Search results for "Molecular chaperones."

showing 10 items of 61 documents

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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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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Ionic self-complementarity induces amyloid-like fibril formation in an isolated domain of a plant copper metallochaperone protein

2004

This article is available from: http://www.biomedcentral.com/1472-6807/4/7

BioquímicaSerum Amyloid A Proteinendocrine systemArabidopsis ProteinsProtein ConformationMolecular Sequence DataOsmolar ConcentrationArabidopsisBiological TransportProtein Structure Secondarylcsh:Biology (General)Amino Acid SequencePeptidesProteïneslcsh:QH301-705.5CopperMolecular ChaperonesResearch Article
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Inhibition of miR-21 restores RANKL/OPG ratio in multiple myeloma-derived bone marrow stromal cells and impairs the resorbing activity of mature oste…

2015

// Maria Rita Pitari 1 , Marco Rossi 1 , Nicola Amodio 1 , Cirino Botta 1 , Eugenio Morelli 1 , Cinzia Federico 1 , Annamaria Gulla 1 , Daniele Caracciolo 1 , Maria Teresa Di Martino 1 , Mariamena Arbitrio 2 , Antonio Giordano 3, 4 , Pierosandro Tagliaferri 1 , Pierfrancesco Tassone 1, 4 1 Department of Experimental and Clinical Medicine and T. Campanella Cancer Center, Magna Graecia University, S. Venuta University Campus, Catanzaro, Italy 2 ISN-CNR, Roccelletta di Borgia, Catanzaro, Italy 3 Department of Human Pathology and Oncology, University of Siena, Siena, Italy 4 Sbarro Institute for Cancer Research and Molecular Medicine, Center for Biotechnology, College of Science and Technology,…

Bone diseaseMessengerOsteoclastsTumor Microenvironment3' Untranslated RegionsMultiple myelomaTumorbiologyMesenchymal Stromal CellsRANKLProtein Inhibitors of Activated STATUp-Regulationmedicine.anatomical_structureOncologyRANKLmiRNAsmiR-21MiRNAMultiple MyelomaMiR-21; MiRNAs; Multiple myeloma bone disease; OPG; RANKL; 3' Untranslated Regions; Bone Marrow Cells; Bone Resorption; Cell Adhesion; Cell Line Tumor; Coculture Techniques; HEK293 Cells; Humans; Interleukin-6; Lentivirus; Mesenchymal Stromal Cells; MicroRNAs; Molecular Chaperones; Multiple Myeloma; Osteoclasts; Osteoprotegerin; Protein Inhibitors of Activated STAT; RANK Ligand; RNA Messenger; STAT3 Transcription Factor; Stromal Cells; Tumor Microenvironment; Up-Regulation; OncologyResearch Papermusculoskeletal diseasesSTAT3 Transcription FactorStromal cellBone Marrow CellsBone resorptionCell LineOsteoprotegerinCell Line TumormedicineCell AdhesionHumansRNA MessengerBone Resorptionbusiness.industryInterleukin-6LentivirusRANK LigandOsteoprotegerinMesenchymal Stem Cellsmedicine.diseaseMolecular medicineCoculture TechniquesMicroRNAsmultiple myeloma bone diseaseHEK293 CellsImmunologyCancer researchbiology.proteinRNAOPGBone marrowStromal CellsbusinessMolecular ChaperonesOncotarget
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Brain Tumor-Derived Extracellular Vesicles as Carriers of Disease Markers: Molecular Chaperones and MicroRNAs

2020

Primary and metastatic brain tumors are usually serious conditions with poor prognosis, which reveal the urgent need of developing rapid diagnostic tools and efficacious treatments. To achieve these objectives, progress must be made in the understanding of brain tumor biology, for example, how they resist natural defenses and therapeutic intervention. One resistance mechanism involves extracellular vesicles that are released by tumors to meet target cells nearby or distant via circulation and reprogram them by introducing their cargo. This consists of different molecules among which are microRNAs (miRNAs) and molecular chaperones, the focus of this article. miRNAs modify target cells in the…

Brain tumorBiologyDiagnostic toolsExtracellular vesicleslcsh:Technologydiagnostic toolslcsh:Chemistry03 medical and health sciences0302 clinical medicineImmune systemmicroRNAmedicineGeneral Materials ScienceInstrumentationlcsh:QH301-705.5030304 developmental biologymiRNAFluid Flow and Transfer ProcessesDiagnostic tool0303 health sciencesMechanism (biology)lcsh:TProcess Chemistry and TechnologyVesiclemolecular chaperonesGeneral Engineeringmedicine.diseaselcsh:QC1-999Computer Science ApplicationsCell biologyBrain tumorlcsh:Biology (General)lcsh:QD1-999lcsh:TA1-2040030220 oncology & carcinogenesisDrug deliverydrug deliverybrain tumorsExtracellular vesicleextracellular vesicleslcsh:Engineering (General). Civil engineering (General)lcsh:PhysicsApplied Sciences
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Allogeneic effector/memory Th-1 cells impair FoxP3+ regulatory T lymphocytes and synergize with chaperone-rich cell lysate vaccine to treat leukemia

2011

AbstractTherapeutic strategies combining the induction of effective antitumor immunity with the inhibition of the mechanisms of tumor-induced immunosuppression represent a key objective in cancer immunotherapy. Herein we demonstrate that effector/memory CD4+ T helper-1 (Th-1) lymphocytes, in addition to polarizing type-1 antitumor immune responses, impair tumor-induced CD4+CD25+FoxP3+ regulatory T lymphocyte (Treg) immunosuppressive function in vitro and in vivo. Th-1 cells also inhibit the generation of FoxP3+ Tregs from naive CD4+CD25−FoxP3− T cells by an interferon-γ–dependent mechanism. In addition, in an aggressive mouse leukemia model (12B1), Th-1 lymphocytes act synergistically with …

