Search results for " Cell Nucleus"

showing 10 items of 62 documents

Mid-region parathyroid hormone-related protein (PTHrP) binds chromatin of MDA-MB231 breast cancer cells and isolated oligonucleotides “in vitro”

2006

We have previously shown that PTHrP(38-94)-amide restrains growth and invasion "in vitro", causes striking toxicity and accelerates death of some breast cancer cell lines, the most responsive being MDA-MB231 whose tumorigenesis was also attenuated "in vivo". PTHrP(38-94)-amide contains the domain implicated in the nuclear import of PTHrP. Although the nucleus was identified as a destination for mid-region PTHrP, evidence for direct DNA-binding capability is lacking to date. Here, we examined the localization of PTHrP(38-94)-amide within MDA-MB231 cells and within metaphase spread preparations and characterized its DNA-binding properties, employing a combination of immunocytochemical, cytoge…

Cancer ResearchBreast cancer DNA-binding PTHrPCellActive Transport Cell NucleusOligonucleotidesDNA footprintingBreast NeoplasmsBiologymedicine.disease_causeModels BiologicalMagneticsIn vivoCell Line TumormedicineHumansSettore BIO/06 - Anatomia Comparata E Citologiaskin and connective tissue diseasesMetaphaseCell NucleusGenomeParathyroid hormone-related proteinParathyroid Hormone-Related ProteinDNAChromatinIn vitroChromatinCell biologySettore BIO/18 - Geneticamedicine.anatomical_structureOncologyCancer researchNuclear transportPeptidesCarcinogenesishormones hormone substitutes and hormone antagonistsProtein Binding
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Involvement of protein kinase Cdelta in contact-dependent inhibition of growth in human and murine fibroblasts.

2001

There is evidence that protein kinase C delta (PKCdelta) is a tumor suppressor, although its physiological role has not been elucidated so far. Since important anti-proliferative signals are mediated by cell-cell contacts we studied whether PKCdelta is involved in contact-dependent inhibition of growth in human (FH109) and murine (NIH3T3) fibroblasts. Cell-cell contacts were imitated by the addition of glutardialdehyde-fixed cells to sparsely seeded fibroblasts. Downregulation of the PKC isoforms alpha, delta, epsilon, and mu after prolonged treatment with 12-O-tetradecanoylphorbol-13-acetate (TPA, 0.1 microM) resulted in a significant release from contact-inhibition in FH109 cells. Bryosta…

Cancer ResearchTime FactorsBryostatin 1ImmunoprecipitationActive Transport Cell NucleusDown-RegulationBiologychemistry.chemical_compoundFixativesLactonesMiceDownregulation and upregulationGeneticsmedicineAnimalsHumansProtein IsoformsBenzopyransEnzyme InhibitorsFibroblastProtein kinase AMolecular BiologyProtein kinase CProtein Kinase CChemotaxisCell CycleAcetophenones3T3 CellsFibroblastsBryostatinsMolecular biologyBlotIsoenzymesProtein Kinase C-deltamedicine.anatomical_structurechemistryGlutaralTetradecanoylphorbol AcetateMacrolidesMitogensRottlerinCell DivisionProtein BindingOncogene
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Cargo transport through the nuclear pore complex at a glance.

2021

ABSTRACT Bidirectional transport of macromolecules across the nuclear envelope is a hallmark of eukaryotic cells, in which the genetic material is compartmentalized inside the nucleus. The nuclear pore complex (NPC) is the major gateway to the nucleus and it regulates nucleocytoplasmic transport, which is key to processes including transcriptional regulation and cell cycle control. Accordingly, components of the nuclear transport machinery are often found to be dysregulated or hijacked in diseases. In this Cell Science at a Glance article and accompanying poster, we provide an overview of our current understanding of cargo transport through the NPC, from the basic transport signals and mach…

Cell Nucleus0303 health sciencesBidirectional transportNuclear EnvelopeActive Transport Cell NucleusCell BiologyBiologyCell biologyNuclear Pore Complex Proteins03 medical and health sciences0302 clinical medicinemedicine.anatomical_structureEukaryotic CellsNucleocytoplasmic TransportCell cycle controlmedicineTranscriptional regulationNuclear PoreNuclear transportMultivalent bindingNuclear poreNucleus030217 neurology & neurosurgery030304 developmental biologyJournal of cell science
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Survivin’s Dual Role: An Export’s View

2007

Survivin is proposed to function as a mitotic regulator and an apoptosis inhibitor during development and pathogenesis. As such, survivin has aroused keen interest in disparate areas of basic and translational research. Survivin acts as a subunit of the chromosomal passenger complex (CPC), composed of the mitotic kinase Aurora-B, Borealin and INCENP, and is essential for proper chromosome segregation and cytokinesis. Our recent findings indicate that the nuclear export receptor Crm1 is critically involved in tethering the CPC to the centromere by interacting with a leucine-rich nuclear export signal (NES), evolutionary conserved in all mammalian survivin proteins. In addition, the survivin/…

Cell NucleusApoptosis InhibitorINCENPSurvivinActive Transport Cell NucleusCell BiologyCell cycleBiologyInhibitor of Apoptosis ProteinsNeoplasm ProteinsCell biologySurvivinAnimalsHumansNuclear export signalMicrotubule-Associated ProteinsneoplasmsMolecular BiologyMitosisCytokinesisNuclear localization sequenceDevelopmental BiologyCell Cycle
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Aryl hydrocarbon receptor activation by cAMP vs. dioxin: divergent signaling pathways.

