Search results for " Cell Nucleu"

showing 10 items of 62 documents

Increased AICD generation does not result in increased nuclear translocation or activation of target gene transcription.

2008

A sequence of amyloid precursor protein (APP) cleavages culminates in the sequential release of the APP intracellular domain (AICD) and the amyloid beta peptide (Abeta) and/or p3 fragment. One of the environmental factors favouring the accumulation of AICD appears to be a rise in intracellular pH. Here we further identified the metabolism and subcellular localization of artificially expressed constructs under such conditions. We also co-examined the mechanistic lead up to the AICD accumulation and explored possible significances for its increased expression. We found that most of the AICD generated under pH neutralized conditions is likely cleaved from C83. While the AICD surplus was unable…

Transcriptional ActivationTranscription GeneticAmyloid betaActive Transport Cell NucleusCHO CellsModels BiologicalTransactivationAmyloid beta-Protein PrecursorCricetulusTranscription (biology)CricetinaeAmyloid precursor proteinAnimalsHumansLuciferaseCells CulturedRegulation of gene expressionCell NucleusbiologyCell BiologyHydrogen-Ion ConcentrationSubcellular localizationMolecular biologyCell biologyProtein Structure TertiaryCytosolbiology.proteinProtein Processing Post-TranslationalProtein BindingExperimental cell research
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Interleukin-7 matures suppressive CD127(+) forkhead box P3 (FoxP3)(+) T cells into CD127(-) CD25(high) FoxP3(+) regulatory T cells.

2011

We have identified a novel interleukin (IL)-7-responsive T cell population [forkhead box P3 (FoxP3(+) ) CD4(+) CD25(+) CD127(+) ] that is comparably functionally suppressive to conventional FoxP3(+) CD4(+) CD25(+) regulatory T cells (T(regs) ). Although IL-2 is the most critical cytokine for thymic development of FoxP3(+) T(regs) , in the periphery other cytokines can be compensatory. CD25(+) CD127(+) T cells treated with IL-7 phenotypically 'matured' into the known 'classical' FoxP3(+) CD4(+) CD25(high) CD127(-) FoxP3(+) T(regs) . In freshly isolated splenocytes, the highest level of FoxP3 expression was found in CD127(+) CD25(+) T cells when compared with CD127(-) CD25(+) or CD127(+) CD25…

Translational StudiesT cellImmunologyActive Transport Cell Nucleuschemical and pharmacologic phenomenaBiologyT-Lymphocytes RegulatoryInterleukin-7 Receptor alpha SubunitInterleukin 21MiceAntigenAntigens CDT-Lymphocyte SubsetsmedicineImmunology and AllergyCytotoxic T cellAnimalsCTLA-4 AntigenIL-2 receptorInterleukin-7 receptorCells CulturedCell NucleusMice Inbred BALB CInterleukin-7autoimmunityInterleukin-2 Receptor alpha SubunitFOXP3virus diseaseshemic and immune systemsCell DifferentiationForkhead Transcription FactorsT lymphocyteMice Inbred C57BLmedicine.anatomical_structureGene Expression RegulationImmunologyLeukocyte Common AntigensFoxP3 TregClinical and experimental immunology
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Human inducible nitric oxide synthase (iNOS) expression depends on chromosome region maintenance 1 (CRM1)- and eukaryotic translation initiation fact…

2012

Human inducible nitric oxide synthase (iNOS) is regulated on the expressional level mostly by post-transcriptional mechanisms modulating the mRNA stability. Another important step in the control of eukaryotic gene expression is the nucleocytoplasmic mRNA transport. Most cellular mRNAs are exported via the TAP/Nxt complex of proteins. However, some mRNAs are transported by a different mechanism involving the nuclear export receptor CRM1. Treatment of DLD-1 cells with the CRM1 inhibitor leptomycin B (LMB) or anti-CRM1 siRNAs reduced cytokine-induced iNOS expression. We could demonstrate that the iNOS mRNA is exported from the nucleus in a CRM1-dependent manner. Since CRM1 itself does not poss…