Cell Extractsmedicine.medical_treatmentBlotting WesternImmunologyMice NudeEnzyme-Linked Immunosorbent Assaychemical and pharmacologic phenomenaMice SCIDBiologyCancer VaccinesT-Lymphocytes RegulatoryBiochemistryInterferon-gammaMiceLymphocytes Tumor-InfiltratingImmune systemCancer immunotherapyAntigenTumor Cells CulturedmedicineAnimalsInterferon gammaIL-2 receptorImmunobiologyMice Inbred BALB CLeukemia ExperimentalFOXP3hemic and immune systemsForkhead Transcription FactorsDendritic CellsT-Lymphocytes Helper-InducerCell BiologyHematologyT lymphocyteFlow Cytometrymedicine.diseaseMice Inbred C57BLLeukemiaImmunologyImmunologic MemoryMolecular ChaperonesT-Lymphocytes Cytotoxicmedicine.drugBlood
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Differential regulation of the clusterin gene by Ha-ras and c-myc oncogenes and during apoptosis

1998

Clusterin (ApoJ) is an extracellular glycoprotein expressed during processes of tissue differentiation and regression that involve programmed cell death (apoptosis). Increased clusterin expression has also been found in tumors, however, the mechanism underlying this induction is not known. Apoptotic processes in tumors could be responsible for clusterin gene activation. Alternatively, oncogenic mutations could modulate signal transduction, thereby inducing the gene. We examined the response of the rat clusterin gene to two oncogenes, Ha-ras and c-myc, in transfected Rat1 fibroblasts. While c-myc overexpression did not modify clusterin gene activity, the Ha-ras oncogene produced a seven to t…

Cell signalingProgrammed cell deathUltraviolet RaysPhysiologyRecombinant Fusion ProteinsClinical BiochemistryGenes mycApoptosisDNA FragmentationBiologyTransfectionProto-Oncogene Proteins c-mycProto-Oncogene Proteins p21(ras)AnimalsRNA MessengerCell Line TransformedGlycoproteinsOncogeneClusterinCell CycleCell BiologyTransfectionFibroblastsCell cycleeye diseasesRatsClusterinGenes rasApoptosisMutationCancer researchbiology.proteinsense organsSignal transductionMolecular ChaperonesSignal TransductionJournal of Cellular Physiology
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Multiple signal transduction pathways regulate clusterin (gp 80) gene expression in MDCK cells

1996

ABSTRACT Clusterin (gp 80, apolipoprotein J, TRPM-2) is a widely expressed multifunctional glycoprotein. Its demonstrated and proposed functions include the transport of lipids and membrane fragments, the inhibition of the cytolytic action of the terminal complement complex and the modulation of cell—cell interactions. The expression of the gene is enhanced during tissue injury and remodelling and by hormone-withdrawal-induced apoptosis of prostate and mammary cells. We show here that, in the kidney-derived epithelial cell line MDCK, clusterin mRNA is repressed by glucocorticoids and by progesterone. Treatment with epidermal growth factor also represses clusterin gene expression in MDCK cel…

Cell typeTranscription GeneticKidneyDexamethasoneEpitheliumCell LineAlkaloidsDogsEndocrinologyEpidermal growth factor1-Methyl-3-isobutylxanthineGene expressionCyclic AMPAnimalsRNA MessengerEnzyme InhibitorsAldosteroneMolecular BiologyProgesteroneProtein Kinase CProtein kinase CGlycoproteinsBenzophenanthridinesMessenger RNAEpidermal Growth FactorClusterinbiologyChemistryMolecular biologyeye diseasesPhenanthridinesCell biologyKineticsClusterinCell culturebiology.proteinTetradecanoylphorbol Acetatesense organsSignal transductionMolecular ChaperonesSignal TransductionJournal of Molecular Endocrinology
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The effect of cadmium on brain cells in culture

2009

Cadmium is a long-living heavy metal, abundantly present in the environment, which accumulates in the body. In this study, we investigated the effects of cadmium on the expression of molecular chaperones, and of certain cell-specific proteins, in a variety of brain cell types in culture, namely primary cultures of rat cortical neurons and astrocytes, a brain capillary endothelial cell line (RB4E.B cells), and pheochromocytoma cells (PC12), induced or not to differentiate by NGF treatment. The metal induces a dose-dependent increase of Hsp70 in all cell types. Responses to the metal are cell-specific in the case of Hsc70 and Hsp90: i) in astrocytes, as well as in PC12 cells, cadmium has no s…

Cell typecadmium brain cells molecular chaperones PIPPinCell SurvivalCellBlotting Westernchemistry.chemical_elementNerve Tissue ProteinsBiologyPC12 CellsSettore BIO/10 - BiochimicaNerve Growth FactorGeneticsmedicineAnimalsCytoskeletonCell ShapeCells CulturedFluorescent DyesCerebral CortexNeuronsCadmiumBrainEndothelial CellsRNA-Binding ProteinsCell DifferentiationGeneral MedicineCell cycleMolecular biologyHsp70Cell biologyRatsEndothelial stem cellmedicine.anatomical_structurechemistryApoptosisAstrocytesCadmiumMolecular Chaperones
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