschemical and pharmacologic phenomenaBiologymedulloblastomamedicine.disease_causemeningiomacomplex mixturesHsp60 Hsp70 astrocytoma glioblastoma multiformae medulloblastoma meningiomaHsp70Meningeal NeoplasmsmedicineHumansHSP70 Heat-Shock ProteinsMeningeal NeoplasmChildastrocytomalcsh:QH301-705.5AgedAged 80 and overMedulloblastomaHsp60 Hsp70 astrocytoma glioblastoma multiformae medulloblastoma meningioma.Brain NeoplasmsBrief ReportfungiAstrocytomaChaperonin 60Cell BiologyMiddle AgedHsp60medicine.diseaseImmunohistochemistryNeoplasms NeuroepithelialNeuroepithelial cellglioblastoma multiformaelcsh:Biology (General)Tumor progressionChild PreschoolCancer cellImmunohistochemistryFemaleCarcinogenesisEuropean Journal of Histochemistry
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Heat-shock protein 60 kDa and atherogenic dyslipidemia in patients with untreated mild periodontitis: a pilot study

2012

Identification of predictors of cardiovascular risk can help in the prevention of pathologic episodes and the management of patients at all stages of illness. Here, we investigated the relationships between serum levels of Hsp60 and dyslipidemia in patients with periodontitis by performing a cross-sectional study of 22 patients with mild periodontitis without any prior treatment for it (i.e., drug naive) and 22 healthy controls, matched for age and body mass index (BMI). All subjects were evaluated for periodontal status, gingival inflammation, and oral hygiene. Levels of circulating Hsp60, C-reactive protein (CRP), and plasma lipids were measured, and small, dense low-density lipoproteins …

AdultMalemedicine.medical_specialtyPeriodontal pathologyPilot ProjectsBiochemistryBody Mass Indexchemistry.chemical_compoundRisk FactorsInternal medicinemedicineHumansperiodontitisTriglyceridesDyslipidemiasPeriodontitisOriginal PaperbiologyCholesterolbusiness.industrydyslipidemiaC-reactive proteinAge FactorsMouth MucosaChaperonin 60Cell BiologyMiddle AgedHsp60medicine.diseaseLipidsHsp60; dyslipidemia; periodontitisLipoproteins LDLDrug-naïveC-Reactive ProteinCross-Sectional StudiesEndocrinologychemistryCardiovascular Diseasesbiology.proteinFemaleMetabolic syndromeLipoproteins HDLbusinessBody mass indexDyslipidemiamedicine.drugCell Stress and Chaperones
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The chaperone system in glioblastoma multiforme and derived cell lines: diagnostic and mechanistic implications.

2022

BACKGROUND: Glioblastoma multiforme (GBM) is the most common and malignant primary brain tumor in adults. Novel treatments are needed to counteract the molecular mechanisms of GBM growth and drug resistance. The chaperone system (CS) members are typically cytoprotective but some, termed Hsp, can become pathogenic and participate in carcinogenesis, along with the vascular endothelial growth factor (VEGF), and we investigated them in GBM biopsies and derived cell lines. The objectives were to identify diagnostic-prognostic biomarkers and gather information for developing chaperonotherapy. METHODS: Cell lines from GBMs were established, characterized (morphology, growth characteristics, and sp…

AdultVascular Endothelial Growth Factor AGeneral Immunology and MicrobiologySettore BIO/16 - Anatomia UmanaBrain Neoplasmschaperone system (CS) glioblastoma multiforme (GBM) GMB cell lines heat shock protein (Hsp) vascular endothelial growth factor (VEGF)HSP27 Heat-Shock ProteinsHumansHSP70 Heat-Shock ProteinsGlioblastomaGeneral Biochemistry Genetics and Molecular BiologyCell LineFrontiers in bioscience (Landmark edition)
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Heat shock protein-27 protects human bronchial epithelial cells against oxidative stress-mediated apoptosis: possible implication in asthma.

2002

Inflammation of the human bronchial epithelium, as observed in asthmatics, is characterized by the selective death of the columnar epithelial cells, which desquamate from the basal cells. Tissue repair initiates from basal cells that resist inflammation. Here, we have evaluated the extent of apoptosis as well as the Hsp27 level of expression in epithelial cells from bronchial biopsy samples taken from normal and asthmatic subjects. Hsp27 is a chaperone whose expression protects against oxidative stress. We report that in asthmatic subjects the basal epithelium cells express a high level of Hsp27 but no apoptotic morphology. In contrast, apoptotic columnar cells are devoid of Hsp27 expressio…

Adultendocrine systemanimal structuresHSP27 Heat-Shock ProteinsInflammationApoptosisBronchiColumnar CellRespiratory MucosaBiologymedicine.disease_causeBiochemistryGene Expression Regulation EnzymologicHsp27Heat shock proteinmedicineBronchial BiopsyHumansHeat-Shock ProteinsEpithelial CellsCell BiologyHydrogen PeroxideOriginal ArticlesMiddle AgedOxidantsEpitheliumAsthmaCell biologyNeoplasm ProteinsOxidative Stressmedicine.anatomical_structureApoptosisImmunologybiology.proteinmedicine.symptomOxidative stressMolecular ChaperonesCell stresschaperones
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BAG3 and friends: co-chaperones in selective autophagy during aging and disease.

