Search results for "HSP70 Heat-Shock Protein"

showing 10 items of 115 documents

Oncolytic parvovirus H1 induces release of heat-shock protein HSP72 in susceptible human tumor cells but may not affect primary immune cells.

2003

Certain autonomous parvoviruses preferentially replicate in and kill in vitro-transformed cells and may reduce the incidence of spontaneous and implanted tumors in animals. Hence, these viruses and their derivatives are currently under evaluation as antitumor vectors. However, the mechanisms underlying their tumor-suppressing properties are not yet understood. We asked whether the lytic parvovirus H1 may enhance the immunogenicity of infected tumor cells. Out of human melanoma and gastrointestinal tumor cells, we selected the cell line SK29-Mel-1 being very susceptible to H1-induced apoptotic killing. Here, no upregulation of HLA class I and costimulatory molecules could be observed followi…

Cancer ResearchTime FactorsCell SurvivalGenetic VectorsApoptosisHSP72 Heat-Shock ProteinsVirusParvovirusImmune systemCell Line TumorHumansHSP70 Heat-Shock ProteinsTransgenesMolecular BiologyMelanomaCells CulturedHeat-Shock ProteinsbiologyParvovirusImmunogenicityHSC70 Heat-Shock Proteinsbiology.organism_classificationVirologyOncolytic virusUp-RegulationCell killingViral replicationCell cultureCancer researchMolecular MedicineCarrier ProteinsCancer gene therapy
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1267 HSP70-2 polymorphism as a risk factor for carotid plaque rupture and cerebral ischaemia in old type 2 diabetes-atherosclerotic patients.

2005

Patients with type 2 diabetes mellitus (NIDDM) are at risk for macrovascular disease complications, such as myocardial infarction (MI) or stroke from plaque rupture. Cytokines play a key role in plaque vulnerability. IFN-gamma inhibits collagen synthesis thereby affecting plaque stability. High IL-6, TNF-alpha, and dyslipidemia are risk factors for thrombosis. Abnormal increments of HSP70 in atherosclerotic plaques might lead to plaque instability and rupture caused by chronic inflammation, which up-regulates the expression of pro-inflammatory cytokines (IL-6 and TNF-alpha) in human monocytes. Studies of a polymorphic PstI site lying in the coding region at position 1267 of the HSP70-2 gene…

Carotid Artery DiseasesMaleAgingmedicine.medical_specialtyGenotypeArteriosclerosisType 2 diabetesGastroenterologyBrain IschemiaInterferon-gammaGene FrequencyRisk FactorsInternal medicinemedicineHumansCarotid StenosisHSP70 Heat-Shock ProteinsMyocardial infarctionRNA MessengerAllelesTriglyceridesMacrovascular diseaseAgedGlycated HemoglobinRupturePolymorphism Geneticbusiness.industryInterleukin-6Tumor Necrosis Factor-alphaType 2 Diabetes MellitusOdds ratioCholesterol LDLMiddle Agedmedicine.diseaseThrombosisEndocrinologyCarotid ArteriesDiabetes Mellitus Type 2Relative riskFemalebusinessDyslipidemiaDevelopmental BiologyMechanisms of ageing and development
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Melanoma-Reactive Class I-Restricted Cytotoxic T Cell Clones Are Stimulated by Dendritic Cells Loaded with Synthetic Peptides, but Fail to Respond to…

2003

Abstract Immunization with heat shock proteins (hsp) isolated from cancer cells has been shown to induce a protective antitumor response. The mechanism of hsp-dependent cellular immunity has been attributed to a variety of immunological activities mediated by hsp. Hsp have been shown to bind antigenic peptides, trim the bound peptides by intrinsic enzymatic activity, improve endocytosis of the chaperoned peptides by APCs, and enhance the ability of APCs to stimulate peptide-specific T cells. We have investigated the potential capacity of hsp70 and gp96 to function as a mediator for Ag-specific CTL stimulation in an in vitro model for human melanoma. Repetitive stimulation of PBLs by autolog…

Cellular immunityT cellImmunologyAntigen-Presenting CellsEpitopes T-LymphocyteBiologyLymphocyte ActivationEpitopeInterferon-gammaMART-1 AntigenAntigenAntigens NeoplasmCell Line TumorHLA-A2 AntigenmedicineHumansImmunology and AllergyCytotoxic T cellHSP70 Heat-Shock ProteinsLymphocyte CountAntigen-presenting cellMelanomaHeat-Shock ProteinsCell Line TransformedAntigen PresentationMonophenol MonooxygenaseDendritic CellsMolecular biologyCoculture TechniquesClone CellsNeoplasm ProteinsUp-RegulationCTL*medicine.anatomical_structureCancer cellK562 CellsPeptidesT-Lymphocytes CytotoxicThe Journal of Immunology
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Mitochondrial compartment: a possible target of cadmium effects on breast epithelial cells.

