Search results for "chaperone"

showing 10 items of 249 documents

Contribution of Extracellular Vesicles and Molecular Chaperones in Age-Related Neurodegenerative Disorders of the CNS

2023

Many neurodegenerative disorders are characterized by the abnormal aggregation of misfolded proteins that form amyloid deposits which possess prion-like behavior such as self-replication, intercellular transmission, and consequent induction of native forms of the same protein in surrounding cells. The distribution of the accumulated proteins and their correlated toxicity seem to be involved in the progression of nervous system degeneration. Molecular chaperones are known to maintain proteostasis, contribute to protein refolding to protect their function, and eliminate fatally misfolded proteins, prohibiting harmful effects. However, chaperone network efficiency declines during aging, prompt…

Inorganic ChemistryOrganic ChemistryGeneral MedicinePhysical and Theoretical Chemistrycentral nervous system extracellular vesicles chaperones system aging neurodegenerationMolecular BiologySpectroscopyCatalysisComputer Science Applications
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HSP27 controls GATA-1 protein level during erythroid cell differentiation.

2010

AbstractHeat shock protein 27 (HSP27) is a chaperone whose cellular expression increases in response to various stresses and protects the cell either by inhibiting apoptotic cell death or by promoting the ubiquitination and proteasomal degradation of specific proteins. Here, we show that globin transcription factor 1 (GATA-1) is a client protein of HSP27. In 2 models of erythroid differentiation; that is, in the human erythroleukemia cell line, K562 induced to differentiate into erythroid cells on hemin exposure and CD34+ human cells ex vivo driven to erythroid differentiation in liquid culture, depletion of HSP27 provokes an accumulation of GATA-1 and impairs terminal maturation. More spec…

LeupeptinsPyridines[SDV]Life Sciences [q-bio]Cellular differentiationCellHSP27 Heat-Shock ProteinsAntigens CD34Biochemistryp38 Mitogen-Activated Protein Kinases0302 clinical medicineTransforming Growth Factor betahemic and lymphatic diseasesChlorocebus aethiopsGATA1 Transcription FactorPhosphorylationComputingMilieux_MISCELLANEOUSCells CulturedHeat-Shock Proteins0303 health sciencesbiologyImidazolesCell DifferentiationHematology[SDV] Life Sciences [q-bio]medicine.anatomical_structure030220 oncology & carcinogenesisembryonic structuresCOS CellsRNA InterferenceSignal transductionProteasome InhibitorsProtein BindingProteasome Endopeptidase ComplexImmunologyImmunoblotting03 medical and health sciencesHsp27Erythroid CellsHeat shock proteinmedicineAnimalsHumansTranscription factor030304 developmental biologyCell NucleusInterleukin-6UbiquitinationCell BiologyTransforming growth factor betaMolecular biologyChaperone (protein)biology.proteinK562 CellsHeLa CellsMolecular ChaperonesBlood
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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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Pro-invasive stimuli and the interacting protein Hsp70 favour the route of alpha-enolase to the cell surface

2017

AbstractCell surface expression of alpha-enolase, a glycolytic enzyme displaying moonlighting activities, has been shown to contribute to the motility and invasiveness of cancer cells through the protein non-enzymatic function of binding plasminogen and enhancing plasmin formation. Although a few recent records indicate the involvement of protein partners in the localization of alpha-enolase to the plasma membrane, the cellular mechanisms underlying surface exposure remain largely elusive. Searching for novel interactors and signalling pathways, we used low-metastatic breast cancer cells, a doxorubicin-resistant counterpart and a non-tumourigenic mammary epithelial cell line. Here, we demon…

Lipopolysaccharides0301 basic medicineAlpha-enolaseScienceCellPlasma protein bindingArticle03 medical and health sciencesCell MovementEpidermal growth factorCell Line TumormedicineHumansHSP70 Heat-Shock ProteinsRegulation of gene expressionMultidisciplinarybiologyQCell MembraneR3. Good healthCell biologyGene Expression Regulation NeoplasticSettore BIO/18 - Genetica030104 developmental biologymedicine.anatomical_structurePhosphopyruvate HydrataseChaperone (protein)Cancer cellbiology.proteinMedicineEnolase Hsp70 protein cell surface cancer biologyIntracellularProtein Binding
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Exploring organ-specific features of fibrogenesis using murine precision-cut tissue slices

2019

Fibrosis is the hallmark of pathologic tissue remodelling in most chronic diseases. Despite advances in our understanding of the mechanisms of fibrosis, it remains uncured. Fibrogenic processes share conserved core cellular and molecular pathways across organs. In this study, we aimed to elucidate shared and organ-specific features of fibrosis using murine precision-cut tissue slices (PCTS) prepared from small intestine, liver and kidneys. PCTS displayed substantial differences in their baseline gene expression profiles: 70% of the extracellular matrix (ECM)-related genes were differentially expressed across the organs. Culture for 48 h induced significant changes in ECM regulation and trig…

