Search results for "Heat-Shock Protein"

showing 10 items of 310 documents

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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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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Characterization of small HSPs from Anemonia viridis reveals insights into molecular evolution of alpha crystallin genes among cnidarians.

2014

Gene family encoding small Heat-Shock Proteins (sHSPs containing α-crystallin domain) are found both in prokaryotic and eukaryotic organisms; however, there is limited knowledge of their evolution. In this study, two small HSP genes termed AvHSP28.6 and AvHSP27, both organized in one intron and two exons, were characterised in the Mediterranean snakelocks anemone Anemonia viridis. The release of the genome sequence of Hydra magnipapillata and Nematostella vectensis enabled a comprehensive study of the molecular evolution of α-crystallin gene family among cnidarians. Most of the H. magnipapillata sHSP genes share the same gene organization described for AvHSP28.6 and AvHSP27, differing from …

LipopolysaccharidesMarine and Aquatic SciencesGene ExpressionCnidarianSea anemoneGenomeAnemoniaGene duplicationProtein Isoformsalpha-CrystallinsPhylogenyGenomic organizationGeneticsMultidisciplinarybiologyReverse Transcriptase Polymerase Chain ReactionQTemperatureRMedicineAnemonia viridiSmall HSP; Anemonia viridis; Cnidarians; molecular evolutionResearch ArticleScienceMolecular Sequence DataMarine BiologySmall HSPEvolution MolecularCnidariaSpecies SpecificityMolecular evolutionMetals HeavySequence Homology Nucleic AcidAnimalsGene familyAmino Acid SequenceMolecular BiologyGeneEvolutionary BiologyBase SequenceSequence Homology Amino Acidmolecular evolutionGene Expression ProfilingEcology and Environmental SciencesBiology and Life SciencesAquatic EnvironmentsCell Biologybiology.organism_classificationHeat-Shock Proteins SmallSea AnemonesEarth SciencesPLoS ONE
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Heat shock response in yeast involver changes in both transcription rates and mRNA stabilities

2011

We have analyzed the heat stress response in the yeast Saccharomyces cerevisiae by determining mRNA levels and transcription rates for the whole transcriptome after a shift from 25uC to 37uC. Using an established mathematical algorithm, theoretical mRNA decay rates have also been calculated from the experimental data. We have verified the mathematical predictions for selected genes by determining their mRNA decay rates at different times during heat stress response using the regulatable tetO promoter. This study indicates that the yeast response to heat shock is not only due to changes in transcription rates, but also to changes in the mRNA stabilities. mRNA stability is affected in 62% of …

Llevat de cervesaTranscription GeneticEstrès oxidatiuRNA StabilitySaccharomyces cerevisiaeGene Expressionlcsh:MedicineYeast and Fungal ModelsRNA-binding proteinSaccharomyces cerevisiaeModels BiologicalGenètica molecularModel OrganismsTranscripció genèticaGenome Analysis ToolsTranscription (biology)Gene Expression Regulation FungalYeastsHeat shock proteinMolecular Cell BiologyGeneticsCluster AnalysisRNA MessengerHeat shocklcsh:ScienceBiologyGeneTranscription factorHeat-Shock ProteinsMultidisciplinaryBase SequenceOrganisms Genetically ModifiedbiologySystems Biologylcsh:RRNA FungalLlevats -- GenèticaGenomicsbiology.organism_classificationMolecular biologyFunctional GenomicsCell biologyRegulonRNAlcsh:QGenome Expression AnalysisHeat-Shock ResponseResearch ArticleTranscription Factors
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HSPH1 inhibition downregulates Bcl-6 and c-Myc and hampers the growth of human aggressive B-cell non-Hodgkin lymphoma

2015

We have shown that human B-cell non-Hodgkin lymphomas (B-NHLs) express heat shock protein (HSP)H1/105 in function of their aggressiveness. Here, we now clarify its role as a functional B-NHL target by testing the hypothesis that it promotes the stabilization of key lymphoma oncoproteins. HSPH1 silencing in 4 models of aggressive B-NHLs was paralleled by Bcl-6 and c-Myc downregulation. In vitro and in vivo analysis of HSPH1-silenced Namalwa cells showed that this effect was associated with a significant growth delay and the loss of tumorigenicity when 10(4) cells were injected into mice. Interestingly, we found that HSPH1 physically interacts with c-Myc and Bcl-6 in both Namalwa cells and pr…

