Search results for " nucleus"

showing 10 items of 1270 documents

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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Deciliation: A stressful event for Paracentrotus lividus embryos.

1998

In this report, by using mono- and two-dimensional electrophoretic analysis, we demonstrate that deciliation on sea urchin embryos induces a stress response. Deciliation indeed causes not only the activation of ciliary subroutine, but also a transient decrease of bulk protein synthesis. This decrease is in agreement with our previous results on heat shock response in sea urchin, although deciliation does not induce the expression of the same main hsp set. We were able to characterize one main deciliation-stress protein of 40 kDa whose expression is transiently induced by deciliation and whose localisation is likely to be nuclear.

CytoplasmEmbryo NonmammalianBiophysicsBiochemistryParacentrotus lividusFight-or-flight responseMethionineStress Physiologicalbiology.animalProtein biosynthesisAnimalsRegenerationElectrophoresis Gel Two-DimensionalCiliaHeat shockMolecular BiologySea urchinCell NucleusSaline Solution HypertonicbiologyProteinsEmbryoCell BiologyGastrulaSea urchin embryobiology.organism_classificationMolecular biologyCell biologyProtein BiosynthesisSea UrchinsElectrophoresis Polyacrylamide GelBiochemical and biophysical research communications
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Translocation of cdk2 to the nucleus during G1-phase in PDGF-stimulated human fibroblasts.

1997

We studied the subcellular distribution of cdk2 in synchronized, PDGF-stimulated human fibroblasts (FH109). After contact inhibition and serum depletion, more than 95% of FH109 cells were arrested in G0/G1-phase. PDGF-AB led to a 16-fold increase in proliferation compared with untreated cells. Cell cycle progression was studied by flow cytometric analysis, [3H]thymidine incorporation, and phosphorylation of the retinoblastoma gene product, pRB. Using Western blot analysis after subcellular fractionation, we revealed that after PDGF stimulation the phosphorylated (Thr 160), i.e., activated, form of cdk2 (33 kDa) first appeared in the nucleus at late G1-phase and persisted throughout until to…

CytoplasmFluorescent Antibody TechniqueProtein Serine-Threonine KinasesmedicineCDC2-CDC28 KinasesHumansCells CulturedCell NucleusPlatelet-Derived Growth FactorbiologyKinaseCyclin-dependent kinase 2Cyclin-Dependent Kinase 2G1 PhaseContact inhibitionBiological TransportCell BiologyCell cycleFibroblastsMolecular biologyCyclin-Dependent KinasesCell biologyCell CompartmentationCytosolmedicine.anatomical_structurebiology.proteinCell fractionationNucleusPlatelet-derived growth factor receptorCyclin-Dependent Kinase-Activating KinaseExperimental cell research
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The La antigen shuttles between the nucleus and the cytoplasm in CV-1 cells

1989

Recently we established a monoclonal antibody against the La-protein (Bachmann et al., Proc. Natl. Acad. Sci. USA, 83, 7770, 1986). The antibody gives a nuclear speckled type staining and, in addition, a perinuclear cytoplasmic staining on cultured cells in immunofluorescence microscopy. After inhibition of RNA synthesis the La-protein is transported into the cytoplasm. After prolonged inhibition it returns into the nucleus forming large growing speckles. The transport into the nucleus apparently depends on glycosylation.

CytoplasmGlycosylationmedicine.drug_classClinical BiochemistryFluorescent Antibody TechniqueMonoclonal antibodyAutoantigensCell Linechemistry.chemical_compoundmedicineAnimalsMolecular BiologyCell NucleusbiologyAutoantibodyAntibodies MonoclonalCell BiologyGeneral MedicineMolecular biologyStainingMolecular Weightmedicine.anatomical_structureRibonucleoproteinschemistryCytoplasmNucleocytoplasmic Transportbiology.proteinAntibodyProtein Processing Post-TranslationalNucleusTranscription FactorsMolecular and Cellular Biochemistry
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DNA binding of L1 is required for human papillomavirus morphogenesis in vivo.