2009

Cadmium–breast epithelial cell interactions were studied by analyzing some mitochondria-related aspects of stress response. We treated immortalized non-tumor breast cells with 5 or 50 μM CdCl2 for 24 or 96 h demonstrating that the exposure did not cause a significant mitochondrial proliferation, while it induced a significant increase in the respiratory activity and mitochondrial polarization. In addition, we found that hsp60 was up-regulated while hsp70 and COXII and COXIV were down-regulated. The mRNA for hsp70 remained constant and only the inducible form of the 70-kDa heat shock protein was over expressed. The mRNAs for COXII and COXIV remained constant after 24 h and increased after lo…

Clinical chemistryCadmium - Mitochondria - Stress - Breast EpithelialClinical BiochemistryCell RespirationMitochondrionBiologyCell LineElectron Transport Complex IVHeat shock proteinmedicineHumansHSP70 Heat-Shock ProteinsBreastCytotoxicityMolecular BiologyMembrane Potential MitochondrialMessenger RNAMembranesDose-Response Relationship DrugEpithelial CellsCell BiologyGeneral MedicineChaperonin 60EpitheliumCell biologyHsp70Mitochondriamedicine.anatomical_structureGene Expression RegulationHSP60FemaleCadmium
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Heat shock and Cd2+ exposure regulate PML and Daxx release from ND10 by independent mechanisms that modify the induction of heat-shock proteins 70 an…

2003

Nuclear domains called ND10 or PML bodies might function as nuclear depots by recruiting or releasing certain proteins. Although recruitment of proteins through interferon-induced upregulation and SUMO-1 modification level of PML had been defined, it is not known whether release of proteins is regulated and has physiological consequences. Exposure to sublethal environmental stress revealed a sequential release of ND10-associated proteins. Upon heat shock Daxx and Sp100 were released but PML remained, whereas exposure to subtoxic concentrations of CdCl2 induced the release of ND10-associated proteins, including PML, with Sp100 remaining in a few sites. In both cases,recovery times were simil…

Co-Repressor ProteinsMAP Kinase Signaling SystemMacromolecular SubstancesSUMO-1 ProteinPromyelocytic Leukemia ProteinMicePromyelocytic leukemia proteinDeath-associated protein 6Stress PhysiologicalHeat shock proteinEndopeptidasesAnimalsHSP70 Heat-Shock ProteinsEnzyme InhibitorsHeat shockTranscription factorCells CulturedHeat-Shock ProteinsbiologyTumor Suppressor ProteinsIntracellular Signaling Peptides and ProteinsNuclear ProteinsCell BiologyCell Nucleus StructuresNeoplasm ProteinsCell biologyHsp70Cysteine EndopeptidasesEukaryotic CellsGene Expression RegulationImmunologybiology.proteinSignal transductionCarrier ProteinsCo-Repressor ProteinsHeat-Shock ResponseCadmiumMolecular ChaperonesTranscription FactorsJournal of Cell Science
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Decipher the mechanisms of protein conformational changes induced by nucleotide binding through free-energy landscape analysis: ATP binding to Hsp70.

2013

ATP regulates the function of many proteins in the cell by transducing its binding and hydrolysis energies into protein conformational changes by mechanisms which are challenging to identify at the atomic scale. Based on molecular dynamics (MD) simulations, a method is proposed to analyze the structural changes induced by ATP binding to a protein by computing the effective free-energy landscape (FEL) of a subset of its coordinates along its amino-acid sequence. The method is applied to characterize the mechanism by which the binding of ATP to the nucleotide-binding domain (NBD) of Hsp70 propagates a signal to its substrate-binding domain (SBD). Unbiased MD simulations were performed for Hsp…

Conformational changeProtein ConformationAllosteric regulationPlasma protein bindingMolecular Dynamics SimulationCellular and Molecular NeuroscienceProtein structureAdenosine TriphosphateGeneticsHSP70 Heat-Shock ProteinsMolecular Biologylcsh:QH301-705.5Nuclear Magnetic Resonance BiomolecularEcology Evolution Behavior and SystematicsEcologybiologyChemistryEscherichia coli ProteinsEnergy landscapeComputational Theory and MathematicsBiochemistrylcsh:Biology (General)Docking (molecular)Modeling and SimulationChaperone (protein)Biophysicsbiology.proteinBinding domainProtein BindingResearch ArticlePLoS computational biology
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Nuclear Translocation of Papillomavirus Minor Capsid Protein L2 Requires Hsc70

2004

ABSTRACT Minor capsid protein L2 of papillomaviruses plays an essential role in virus assembly by recruiting viral components to PML bodies, the proposed sites of virus morphogenesis. We demonstrate here that the function of L2 in virus assembly requires the chaperone Hsc70. Hsc70 was found dispersed in naturally infected keratinocytes and cultured cells. A dramatic relocation of Hsc70 from the cytoplasm to PML bodies was induced in these cells by L2 expression. Hsc70-L2 complex formation was confirmed by coimmunoprecipitation. The complex was modulated by the cochaperones Hip and Bag-1, which stabilize and destabilize Hsc70-substrate complexes, respectively. Cytoplasmic depletion of Hsc70 …