Liver CirrhosisEXPRESSION0301 basic medicineINHIBITOR LY2157299 MONOHYDRATEPROTEINPrecision-cut tissue slicesSmad2 ProteinLIVER FIBROSISBiologyKidneyMECHANISMSSMAD2ACTIVATIONPATHWAYExtracellular matrixMiceTGFβ03 medical and health sciences0302 clinical medicineTransforming Growth Factor betaTGF betaFibrosisGene expressionTGF beta signaling pathwaymedicineAnimalsGalunisertibProtein Kinase InhibitorsMolecular BiologyMOLECULAR CHAPERONEGROWTH-FACTOR-BETAKinaseTGF-BETAExtracellular matrixmedicine.diseaseFibrosisPathophysiologyCell biologyMice Inbred C57BL030104 developmental biologyLiver030220 oncology & carcinogenesisQuinolinesPyrazolesMolecular MedicineCollagenHomeostasisSignal TransductionBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
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The Hsc/Hsp70 Co-Chaperone Network Controls Antigen Aggregation and Presentation during Maturation of Professional Antigen Presenting Cells

2011

The maturation of mouse macrophages and dendritic cells involves the transient deposition of ubiquitylated proteins in the form of dendritic cell aggresome-like induced structures (DALIS). Transient DALIS formation was used here as a paradigm to study how mammalian cells influence the formation and disassembly of protein aggregates through alterations of their proteostasis machinery. Co-chaperones that modulate the interplay of Hsc70 and Hsp70 with the ubiquitin-proteasome system (UPS) and the autophagosome-lysosome pathway emerged as key regulators of this process. The chaperone-associated ubiquitin ligase CHIP and the ubiquitin-domain protein BAG-1 are essential for DALIS formation in mou…

Macromolecular AssembliesImmune CellsCellular differentiationImmunologyAntigen presentationAntigen-Presenting Cellslcsh:MedicineAntigen Processing and RecognitionMajor histocompatibility complexBiochemistryMiceMolecular Cell BiologyMHC class IAutophagyAnimalsHSP70 Heat-Shock ProteinsAntigensProtein Interactionslcsh:ScienceAntigen-presenting cellBiologyImmune ResponseCellular Stress ResponsesAntigen PresentationMultidisciplinarybiologylcsh:RHSC70 Heat-Shock ProteinsImmunityProteinsCell DifferentiationDendritic cellChaperone ProteinsUbiquitin ligaseCell biologyProteostasisbiology.proteinlcsh:QProtein MultimerizationResearch ArticlePLoS ONE
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Decoding the Folding of Burkholderia glumae Lipase: Folding Intermediates En Route to Kinetic Stability

2012

The lipase produced by Burkholderia glumae folds spontaneously into an inactive near-native state and requires a periplasmic chaperone to reach its final active and secretion-competent fold. The B. glumae lipase-specific foldase (Lif) is classified as a member of the steric-chaperone family of which the propeptides of alpha-lytic protease and subtilisin are the best known representatives. Steric chaperones play a key role in conferring kinetic stability to proteins. However, until present there was no solid experimental evidence that Lif-dependent lipases are kinetically trapped enzymes. By combining thermal denaturation studies with proteolytic resistance experiments and the description of…

Macromolecular AssembliesProtein StructureProtein FoldingBurkholderiaProtein ConformationStereochemistryBiophysicslcsh:MedicineBiochemistryProtein Chemistrybacterial lipasemolten globuleBacterial ProteinsNative stateBurkholderia glumaeLipaseProtein Interactionslcsh:ScienceBiologyMultidisciplinarybiologylipase-specific foldasePhysicslcsh:RSubtilisinProteinsLipasebiology.organism_classificationMolten globuleEnzymesChaperone ProteinsKineticsBiochemistryChaperone (protein)Enzyme StructureProteolysisFoldasebiology.proteinlcsh:Qsteric chaperoneProtein foldingnear-native folding intermediateResearch ArticleMolecular Chaperones
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Moderate weight loss attenuates chronic endoplasmic reticulum stress and mitochondrial dysfunction in human obesity

2018

Abstract Objective In obese patients undergoing caloric restriction, there are several potential mechanisms involved in the improvement of metabolic outcomes. The present study further explores whether caloric restriction can modulate endoplasmic reticulum (ER) stress and mitochondrial function, as both are known to be mechanisms underlying inflammation and insulin resistance (IR) during obesity. Methods A total of 64 obese patients with BMI ≥35 kg/m2 underwent a dietary program consisting of 6 weeks of a very-low-calorie diet followed by 18 weeks of low-calorie diet. We evaluated changes in the metabolic and inflammatory markers -TNFα, hsCRP, complement component 3 (C3c), and retinol bindi…

