Search results for "Hsp"

showing 10 items of 557 documents

Heat Shock Protein 60 in Cardiovascular Physiology and Diseases.

2020

Heat shock protein 60 (HSP60) is a highly conserved protein abundantly expressed in both prokaryotic and eukaryotic cells. In mammals, HSP60 has been primarily considered to reside in the mitochondria, where HSP60 and HSP10 form a complex and facilitate mitochondrial protein folding. However, HSP60 is also observed in the cytoplasm, the plasma membrane, and the extracellular space. HSP60 regulates a broad spectrum of cellular events including protein trafficking, peptide hormone signaling, cell survival, cell proliferation, inflammation, and immunization. In the cardiovascular system, growing evidence indicates that HSP60 could not only play an important role under physiological conditions,…

0301 basic medicineanimal structuresMini Reviewheat shock proteinheart failureInflammationchemical and pharmacologic phenomenacardiomyocyteBiologyMitochondrionBiochemistry Genetics and Molecular Biology (miscellaneous)Biochemistrycomplex mixtures03 medical and health sciences0302 clinical medicineHeat shock proteinmedicineMolecular Bioscienceslcsh:QH301-705.5Molecular BiologyCell growthfungiCardiovascular physiologyCell biology030104 developmental biologylcsh:Biology (General)Cytoplasm030220 oncology & carcinogenesisHSP60medicine.symptomSignal transductionatherosclerosisHSP60Frontiers in molecular biosciences
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Alexander Disease Mutations Produce Cells with Coexpression of Glial Fibrillary Acidic Protein and NG2 in Neurosphere Cultures and Inhibit Differenti…

2017

Background Alexander disease (AxD) is a rare disease caused by mutations in the gene encoding glial fibrillary acidic protein (GFAP). The disease is characterized by presence of GFAP aggregates in the cytoplasm of astrocytes and loss of myelin. Objectives Determine the effect of AxD-related mutations on adult neurogenesis. Methods We transfected different types of mutant GFAP into neurospheres using the nucleofection technique. Results We find that mutations may cause coexpression of GFAP and NG2 in neurosphere cultures, which would inhibit the differentiation of precursors into oligodendrocytes and thus explain the myelin loss occurring in the disease. Transfection produces cells that diff…

0301 basic medicinecaspase-3Cathepsin Dmacromolecular substancesHSP27lcsh:RC346-429oligodendrocyte precursors03 medical and health sciencesMyelin0302 clinical medicineAlexander diseaseNG2Neurosphereneurospheresmedicinecathepsinlcsh:Neurology. Diseases of the nervous systemOriginal ResearchGlial fibrillary acidic proteinbiologyNeurogenesisNestinGFAP stainmedicine.diseaseMolecular biologyAlexander disease030104 developmental biologymedicine.anatomical_structurenervous systemNeurologyglial fibrillary acidic proteinbiology.proteinNeurology (clinical)030217 neurology & neurosurgeryNeuroscienceFrontiers in Neurology
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Complex Destabilization in the Mitochondrial Chaperonin Hsp60 Leads to Disease.

2020

Several neurological disorders have been linked to mutations in chaperonin genes and more specifically to the HSPD1 gene. In humans, HSPD1 encodes for the mitochondrial Heat Shock Protein 60 (mtHsp60) chaperonin, which carries out essential protein refolding reactions that help maintain mitochondrial and cellular homeostasis. It functions as a macromolecular complex that provides client proteins an environment that favors proper folding in an ATP dependent manner. It has been established that mtHsp60 plays a crucial role in the proper folding of mitochondrial proteins involved in ATP producing pathways. Recently, various single-point mutations in the mtHsp60 encoding gene have been directly…

0301 basic medicinechaperoninMini ReviewCellular homeostasisBiologyBiochemistry Genetics and Molecular Biology (miscellaneous)BiochemistryGroELChaperonin03 medical and health sciences0302 clinical medicineHeat shock proteinprotein foldingmtHsp60Molecular BiosciencesMolecular Biologylcsh:QH301-705.5Point mutationGroELFKBP5 GeneCell biology030104 developmental biologylcsh:Biology (General)030220 oncology & carcinogenesisHSP60Protein foldingchaperonopathyFrontiers in molecular biosciences
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Hsp60 Post-translational Modifications: Functional and Pathological Consequences.

2020

Hsp60 is a chaperone belonging to the Chaperonins of Group I and typically functions inside mitochondria in which, together with the co-chaperonin Hsp10, maintains protein homeostasis. In addition to this canonical role, Hsp60 plays many others beyond the mitochondria, for instance in the cytosol, plasma-cell membrane, extracellular space, and body fluids. These non-canonical functions include participation in inflammation, autoimmunity, carcinogenesis, cell replication, and other cellular events in health and disease. Thus, Hsp60 is a multifaceted molecule with a wide range of cellular and tissue locations and functions, which is noteworthy because there is only one hsp60 gene. The questio…

0301 basic medicinechaperoninnon-canonical functionsReviewMitochondrioncanonical functionsBiochemistry Genetics and Molecular Biology (miscellaneous)Biochemistrychaperonopathies03 medical and health sciences0302 clinical medicineUbiquitinMolecular Bioscienceslcsh:QH301-705.5Molecular Biologybiologycanonical functions chaperonin Hsp60 non-canonical functions post-translation modificationChemistryfungiCitrullinationCell cycleHsp60Cell biology030104 developmental biologylcsh:Biology (General)Mitochondrial permeability transition pore030220 oncology & carcinogenesisChaperone (protein)biology.proteinPhosphorylationHSP60post-translation modificationFrontiers in molecular biosciences
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The severe phenotype of Diamond-Blackfan anemia is modulated by heat shock protein 70.