Cytoplasmanimal structuresImmunoprecipitationvirusesImmunologyActive Transport Cell Nucleusmacromolecular substancesBiologyMicrobiologyVirusGreen fluorescent proteinCell Line TumorVirologyAnimalsHSP70 Heat-Shock ProteinsCOS cellsHSC70 Heat-Shock ProteinsVirionOncogene Proteins ViralMolecular biologyVirus-Cell InteractionsTransport proteinCell biologyProtein TransportCapsidCytoplasmInsect ScienceChaperone (protein)COS Cellsembryonic structuresbiology.proteinCapsid ProteinsJournal of Virology
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Heat shock protein-antigen fusions lose their enhanced immunostimulatory capacity after endotoxin depletion.

2008

Heat shock proteins (HSPs) induce cross-presentation of antigens by dendritic cells (DC) as well as DC maturation. These properties make HSP antigen complexes good candidates to prime CD8 T cell responses against tumor-associated antigens. In this study, we analyzed four different members of the HSP70 family fused to a fragment of ovalbumin (OVA) as a model tumor antigen. E. coli-derived recombinant HSP70-OVA fusion proteins efficiently primed antigen-specific cytotoxic T cells in short-term in vivo immunization assays. Because of concerns that the adjuvant effect of HSPs may be due to endotoxin contamination, we studied this issue in detail. Induction of OVA-specific cytotoxicity was signi…

Cytotoxicity ImmunologicCpG OligodeoxynucleotideOvalbuminRecombinant Fusion ProteinsImmunologyReceptors Antigen T-CellMice TransgenicBiologyCD8-Positive T-LymphocytesLymphocyte ActivationMiceImmune systemCross-PrimingAntigenAdjuvants ImmunologicHeat shock proteinNeoplasmsCytotoxic T cellAnimalsHSP70 Heat-Shock ProteinsAntigensMolecular BiologyTLR9Dendritic CellsMolecular biologyFusion proteinTumor antigenEndotoxinsMice Inbred C57BLOligodeoxyribonucleotidesT-Lymphocytes CytotoxicMolecular immunology
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Enhanced susceptibility to cytotoxic T lymphocytes without increase of MHC class I antigen expression after conditional overexpression of heat shock …

1999

Antigenic peptides have been found associated with heat shock proteins (HSP) including cytoplasmic HSP70 and heat shock cognate protein 70 as well as the endoplasmic reticulum-resident glucose-regulated protein 94. Recently, HSP70 transfection has been reported to increase MHC class I cell surface expression and antigen presentation on mouse melanoma B16 cells (Wells et al., Int. Immunol. 1998. 10: 609). To analyze the effect of HSP70 on MHC class I cell surface expression and lysability of target cells we transfected a human melanoma cell line with the rat Hsp70-1 gene using the Tet-On system for conditional overexpression of HSP70. Induction of HSP70 did not increase cell surface expressi…

Cytotoxicity ImmunologicT-LymphocytesImmunologyAntigen presentationCD1BiologyMajor histocompatibility complexMajor Histocompatibility ComplexMiceMHC class ITumor Cells CulturedImmunology and AllergyCytotoxic T cellAnimalsHumansHSP70 Heat-Shock ProteinsMelanomaAntigen PresentationAntigen processingMHC class I antigenGene Transfer TechniquesMHC restrictionMolecular biologyRatsGene Expression Regulation Neoplasticbiology.proteinEuropean journal of immunology
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Induction of DNA strand breaks and expression of HSP70 and GRP78 homolog by cadmium in the marine sponge Suberites domuncula

1998

The marine sponge Suberites domuncula was used as a bioindicator to study the effects of cadmium on the occurrence of DNA strand breakage and on the induction of the expression of the stress biomarkers, heat shock protein 70 (HSP70) and glucose-regulated protein 78 (GRP78) homolog. The cDNA encoding GRP78 homolog from S. domuncula was isolated and characterized. The GRP78 cDNA has a length of 2.1 kb and displays characteristic features of the HSP70 family ; it encodes an aa sequence of M-r 72, 000. Exposure of S. domuncula to 1 mg/L of cadmium chloride for 24 h caused a strong(16.6-fold) increase in cadmium content to 7.7 mu g/g wet weight of sponge tissue ; after an incubation period of 6 …

DNA damageHealth Toxicology and MutagenesisMolecular Sequence Datachemistry.chemical_elementCadmium chlorideToxicologyIncubation periodchemistry.chemical_compoundCadmium ChlorideGlucose-regulated protein. Heat-shock proteins. Geodia-cydonium.Mediterranean SeaAnimalsHSP70 Heat-Shock ProteinsAmino Acid SequenceNorthern blotIncubationHeat-Shock ProteinsCadmiumGreeceSequence Homology Amino AcidbiologyEcologyDNAGeneral Medicinebiology.organism_classificationPollutionMolecular biologyPoriferaHsp70Suberites domunculaZincchemistryWater Pollutants ChemicalDNA DamageMutagens
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