Male0301 basic medicineGPX1MitochondrionSystemic inflammationmedicine.disease_causeGlutathione Peroxidase GPX10302 clinical medicineSirtuin 1Endoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsMembrane Potential MitochondrialbiologyComplement C3Middle AgedEndoplasmic Reticulum StressMitochondriaC-Reactive ProteinFemalemedicine.symptomAdultmedicine.medical_specialty030209 endocrinology & metabolism03 medical and health sciencesInsulin resistanceInternal medicineWeight LossmedicineHumansObesityMolecular BiologyCaloric RestrictionInflammationGlutathione PeroxidaseRetinol binding protein 4Tumor Necrosis Factor-alphabusiness.industryEndoplasmic reticulumCell Biologymedicine.disease030104 developmental biologyEndocrinologySpainbiology.proteinUnfolded protein responseInsulin ResistanceReactive Oxygen SpeciesbusinessRetinol-Binding Proteins PlasmaOxidative stressMolecular Metabolism
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Long-Term Calorie Restriction Enhances Cellular Quality-Control Processes in Human Skeletal Muscle

2015

Calorie restriction (CR) retards aging, acts as a hormetic intervention, and increases serum corticosterone and HSP70 expression in rodents. However, less is known regarding the effects of CR on these factors in humans. Serum cortisol and molecular chaperones and autophagic proteins were measured in the skeletal muscle of subjects on CR diets for 3-15 years and in control volunteers. Serum cortisol was higher in the CR group than in age-matched sedentary and endurance athlete groups (15.6 ± 4.6 ng/dl versus 12.3 ± 3.9 ng/dl and 11.2 ± 2.7 ng/dl, respectively; p ≤ 0.001). HSP70, Grp78, beclin-1, and LC3 mRNA and/or protein levels were higher in the skeletal muscle of the CR group compared to…

Male0301 basic medicineGenetics and Molecular Biology (all)Time FactorsHydrocortisoneBiochemistryCortisolBody Mass IndexCluster Analysislcsh:QH301-705.5Endoplasmic Reticulum Chaperone BiPAldosteroneHeat-Shock ProteinsHSP70Serum cortisolMiddle Agedmedicine.anatomical_structureBeclin-1Femalemedicine.symptomMicrotubule-Associated Proteinsmedicine.drugAdultmedicine.medical_specialtyCalorie restrictionInflammationBiologyGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciencesEndurance trainingInternal medicineHeat shock proteinmedicineAutophagyHumansHSP70 Heat-Shock ProteinsRNA MessengerMuscle SkeletalExerciseCalorie restrictionCaloric RestrictionHydrocortisoneHSP70; aldosterone; autophagy; calorie restriction; cortisol; adult; apoptosis regulatory proteins; beclin-1; body mass index; cluster analysis; exercise; female; gene expression regulation; hsp70 heat-shock proteins; heat-shock proteins; humans; hydrocortisone; male; membrane proteins; microtubule-associated proteins; middle aged; muscle skeletal; RNA messenger; time factors; transcription factors; caloric restrictionCalorie restriction (CR)AutophagyMembrane ProteinsSkeletal muscleHsp70030104 developmental biologyEndocrinologylcsh:Biology (General)Gene Expression RegulationAldosterone; Autophagy; Calorie restriction; Cortisol; HSP70; Biochemistry Genetics and Molecular Biology (all)Apoptosis Regulatory ProteinsTranscription Factors
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Immunomorphological Pattern of Molecular Chaperones in Normal and Pathological Thyroid Tissues and Circulating Exosomes: Potential Use in Clinics

2019

The thyroid is a major component of the endocrine system and its pathology can cause serious diseases, e.g., papillary carcinoma (PC). However, the carcinogenic mechanisms are poorly understood and clinical useful biomarkers are scarce. Therefore, we determined if there are quantitative patterns of molecular chaperones in the tumor tissue and circulating exosomes that may be useful in diagnosis and provide clues on their participation in carcinogenesis. Hsp27, Hsp60, Hsp70, and Hsp90 were quantified by immunohistochemistry in PC, benign goiter (BG), and normal peritumoral tissue (PT). The same chaperones were assessed in plasma exosomes from PC and BG patients before and after ablative surg…

Male0301 basic medicineGoiterdiagnosismedicine.disease_causelcsh:Chemistry0302 clinical medicinelcsh:QH301-705.5Heat-Shock ProteinsSpectroscopygoiterbiologyThyroidmolecular chaperonesGeneral MedicineMiddle Agedmolecular chaperone3. Good healthComputer Science ApplicationsBlotdiagnosimedicine.anatomical_structure030220 oncology & carcinogenesisheat shock proteins (Hsp)ImmunohistochemistryFemalethyroid gland; papillary carcinoma; molecular chaperones; heat shock proteins (Hsp); goiter; exosomes; diagnosiendocrine systemanimal structuresexosomesArticleCatalysisInorganic Chemistry03 medical and health sciencesHsp27medicineHumansEndocrine systemexosomePhysical and Theoretical ChemistryMolecular Biologythyroid glandbusiness.industryOrganic Chemistrymedicine.diseaseCarcinoma PapillaryMicrovesicles030104 developmental biologylcsh:Biology (General)lcsh:QD1-999Cancer researchbiology.proteinCarcinogenesisbusinesspapillary carcinomaInternational Journal of Molecular Sciences
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