2005

Even before the first vertebrates appeared on our planet, the aryl hydrocarbon receptor ( AHR ) gene was present to carry out one or more critical life functions. The vertebrate AHR then evolved to take on functions of detecting and responding to certain classes of environmental toxicants. These environmental pollutants include polycyclic aromatic hydrocarbons (e.g., benzo[ a ]pyrene), polyhalogenated hydrocarbons, dibenzofurans, and the most potent small-molecular-weight toxicant known, 2,3,7,8-tetrachlorodibenzo- p -dioxin (TCDD or dioxin). After binding of these ligands, the activated AHR translocates rapidly from the cytosol to the nucleus, where it forms a heterodimer with aryl hydroc…

Conservation of Natural ResourcesAryl hydrocarbon receptor nuclear translocatorPolychlorinated DibenzodioxinsTime FactorsTranscription GeneticGenetic VectorsGreen Fluorescent ProteinsImmunoblottingActive Transport Cell NucleusEnvironmentDioxinsLigandschemistry.chemical_compoundMiceCytosolGenes ReporterCell Line TumorCyclic AMPAnimalsImmunoprecipitationReceptorFluorescent Antibody Technique IndirectCell NucleusMultidisciplinarybiologyChemistryColforsinEndogenous mediatorrespiratory systemBiological SciencesAryl hydrocarbon receptorCyclic AMP-Dependent Protein KinasesCytosolProtein TransportBiochemistryBucladesineMicroscopy FluorescenceReceptors Aryl HydrocarbonSecond messenger systembiology.proteinProstaglandinsEnvironmental PollutantsSignal transductionDimerizationToxicantPlasmidsProtein BindingSignal TransductionProceedings of the National Academy of Sciences of the United States of America
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Nuclear and Cytoplasmic Survivin: Molecular Mechanism, Prognostic, and Therapeutic Potential.

2007

Abstract Survivin's proposed dual role as an apoptosis inhibitor and a mitotic effector positioned it in the front line of cancer research. Notably, survivin is detected as a cytoplasmic and nuclear protein in cancer patients, which stimulated numerous studies to investigate and to speculate on the functional and prognostic significance of its dynamic localization. Recent evidence shows that the direct interaction of survivin with the nuclear export receptor Crm1 is critically involved in its intracellular localization and cancer-relevant functions. Here, we review our current understanding of the Crm1/survivin interface and discuss its potential prognostic and therapeutic relevance. [Cance…

CytoplasmCancer ResearchPathologymedicine.medical_specialtyApoptosis InhibitorSurvivinActive Transport Cell NucleusMitosisReceptors Cytoplasmic and NuclearKaryopherinsBiologyModels BiologicalInhibitor of Apoptosis ProteinsNeoplasmsSurvivinmedicineHumansNuclear proteinNuclear export signalReceptorMitosisCell NucleusEffectorCancerPrognosismedicine.diseaseNeoplasm ProteinsGene Expression Regulation NeoplasticOncologyCancer researchMicrotubule-Associated ProteinsBiologie
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Glutathione is recruited into the nucleus in early phases of cell proliferation.

2007

We have studied the possible correlation between nuclear glutathione distribution and the progression of the cell cycle. The former was studied by confocal microscopy using 5-chloromethyl fluorescein diacetate and the latter by flow cytometry and protein expression of Id2 and p107. In proliferating cells, when 41% of them were in the S+G(2)/M phase of the cell cycle GSH was located mainly in the nucleus. When cells reached confluence (G(0)/G(1)) GSH was localized in the cytoplasm with a perinuclear distribution. The nucleus/cytoplasm fluorescence ratio for GSH reached a maximal mean value of 4.2 +/- 0.8 at 6 h after cell plating. A ratio higher than 2 was maintained during exponential cell …

CytoplasmCellActive Transport Cell NucleusRetinoblastoma-Like Protein p107BiologyBiochemistry3T3 cellsFlow cytometrychemistry.chemical_compoundMicemedicineAnimalsMolecular BiologyInhibitor of Differentiation Protein 2Cell NucleusMicroscopy Confocalmedicine.diagnostic_testCell growthCell CycleCell BiologyGlutathione3T3 CellsCell cycleFlow CytometryMolecular biologyGlutathioneCell biologymedicine.anatomical_structurechemistryGene Expression RegulationCytoplasmNucleusThe Journal of biological chemistry
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Nuclear Translocation of Mismatch Repair Proteins MSH2 and MSH6 as a Response of Cells to Alkylating Agents