2011

There is a reciprocal change in the expression of two members of the BAG (Bcl-2-associated athanogen) family, BAG1 and BAG3, during cellular aging and under acute stress ("BAG1-BAG3-switch"). BAG3 was recently described as a mediator of a novel macroautophagy pathway that uses the specificity of heat shock protein 70 (HSP70) to misfolded proteins and also involves other protein partners, such as HSPB8. Also crucial for induction and execution of autophagy are sequestosome-1/p62 (SQSTM1/p62) and LC3, an autophagosome-associated protein. In this novel pathway, BAG3 mediates the targeting and transport of degradation-prone substrates into aggresomes via the microtubule-motor dynein. Interestin…

AgingProteasome Endopeptidase ComplexDyneinBAG3Models BiologicalJUNQ and IPODUbiquitinAutophagyAnimalsDiseaseMolecular BiologyAdaptor Proteins Signal TransducingbiologyAutophagyUbiquitinationSignal transducing adaptor proteinDyneinsCell BiologyAdaptation PhysiologicalCell biologyHsp70DNA-Binding ProteinsAggresomeBiochemistrybiology.proteinMolecular ChaperonesTranscription FactorsAutophagy
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Chaperonopathies of senescence and the scrambling of interactions between the chaperoning and the immune systems.

2010

Aging entails progressive deterioration of molecules and supramolecular structures, including Hsp chaperones and their complexes, paralleled by functional decline. Recent research has changed our views on Hsp chaperones. They work inside and outside cells in many locations, alone or forming teams, interacting with cells, receptors, and molecules that are not chaperones, in roles that are not typically attributed to chaperones, such as protein folding. Hsp chaperones form a physiological system with a variety of functions and interactions with other systems, for example, the immune system. We propose that chaperone malfunctioning due to structural damage or gene dysregulation during aging ha…

AgingProtein Foldingchaperonopathies by mistakeSettore BIO/16 - Anatomia Umanachaperoning systemImmune Systemchaperoning system interactionchaperonopathieCarrier Proteinschaperonotherapy Hsp60Molecular ChaperonesAnnals of the New York Academy of Sciences
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HSF1-controlled and age-associated chaperone capacity in neurons and muscle cells of C. elegans.

2010

Protein stability under changing conditions is of vital importance for the cell and under the control of a fine-tuned network of molecular chaperones. Aging and age-related neurodegenerative diseases are directly associated with enhanced protein instability. Employing C. elegans expressing GFP-tagged luciferase as a reporter for evaluation of protein stability we show that the chaperoning strategy of body wall muscle cells and neurons is significantly different and that both are differently affected by aging. Muscle cells of young worms are largely resistant to heat stress, which is directly mediated by the stress response controlled through Heat Shock Transcription Factor 1. During recover…

AgingProteomeGreen Fluorescent Proteinslcsh:MedicineBiologyBiochemistryBiochemistry/Protein FoldingAnimals Genetically ModifiedHeat shock proteinAnimalsMyocyteHeat shockCaenorhabditis elegansCaenorhabditis elegans ProteinsHSF1lcsh:ScienceDNA PrimersNeuronsMultidisciplinaryBase SequenceMuscleslcsh:RCell Biology/Cellular Death and Stress ResponsesMolecular biologyCell biologyHeat shock factorMicroscopy FluorescenceChaperone (protein)biology.proteinProtein foldinglcsh:QProtein stabilizationResearch ArticleMolecular ChaperonesTranscription FactorsPLoS ONE
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Stress protein/peptide complexes derived from autologous tumor tissue as tumor vaccines.

1999

Vaccination of inbred mice with tumor-derived stress proteins hsp70, hsp90, and gp96/grp94 elicits a protective immunity to the tumor from which the vaccine was purified. There is now comprehensive experimental evidence that the antigenicity of tumor-derived hsp70, hsp90, and gp96 preparations results from diverse arrays of endogenous peptide antigens complexed with these stress proteins. Vaccination with tumor-derived stress protein/peptide complexes leads to their uptake and processing by professional antigen-presenting cells and to presentation of associated tumor peptide antigens to cytotoxic T cells. This induces a tumor-specific cytotoxic T cell response. The attractiveness of the con…

AntigenicityPeptideMice Inbred StrainsBiologyBiochemistryCancer VaccinesMiceImmune systemAntigenAntigens NeoplasmHeat shock proteinHistocompatibility AntigensNeoplasmsCytotoxic T cellAnimalsHumansHeat-Shock ProteinsPharmacologychemistry.chemical_classificationHsp90Hsp70chemistryImmunologyCancer researchbiology.proteinMolecular ChaperonesT-Lymphocytes CytotoxicBiochemical pharmacology
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Lack of Dystrophin Affects Bronchial Epithelium in mdx Mice

2016

Mild exercise training may positively affect the course of Duchenne Muscular Dystrophy (DMD). Training causes mild bronchial epithelial injury in both humans and mice, but no study assessed the effects of exercise in mdx mice, a well known model of DMD. The airway epithelium was examined in mdx (C57BL/10ScSn-Dmdmdx) mice, and in wild type (WT, C57BL/10ScSc) mice either under sedentary conditions (mdx-SD, WT-SD) or during mild exercise training (mdx-EX, WT-EX). At baseline, and after 30 and 45 days of training (5 d/wk for 6 weeks), epithelial morphology and markers of regeneration, apoptosis, and cellular stress were assessed. The number of goblet cells in bronchial epithelium was much lower…

Apoptosis; Chaperonin 60 (HSP60); Dystrophin; Goblet cells; Proliferation; Clinical Biochemistry; Cell Biology; PhysiologyPhysiologyProliferationClinical BiochemistryGene ExpressionApoptosiBronchiCell BiologyEpitheliumMice Inbred C57BLMuscular Dystrophy DuchenneDystrophinMice Inbred mdxAnimalsRegenerationChaperonin 60 (HSP60)Muscle SkeletalGoblet cell
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