2017

International audience; Diamond-Blackfan anemia (DBA) is a rare congenital bone marrow failure syndrome that exhibits an erythroid-specific phenotype. In at least 70% of cases, DBA is related to a haploinsufficient germ line mutation in a ribosomal protein (RP) gene. Additional cases have been associated with mutations in GATA1. We have previously established that the RPL11+/Mut phenotype is more severe than RPS19+/Mut phenotype because of delayed erythroid differentiation and increased apoptosis of RPL11+/Mut erythroid progenitors. The HSP70 protein is known to protect GATA1, the major erythroid transcription factor, from caspase-3 mediated cleavage during normal erythroid differentiation.…

0301 basic medicinecongenital hereditary and neonatal diseases and abnormalitiesIdentificationApoptosis-Inducing FactorGata1 MutationsInhibits ApoptosisBiologyHsp7003 medical and health sciencesGermline mutationRed Cells Iron and Erythropoiesishemic and lymphatic diseasesmedicine[ SDV.MHEP.HEM ] Life Sciences [q-bio]/Human health and pathology/HematologyNuclear ImportErythropoiesisDiamond–Blackfan anemiaHuman ErythroblastsBone marrow failure[SDV.MHEP.HEM]Life Sciences [q-bio]/Human health and pathology/HematologyGATA1Hematologymedicine.diseasePhenotypeMolecular biology3. Good healthHsp70030104 developmental biologyRibosomal-ProteinsProtein Gene DeletionsErythropoiesisHaploinsufficiencyBlood advances
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Heat Shock Proteins in Alzheimer’s Disease: Role and Targeting

2018

Among diseases whose cure is still far from being discovered, Alzheimer’s disease (AD) has been recognized as a crucial medical and social problem. A major issue in AD research is represented by the complexity of involved biochemical pathways, including the nature of protein misfolding, which results in the production of toxic species. Considering the involvement of (mis)folding processes in AD aetiology, targeting molecular chaperones represents a promising therapeutic perspective. This review analyses the connection between AD and molecular chaperones, with particular attention toward the most important heat shock proteins (HSPs) as representative components of the human chaperome: Hsp60,…

0301 basic medicineheat shock proteinDiseaseReviewprotein TauHsp70lcsh:ChemistrychaperoneEnzyme Inhibitorslcsh:QH301-705.5SpectroscopybiologyGeneral MedicineHsp60Hsp90Computer Science Applicationsamyloid peptideModels AnimalHSP60Protein foldingAlzheimer’s diseaseheat shock proteins; chaperones; Alzheimer’s disease; amyloid peptide; protein Tau; Hsp60; Hsp70; Hsp90Tau proteintau ProteinsHsp90Computational biologyCatalysisInorganic ChemistryMitochondrial Proteins03 medical and health sciencesAlzheimer DiseaseHeat shock proteinAnimalsHumanschaperonesHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsPhysical and Theoretical ChemistryMolecular BiologyAmyloid beta-PeptidesSettore BIO/16 - Anatomia UmanaOrganic ChemistryChaperonin 60Settore CHIM/06 - Chimica OrganicaHsp70030104 developmental biologylcsh:Biology (General)lcsh:QD1-999heat shock proteinsbiology.protein
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Inhibition of cell migration and induction of apoptosis by a novel class II histone deacetylase inhibitor, MCC2344.

2020

Epigenetic modifiers provide a new target for the development of anti-cancer drugs. The eraser histone deacetylase 6 (HDAC6) is a class IIb histone deacetylase that targets various non-histone proteins such as transcription factors, nuclear receptors, cytoskeletal proteins, DNA repair proteins, and molecular chaperones. Therefore, it became an attractive target for cancer treatment. In this study, virtual screening was applied to the MicroCombiChem database with 1162 drug-like compounds to identify new HDAC6 inhibitors. Five compounds were tested in silico and in vitro as HDAC6 inhibitors. Both analyses revealed 1-cyclohexene-1-carboxamide, 2-hydroxy-4,4-dimethyl-N-1-naphthalenyl-6-oxo- (MC…

0301 basic medicinemedicine.drug_classDNA repairAntineoplastic AgentsApoptosisHistone Deacetylase 6MicrotubulesEpigenesis Genetic03 medical and health sciences0302 clinical medicineCell MovementTubulinNeoplasmsCyclohexenesmedicineAnimalsHumansNeoplasm InvasivenessEpigeneticsHSP90 Heat-Shock ProteinsTranscription factorZebrafishPharmacologyChemistryHistone deacetylase inhibitorCell migrationAcetylationHDAC6Xenograft Model Antitumor AssaysCell biologyHistone Deacetylase Inhibitors030104 developmental biologyCell culture030220 oncology & carcinogenesisMCF-7 CellsHistone deacetylaseApoptosis Regulatory ProteinsPharmacological research
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Heat Shock Protein 60 Antibodies Are Associated With a Risk Factor for Cardiovascular Disease in Bedridden Elderly Patients