Untranslated regionCancer ResearchPhysiologyClinical BiochemistryActive Transport Cell NucleusNitric Oxide Synthase Type IIReceptors Cytoplasmic and NuclearKaryopherinsBiologyenvironment and public healthBiochemistryRNA TransportEukaryotic translationCell Line TumorRibavirinGene expressionP-bodiesHumansMRNA transportRNA MessengerLuciferasesNuclear export signalAnalysis of VarianceMessenger RNAfungiEIF4EMolecular biologyEukaryotic Initiation Factor-4Elipids (amino acids peptides and proteins)Nitric Oxide
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Cytoplasmic Parvovirus Capsids Recruit Importin Beta for Nuclear Delivery

2019

Parvoviruses are an important platform for gene and cancer therapy. Their cell entry and the following steps, including nuclear import, are inefficient, limiting their use in therapeutic applications. Two models exist on parvoviral nuclear entry: the classical import of the viral capsid using nuclear transport receptors of the importin (karyopherin) family or the direct attachment of the capsid to the nuclear pore complex leading to the local disintegration of the nuclear envelope. Here, by laser scanning confocal microscopy and in situ proximity ligation analyses combined with coimmunoprecipitation, we show that infection requires importin β-mediated access to the nuclear pore complex and …

alpha KaryopherinsCytoplasmNuclear EnvelopevirusesImmunologyActive Transport Cell NucleusImportinKaryopherinsBiologyVirus ReplicationMicrobiologyCell LineParvoviridae InfectionsParvovirus03 medical and health sciencesCapsidCytosolViral entryVirologyAnimalsNuclear pore030304 developmental biologyKaryopherinCell Nucleuschemistry.chemical_classification0303 health sciencesNucleoplasm030302 biochemistry & molecular biologyVirus Internalizationbeta KaryopherinsVirus-Cell InteractionsCell biologychemistryCytoplasmInsect ScienceNuclear PoreCapsid ProteinsNucleoporinNuclear transportJournal of Virology
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The increase in maternal expression of axin1 and axin2 contribute to the zebrafish mutant ichabod ventralized phenotype.

2014

β-Catenin is a central effector of the Wnt pathway and one of the players in Ca(+)-dependent cell-cell adhesion. While many wnts are present and expressed in vertebrates, only one β-catenin exists in the majority of the organisms. One intriguing exception is zebrafish that carries two genes for β-catenin. The maternal recessive mutation ichabod presents very low levels of β-catenin2 that in turn affects dorsal axis formation, suggesting that β-catenin1 is incapable to compensate for β-catenin2 loss and raising the question of whether these two β-catenins may have differential roles during early axis specification. Here we identify a specific antibody that can discriminate selectively for β-…

axin1axin2zebrafish mutant ichabodMessengerEmbryonic DevelopmentBiochemistryBETA-CATENINAxin2-RGS DOMAINAxin ProteinAntibody SpecificitySettore BIO/10 - BiochimicaAnimalsAxin2-RGS DOMAIN; AXIS FORMATION; BETA-CATENIN; Wnt signaling; ZEBRAFISH; Animals; Antibody Specificity; Axin Protein; Blastula; Cell Nucleus; Embryonic Development; Female; Gene Expression Regulation Developmental; Genes Dominant; Immunohistochemistry; Lithium Chloride; Mutation; Phenotype; Protein Stability; Protein Transport; RNA Messenger; Signal Transduction; Up-Regulation; Zebrafish; Zebrafish Proteins; beta Catenin; Biochemistry; Cell Biology; Molecular BiologyDevelopmentalDominantRNA MessengerMolecular BiologyZebrafishbeta CateninGenes DominantAXIS FORMATIONCell NucleusProtein StabilityGene Expression Regulation DevelopmentalCell BiologyBlastulaZebrafish ProteinsWnt signalingImmunohistochemistryUp-RegulationProtein TransportPhenotypeGene Expression RegulationGenesMutationRNAFemaleLithium ChlorideSignal Transduction
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Phosphorylation of mismatch repair proteins MSH2 and MSH6 affecting MutSα mismatch-binding activity