2000

Mammalian mismatch repair has been implicated in mismatch correction, the prevention of mutagenesis and cancer, and the induction of genotoxicity and apoptosis. Here, we show that treatment of cells specifically with agents inducing O(6)-methylguanine in DNA, such as N-methyl-N'-nitro-N-nitrosoguanidine and N-methyl-N-nitrosourea, elevates the level of MSH2 and MSH6 and increases GT mismatch binding activity in the nucleus. This inducible response occurs immediately after alkylation, is long-lasting and dose-dependent, and results from translocation of the preformed MutSalpha complex (composed of MSH2 and MSH6) from the cytoplasm into the nucleus. It is not caused by an increase in MSH2 gen…

CytoplasmDNA RepairBase Pair MismatchRNA StabilityChromosomal translocationmedicine.disease_causeBiochemistrychemistry.chemical_compoundMismatch Repair Endonuclease PMS2Adenosine TriphosphatasesNuclear ProteinsMethylnitrosoureaNeoplasm ProteinsDNA-Binding ProteinsMutS Homolog 2 ProteinDNA mismatch repairMutL Protein Homolog 1Protein BindingAlkylating AgentsMethylnitronitrosoguanidinecongenital hereditary and neonatal diseases and abnormalitiesGuanineActive Transport Cell NucleusBiologyCell LineO(6)-Methylguanine-DNA MethyltransferaseProto-Oncogene ProteinsDNA Repair ProteinmedicineHumansRNA MessengerneoplasmsMolecular BiologyAdaptor Proteins Signal TransducingCell NucleusMutagenesisnutritional and metabolic diseasesDNACell BiologyDNA MethylationMolecular biologydigestive system diseasesMSH6DNA Repair EnzymesGene Expression RegulationchemistryMSH2Carrier ProteinsGenotoxicityDNADNA DamageHeLa CellsJournal of Biological Chemistry
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Multifunctionality of F-rich nucleoporins

2020

Nucleoporins (Nups) represent a range of proteins most known for composing the macromolecular assembly of the nuclear pore complex (NPC). Among them, the family of intrinsically disordered proteins (IDPs) phenylalanine-glycine (FG) rich Nups, form the permeability barrier and coordinate the high-speed nucleocytoplasmic transport in a selective way. Those FG-Nups have been demonstrated to participate in various biological processes besides nucleocytoplasmic transport. The high number of accessible hydrophobic motifs of FG-Nups potentially gives rise to this multifunctionality, enabling them to form unique microenvironments. In this review, we discuss the multifunctionality of disordered and …

CytoplasmProtein FoldingDNA RepairPhenylalanineAmino Acid MotifsActive Transport Cell NucleusGlycineIntrinsically disordered proteinsBiochemistryArticle03 medical and health sciences0302 clinical medicineAnimalsHumansCell LineageCiliaNuclear pore030304 developmental biologyCell Nucleus0303 health sciencesChemistryNeurodegenerative DiseasesIntrinsically Disordered ProteinsNuclear Pore Complex ProteinsMacromolecular assemblyProtein TransportGene Expression RegulationNucleocytoplasmic TransportNuclear PoreBiophysicsNucleoporinHydrophobic and Hydrophilic Interactions030217 neurology & neurosurgeryBiological networkBiochemical Society Transactions
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The Yeast RNA Polymerase II-associated Factor Iwr1p Is Involved in the Basal and Regulated Transcription of Specific Genes

2009

RNA polymerase II (RNA pol II) is a multisubunit enzyme that requires many auxiliary factors for its activity. Over the years, these factors have been identified using both biochemical and genetic approaches. Recently, the systematic characterization of protein complexes by tandem affinity purification and mass spectroscopy has allowed the identification of new components of well established complexes, including the RNA pol II holoenzyme. Using this approach, a novel and highly conserved factor, Iwr1p, that physically interacts with most of the RNA pol II subunits has been described in yeast. Here we show that Iwr1p genetically interacts with components of the basal transcription machinery …

CytoplasmSaccharomyces cerevisiae ProteinsTranscription GeneticActive Transport Cell NucleusRNA polymerase IISaccharomyces cerevisiaeBiologyBiochemistryPhosphatesFungal ProteinsGene Expression Regulation FungalTranscription Chromatin and EpigeneticsPromoter Regions GeneticMolecular BiologyRNA polymerase II holoenzymeGeneticsModels Geneticbeta-FructofuranosidaseGeneral transcription factorCell BiologyCell biologyKineticsGene Expression RegulationMicroscopy FluorescenceMutationbiology.proteinTranscription factor II FRNA Polymerase IITranscription factor II ETranscription factor II DCarrier ProteinsTranscription factor II BTranscription factor II AJournal of Biological Chemistry
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