2020

Made available in DSpace on 2020-12-12T02:12:50Z (GMT). No. of bitstreams: 0 Previous issue date: 2020-06-12 Frailty, in elderly people, represents multiple deficiencies in different organs and is characterized by decreased physiological reserves and greater vulnerability to stressors. Bedridden elderly, with cardiovascular disease (CVD), have a worse prognosis than non-bedridden patients. Heat-shock proteins (HSPs) are molecular chaperones that under physiological conditions facilitate the transport, folding and assembly of proteins. Serum HSP 60-kDa concentrations and their antibodies are increased, in response to non-physiological conditions, suggesting the involvement of HSPs and their …

0301 basic medicinemedicine.medical_specialtyDiseaseBiochemistry Genetics and Molecular Biology (miscellaneous)Biochemistry03 medical and health sciences0302 clinical medicineanti-HSP60 antibodycardiovascular diseaseInternal medicineHeat shock proteinmedicineElderly peoplerisk factorsMolecular BiosciencesRisk factorlcsh:QH301-705.5Molecular BiologyOriginal ResearchFramingham Risk Scorebiologybedridden elderlybusiness.industryPlasma levels030104 developmental biologylcsh:Biology (General)030220 oncology & carcinogenesisbiology.proteinHSP60AntibodybusinessHSP60
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HSP60 activity on human bronchial epithelial cells

2017

HSP60 has been implicated in chronic inflammatory disease pathogenesis, including chronic obstructive pulmonary disease (COPD), but the mechanisms by which this chaperonin would act are poorly understood. A number of studies suggest a role for extracellular HSP60, since it can be secreted from cells and bind Toll-like receptors; however, the effects of this stimulation have never been extensively studied. We investigated the effects (pro- or anti-inflammatory) of HSP60 in human bronchial epithelial cells (16-HBE) alone and in comparison with oxidative, inflammatory, or bacterial challenges. 16-HBE cells were cultured for 1–4 h in the absence or presence of HSP60, H2O2, lipopolysaccharide (…

0301 basic medicinep38αSettore BIO/17 - IstologiaLipopolysaccharidep38 mitogen-activated protein kinasesImmunologyStimulationBronchip38 Mitogen-Activated Protein KinasesERK1Cell LinePathogenesisMitochondrial Proteins03 medical and health scienceschemistry.chemical_compound0302 clinical medicineOriginal Research ArticlesHumansImmunology and AllergyCOPDInterleukin 8Protein kinase AReceptor16-HBE; COPD; CREB1; ERK1; HSP60; IL-10; IL-8; JNK1; MyD88; NF-κB p65 subunit; TLR-4; p38αPharmacologyIL-8Settore BIO/16 - Anatomia UmanaInterleukin-8JNK1NF-κB p65 subunitEpithelial CellsTLR-4Chaperonin 60MyD88Interleukin-1016-HBEToll-Like Receptor 416-HBE; COPD; CREB1; ERK1; HSP60; IL-10; IL-8; JNK1; MyD88; NF-κB p65 subunit; p38α; TLR-4; Immunology and Allergy; Immunology; PharmacologyInterleukin 10030104 developmental biologychemistry030220 oncology & carcinogenesisIL-10Cancer researchCREB1NF-κB p65 subunitHSP60p38α
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Exosomal HSP60: a potentially useful biomarker for diagnosis, assessing prognosis, and monitoring response to treatment.

2017

Introduction: Cell-to-cell communication is imperative for life and it is mediated by sending and receiving information via the secretion and subsequent receptor-mediated detection of biological molecules. Exosomes (EXs) secreted from cells to the extracellular environment play an important role in intercellular communication in normal and pathological conditions. Areas covered: New evidence indicates that tumor cells-derived EXs contribute to cancer progression through the modulation of tumor microenvironment. The exosomal heat shock protein 60 (HSP60) is very likely a key player in intercellular cross-talk, particularly during the progress of diseases, such as cancer. Many studies have fo…

0301 basic medicinetheranostic2734BiologyExosomesPathology and Forensic Medicine03 medical and health sciencesExtracellular VesiclesImmune systemHeat shock proteinNeoplasmsGeneticsmedicineBiomarkers TumorAnimalsHumansMolecular Targeted TherapyLiquid biopsyExtracellular Vesicles (EVs)Molecular BiologyCancerTumor microenvironmentLiquid BiopsyExosomes (EXs)CancerChaperonin 60medicine.diseasePrognosisHeat Shock Protein 60 (HSP60)MicrovesiclesBiomarker030104 developmental biologyTreatment OutcomeImmunologyCancer researchMolecular MedicineHSP60BiomarkersExpert review of molecular diagnostics
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