Search results for " CHAPERONES."

showing 10 items of 71 documents

The ribosome assembly gene network is controlled by the feedback regulation of transcription elongation

2017

Ribosome assembly requires the concerted expression of hundreds of genes, which are transcribed by all three nuclear RNA polymerases. Transcription elongation involves dynamic interactions between RNA polymerases and chromatin. We performed a synthetic lethal screening in Saccharomyces cerevisiae with a conditional allele of SPT6, which encodes one of the factors that facilitates this process. Some of these synthetic mutants corresponded to factors that facilitate pre-rRNA processing and ribosome biogenesis. We found that the in vivo depletion of one of these factors, Arb1, activated transcription elongation in the set of genes involved directly in ribosome assembly. Under these depletion c…

0301 basic medicineRibosomal ProteinsSaccharomyces cerevisiae ProteinsTranscription Elongation GeneticCèl·lulesÀcids nucleicsGene regulatory networkRibosome biogenesisSaccharomyces cerevisiaeBiologyRibosome assembly03 medical and health sciencesRegulació genèticaGeneticsGene Regulatory NetworksHistone ChaperonesRNA Processing Post-TranscriptionalGeneAdenosine TriphosphatasesFeedback PhysiologicalMessenger RNAOrganelle BiogenesisGene regulation Chromatin and EpigeneticsRNAChromatinCell biology030104 developmental biologyRNA RibosomalMutationATP-Binding Cassette TransportersOrganelle biogenesisTranscriptional Elongation FactorsSynthetic Lethal MutationsTranscriptomeRibosomes
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Functions and Therapeutic Potential of Extracellular Hsp60, Hsp70, and Hsp90 in Neuroinflammatory Disorders

2021

Neuroinflammation is implicated in central nervous system (CNS) diseases, but the molecular mechanisms involved are poorly understood. Progress may be accelerated by developing a comprehensive view of the pathogenesis of CNS disorders, including the immune and the chaperone systems (IS and CS). The latter consists of the molecular chaperones; cochaperones; and chaperone cofactors, interactors, and receptors of an organism and its main collaborators in maintaining protein homeostasis (canonical function) are the ubiquitin–proteasome system and chaperone-mediated autophagy. The CS has also noncanonical functions, for instance, modulation of the IS with induction of proinflammatory cytokines. …

0301 basic medicineamyotrophic lateral sclerosislcsh:TechnologychaperonopathiesProinflammatory cytokinelcsh:Chemistrys disease03 medical and health sciences0302 clinical medicinechaperone systemmedicineamyotrophic lateral sclerosiGeneral Materials Sciencelcsh:QH301-705.5InstrumentationchaperonotherapyNeuroinflammationFluid Flow and Transfer Processesbiologylcsh:TMechanism (biology)Process Chemistry and Technologymolecular chaperonesNeurodegenerationAutophagyGeneral EngineeringParkinson’S diseasemolecular chaperonemedicine.diseaseHuntington’ s diseaseHsp90lcsh:QC1-999Computer Science Applications030104 developmental biologylcsh:Biology (General)lcsh:QD1-999lcsh:TA1-2040multiple sclerosiChaperone (protein)Alzheimerbiology.proteinHSP60lcsh:Engineering (General). Civil engineering (General)Alzheimer’s diseaseNeurosciencelcsh:Physics030217 neurology & neurosurgeryHuntington’s diseaseApplied Sciences
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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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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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