Lymphoma B-CellXenograft Model Antitumor AssayDNA-Binding ProteinImmunologyDown-RegulationMice SCIDSettore MED/08 - Anatomia PatologicaBiologyBiochemistryHSP110 Heat-Shock ProteinProto-Oncogene Proteins c-mycMiceDownregulation and upregulationimmune system diseasesCell Line Tumorhemic and lymphatic diseasesHeat shock proteinGene Knockdown TechniquesmedicineAnimalsHumansGene silencingHSP110 Heat-Shock ProteinsAnimals; Cell Line Tumor; DNA-Binding Proteins; Down-Regulation; Gene Knockdown Techniques; HSP110 Heat-Shock Proteins; Humans; Lymphoma B-Cell; Mice; Mice SCID; Proto-Oncogene Proteins c-myc; Xenograft Model Antitumor Assays; Biochemistry; Immunology; Medicine (all); Hematology; Cell BiologyAnimalMedicine (all)Cell BiologyHematologymedicine.diseaseXenograft Model Antitumor AssaysIn vitroLymphomaDNA-Binding ProteinsCell cultureGene Knockdown TechniquesGene Knockdown TechniqueImmunologyProto-Oncogene Proteins c-bcl-6Cancer researchB-Cell Non-Hodgkin LymphomaHumanBlood
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Heat shock proteins in fibrosis and wound healing: Good or evil?

2014

Heat shock proteins (HSPs) are key regulators of cell homeostasis, and their cytoprotective role has been largely investigated in the last few decades. However, an increasing amount of evidence highlights their deleterious effects on several human pathologies, including cancer, in which they promote tumor cell survival, proliferation and drug resistance. Therefore, HSPs have recently been suggested as therapeutic targets for improving human disease outcomes. Fibrotic diseases and cancer share several properties; both pathologies are characterized by genetic alterations, uncontrolled cell proliferation, altered cell interactions and communication and tissue invasion. The discovery of new HSP…

MAPK/ERK pathwayPulmonary FibrosisCellApoptosisBiologyCell Physiological PhenomenaTransforming Growth Factor beta1PathogenesisFibrosisNeoplasmsHeat shock proteinmedicineHumansHSP70 Heat-Shock ProteinsPharmacology (medical)HSP90 Heat-Shock ProteinsHSP110 Heat-Shock ProteinsHSP47 Heat-Shock ProteinsHeat-Shock ProteinsPharmacologyWound HealingCell growthCancerEndomyocardial Fibrosismedicine.diseaseFibrosisHeat-Shock Proteins Smallmedicine.anatomical_structureImmunologyCancer researchCollagenWound healingPharmacology & Therapeutics
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In vitro effect of cadmium and copper on separated blood leukocytes of Dicentrarchus labrax.

2013

The immunotoxic effects of heavy metals on blood leukocytes of sea bass (Dicentrarchus labrax) were examined. The cells, separated by a discontinuous Percoll-gradients, were exposed in vitro to various sublethal concentrations of cadmium and copper (10(-7) M, 10(-5) M, and 10(-3) M) and their immunotoxic effect was then evaluated by measuring neutral red uptake, MU assay, DNA fragmentation and Hsp70 gene expression. First of all, we demonstrated that the cells treated in vitro could incorporate Cd and Cu. A relationship between heavy metal exposure and dose-time-dependent alterations in responses of leukocytes from blood was found for both metals, but copper was more immunotoxic than cadmiu…

MTTNeutral redMembrane permeabilityHealth Toxicology and MutagenesisSettore BIO/05 - Zoologiachemistry.chemical_elementNRchemistry.chemical_compoundReal-time-PCRLeukocytesAnimalsMTT assayHSP70 Heat-Shock ProteinsCytotoxicityCadmiumHeavy metal; Leukocytes; NR; MTT; Hsp70 gene; Real-time-PCRbiologyPublic Health Environmental and Occupational HealthGeneral MedicineLeukocytebiology.organism_classificationPollutionMolecular biologyIn vitroHeavy metalchemistryGene Expression RegulationNeutral RedImmunologyHsp70 geneDNA fragmentationDicentrarchusBassCopperWater Pollutants ChemicalCadmium
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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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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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