Search results for "Molecular Chaperone"

showing 10 items of 117 documents

The Arabidopsis heavy metal P-type ATPase HMA5 interacts with metallochaperones and functions in copper detoxification of roots

2005

*† ‡ § Summary Since copper (Cu) is essential in key physiological oxidation reactions, organisms have developed strategies for handling Cu while avoiding its potentially toxic effects. Among the tools that have evolved to cope with Cu is a network of Cu homeostasis factors such as Cu-transporting P-type ATPases that play a key role in transmembrane Cu transport. In this work we present the functional characterization of an Arabidopsis Cutransporting P-type ATPase, denoted heavy metal ATPase 5 (HMA5), and its interaction with Arabidopsis metallochaperones. HMA5 is primarily expressed in roots, and is strongly and specifically induced by Cu in whole plants. We have identified and characteriz…

ATPaseMolecular Sequence DataMutantArabidopsisPlant ScienceGenes PlantPlant RootsMetallochaperonesArabidopsisGeneticsAmino Acid SequenceRNA MessengerDNA PrimersAdenosine TriphosphatasesBase SequenceSequence Homology Amino AcidbiologyArabidopsis ProteinsCell BiologyCompartmentalization (fire protection)biology.organism_classificationTransmembrane proteinCell biologyBiochemistryChaperone (protein)biology.proteinP-type ATPaseCopperMolecular ChaperonesThe Plant Journal
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Heat shock protein-27 protects human bronchial epithelial cells against oxidative stress-mediated apoptosis: possible implication in asthma.

2002

Inflammation of the human bronchial epithelium, as observed in asthmatics, is characterized by the selective death of the columnar epithelial cells, which desquamate from the basal cells. Tissue repair initiates from basal cells that resist inflammation. Here, we have evaluated the extent of apoptosis as well as the Hsp27 level of expression in epithelial cells from bronchial biopsy samples taken from normal and asthmatic subjects. Hsp27 is a chaperone whose expression protects against oxidative stress. We report that in asthmatic subjects the basal epithelium cells express a high level of Hsp27 but no apoptotic morphology. In contrast, apoptotic columnar cells are devoid of Hsp27 expressio…

Adultendocrine systemanimal structuresHSP27 Heat-Shock ProteinsInflammationApoptosisBronchiColumnar CellRespiratory MucosaBiologymedicine.disease_causeBiochemistryGene Expression Regulation EnzymologicHsp27Heat shock proteinmedicineBronchial BiopsyHumansHeat-Shock ProteinsEpithelial CellsCell BiologyHydrogen PeroxideOriginal ArticlesMiddle AgedOxidantsEpitheliumAsthmaCell biologyNeoplasm ProteinsOxidative Stressmedicine.anatomical_structureApoptosisImmunologybiology.proteinmedicine.symptomOxidative stressMolecular ChaperonesCell stresschaperones
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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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Chaperonopathies of senescence and the scrambling of interactions between the chaperoning and the immune systems.

2010

Aging entails progressive deterioration of molecules and supramolecular structures, including Hsp chaperones and their complexes, paralleled by functional decline. Recent research has changed our views on Hsp chaperones. They work inside and outside cells in many locations, alone or forming teams, interacting with cells, receptors, and molecules that are not chaperones, in roles that are not typically attributed to chaperones, such as protein folding. Hsp chaperones form a physiological system with a variety of functions and interactions with other systems, for example, the immune system. We propose that chaperone malfunctioning due to structural damage or gene dysregulation during aging ha…

AgingProtein Foldingchaperonopathies by mistakeSettore BIO/16 - Anatomia Umanachaperoning systemImmune Systemchaperoning system interactionchaperonopathieCarrier Proteinschaperonotherapy Hsp60Molecular ChaperonesAnnals of the New York Academy of Sciences
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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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Incipient genome erosion and metabolic streamlining for antibiotic production in a defensive symbiont

2021

Significance Genome reduction is commonly observed in bacteria of several phyla engaging in obligate nutritional symbioses with insects. In Actinobacteria, however, little is known about the process of genome evolution, despite their importance as prolific producers of antibiotics and their increasingly recognized role as defensive partners of insects and other organisms. Here, we show that “Streptomyces philanthi,” a defensive symbiont of digger wasps, has a G+C-enriched genome in the early stages of erosion, with inactivating mutations in a large proportion of genes, causing dependency on its hosts for certain nutrients, which was validated in axenic symbiont cultures. Additionally, overe…

Arthropod Antennaeprotective mutualismEvolutionWaspsBeewolfGenomicsProteomicsGenomeStreptomyces03 medical and health sciencesdefensive symbiosis418AnimalsSymbiosisGene030304 developmental biologyGenetics0303 health sciencesMultidisciplinarybiologyObligate030306 microbiologyHost (biology)fungiBiological Sciencesbiology.organism_classificationStreptomycesAnti-Bacterial Agentsgenome erosionAphidsCommentarybacteriaFemalepseudogenizationGenome BacterialPseudogenesMolecular Chaperones
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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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