2002

Mismatch repair (MMR) is involved in the removal of mispaired bases from DNA and thus plays an important role in the maintenance of genomic stability and the prevention of mutations and cancer. Moreover, MMR triggers genotoxicity and apoptosis upon processing of DNA lesions such as O6-methylguanine. Whereas the enzymology of MMR has been elucidated in great detail, only limited data are available concerning its regulation. Here we show that the major mismatch-binding proteins MSH2 and MSH6, forming the MutSalpha complex, are phosphorylated in vitro by protein kinase C and casein kinase II, but not by protein kinase A. Phosphorylation of MSH2 and MSH6 was also found within the cell, with MSH…

congenital hereditary and neonatal diseases and abnormalitiesDNA RepairDNA repairBase Pair MismatchMacromolecular SubstancesActive Transport Cell NucleusBiologyProtein Serine-Threonine KinasesArticleProto-Oncogene ProteinsGeneticsHumansProtein phosphorylationPhosphorylationProtein kinase ACasein Kinase IIneoplasmsProtein kinase CProtein Kinase CCell Nucleusnutritional and metabolic diseasesdigestive system diseasesDNA-Binding ProteinsMutS Homolog 2 ProteinBiochemistryMSH2PhosphorylationDNA mismatch repairCasein kinase 2HeLa Cells
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Nuclear entry and egress of parvoviruses.

2022

Parvoviruses are small non-enveloped single-stranded DNA viruses, which depend on host cell nuclear transcriptional and replication machinery. After endosomal exposure of nuclear localization sequence and a phospholipase A2 domain on the capsid surface, and escape into the cytosol, parvovirus capsids enter the nucleus. Due to the small capsid diameter of 18–26 nm, intact capsids can potentially pass into the nucleus through nuclear pore complexes (NPCs). This might be facilitated by active nuclear import, but capsids may also follow an alternative entry pathway that includes activation of mitotic factors and local transient disruption of the nuclear envelope. The nuclear entry is followed b…

import and exportCell NucleusisäntäsolutviruksetparvovirusesNuclear Envelopenuclear pore complexesnucleusActive Transport Cell NucleusDNA Single-Strandednuclear envelopeVirus ReplicationMicrobiologyinfektiotParvovirusPhospholipasestumaNuclear PoreCapsid ProteinsMolecular BiologyparvoviruksetkapsidiMolecular microbiologyREFERENCES
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Stromal Interaction Molecule 1 (STIM1) Is Involved in the Regulation of Mitochondrial Shape and Bioenergetics and Plays a Role in Oxidative Stress

2012

Calcium ions are involved in a plethora of cellular functions including cell death and mitochondrial energy metabolism. Store-operated Ca(2+) entry over the plasma membrane is activated by depletion of intracellular Ca(2+) stores and is mediated by the sensor STIM1 and the channel ORAI1. We compared cell death susceptibility to oxidative stress in STIM1 knock-out and ORAI1 knockdown mouse embryonic fibroblasts and in knock-out cells with reconstituted wild type and dominant active STIM1. We show that STIM1 and ORAI1 deficiency renders cells more susceptible to oxidative stress, which can be rescued by STIM1 and ORAI1 overexpression. STIM1 knock-out mitochondria are tubular, have a higher Ca…

inorganic chemicalsProgrammed cell deathORAI1 ProteinEukaryotic Initiation Factor-2Active Transport Cell NucleusApoptosisMitochondrionBiologymedicine.disease_causeBiochemistryMiceeIF-2 KinasemedicineAnimalsStromal Interaction Molecule 1PhosphorylationMolecular BiologyTranscription factorCells CulturedMice KnockoutEIF-2 kinaseMembrane GlycoproteinsEndoplasmic reticulumMolecular Bases of DiseaseSTIM1Cell BiologyFibroblastsEmbryo MammalianMitochondriaCell biologyOxidative Stressbiology.proteinCalciumCalcium ChannelsEnergy MetabolismIntracellularOxidative stressJournal of Biological Chemistry
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The estrogen receptor α:insulin receptor substrate 1 complex in breast cancer: structure–function relationships

2007

Background: Insulin receptor substrate 1 (IRS-1) is a signaling molecule that exerts a key role in mediating cross talk between estrogen receptor a (ERa) and insulin-like growth factor 1 (IGF-1) in breast cancer cells. Previously, we demonstrated that a fraction of IRS-1 binds ERa, translocates to the nucleus, and modulates ERa-dependent transcription at estrogen response elements (ERE). Here, we studied structure-function relationships of the ER-a:IRS-1 complex under IGF-1 and/or estradiol (E 2 ) stimulation. Materials and methods: ERa and IRS-1 deletion mutants were used to analyze structural and functional ERα/IRS-1 interactions. IRS-1 binding to ERE and IRS-1 role in ERa-dependent ERE t…

medicine.medical_specialtyInsulin Receptor Substrate ProteinsActive Transport Cell NucleusEstrogen receptorRepressorBreast NeoplasmsBiologyStructure-Activity Relationshipestrogen receptor alpha (ERa) Insulin receptor substrate 1 (IRS-1) breast cancerCell Line TumorInternal medicineCoactivatormedicineHumansInsulin-Like Growth Factor IReceptors InterferonEstradiolEstrogen Receptor alphaHematologyDNA-binding domainPhosphoproteinsPeptide FragmentsReceptor InsulinProtein Structure TertiaryCell biologyIRS1Repressor ProteinsPleckstrin homology domainEndocrinologyOncologyInsulin Receptor Substrate ProteinsFemaleChromatin immunoprecipitationProtein BindingAnnals of Oncology
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Synergistic effects of fluticasone propionate and salmeterol on in vitro T-cell activation and apoptosis in asthma

2004

Background In asthma T cells are characterized by an increased activation state and by reduced apoptosis. Objective Because the clinical efficacy of inhaled corticosteroids combined with long-acting β 2 -agonists has been widely demonstrated in asthma, we studied, in vitro , the effect of fluticasone propionate (FP) and salmeterol alone and in combination on the activation and apoptosis of peripheral blood T cells (PBTs), on the expression of phosphorylated nuclear factor κB inhibitor (IκBα), and on the nuclear translocation of glucocorticoid receptor (GR) in PBTs from asthmatic subjects. Methods Apoptosis was evaluated on the basis of annexin V binding, whereas the expression of caspases 8…

medicine.medical_specialtyProgrammed cell deathAdolescentT cellT-LymphocytesImmunologyActive Transport Cell NucleusApoptosisAndrostadienes; Active Transport Cell Nucleus; NF-kappa B; Apoptosis; Humans; Albuterol; Receptors Glucocorticoid; Asthma; Child; Caspases; Lymphocyte Activation; Phosphorylation; I-kappa B Proteins; Adolescent; Drug Synergism; T-LymphocytesLymphocyte ActivationGlucocorticoid receptorReceptors GlucocorticoidNF-KappaB Inhibitor alphaAnnexinInternal medicinemedicineHumansImmunology and AllergyAlbuterolPhosphorylationChildSalmeterol XinafoateAndrostadieneChemistryActive Transport Cell NucleuNF-kappa BApoptosiDrug SynergismCaspaseAsthmaAndrostadienesIκBαEndocrinologymedicine.anatomical_structureApoptosisCaspasesFluticasoneI-kappa B ProteinI-kappa B ProteinsSalmeterolGlucocorticoidmedicine.drugHuman
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