2002

AbstractThe role of putative DNA-binding domains of human papillomavirus (HPV) capsid proteins for DNA encapsidation in vivo is still unknown. We have now analyzed mutants of the major capsid protein L1 of HPV type 33, which are defective for DNA binding, for their ability to encapsidate DNA using an in vivo packaging approach. Since the DNA-binding domain and the nuclear localization signal (NLS) of L1 overlap, both a carboxy-terminal deletion mutant (L1-1/470) and a substitution mutant (L1-1/477M9) were analyzed. L1-1/477M9 has the classical NLS replaced by a noncanonical NLS taken from the human hnRNP protein A1. The mutant proteins were defective for DNA binding in contrast to wild-type…

CytoplasmHMG-boxMutantBiologyKidneypapillomavirusCell Linechemistry.chemical_compoundCapsidVirologyHumansPoint MutationDNA bindingPapillomaviridaeInfectivityCell NucleusVirus AssemblypseudovirionsL1DNA encapsidationMolecular biologyChromatinDNA-Binding ProteinschemistryCapsidCytoplasmDNA ViralchromatinDNANuclear localization sequenceVirology
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Intracellular distribution of the La antigen in CV-1 cells after herpes simplex virus type 1 infection compared with the localization of U small nucl…

1989

The La antigen is known to associate, at least transiently, with a series of small nuclear and cytoplasmic ribonucleoprotein particles (snRNPs and scRNPs), e.g. U1 and U6 snRNPs. In CV-1 cells a monoclonal antibody (MAb), directed against the La protein (La1B5), immunostained intranuclear speckles. These speckles were found to co-localize with speckles that were stained by MAbs directed against either all U snRNPs or only against U1 snRNPs. Two h after infection of CV-1 cells with herpes simplex virus type 1 (HSV-1) (strain HFEM) the staining of nuclear speckles with the anti-La MAb disappeared and the La protein was found quantitatively in the cytoplasm. In contrast nuclear speckles remain…

CytoplasmImmunoblottingFluorescent Antibody TechniqueBiologymedicine.disease_causeenvironment and public healthAutoantigensImmediate early proteinCell LineAntigenVirologymedicineHumansSimplexvirussnRNPRibonucleoproteinCell NucleusAntibodies MonoclonalRibonucleoproteins Small NuclearVirologyMolecular biologyCell nucleusHerpes simplex virusmedicine.anatomical_structureRibonucleoproteinsCytoplasmMutationSmall nuclear ribonucleoproteinTranscription FactorsThe Journal of general virology
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Dynamic intracellular survivin in oral squamous cell carcinoma: underlying molecular mechanism and potential as an early prognostic marker

2007

Survivin functions as an apoptosis inhibitor and a regulator of cell division in many tumours. The intracellular localization of survivin in tumours has been suggested as a prognostic marker. However, current reports are inconsistent and the underlying molecular mechanisms are not understood. The present study has examined the localization and prognostic value of nuclear and cytoplasmic survivin in the pre-therapeutic biopsies from 71 oral and oropharyngeal squamous carcinoma (OSCC) patients. Statistical analysis indicated that preferential nuclear versus cytoplasmic survivin correlated with favourable versus unfavourable disease outcome. Uni- and multi-variate analysis showed that in contr…

CytoplasmProgrammed cell deathPathologymedicine.medical_specialtySurvivinReceptors Cytoplasmic and NuclearApoptosisKaplan-Meier EstimateCysteine Proteinase InhibitorsKaryopherinsInhibitor of Apoptosis ProteinsPathology and Forensic MedicineCell Line TumorSurvivinBiomarkers TumorCarcinomaHumansMedicineNuclear export signalneoplasmsCell NucleusNuclear Export SignalsPredictive markerbusiness.industryCell cyclePrognosismedicine.diseaseImmunohistochemistryNeoplasm ProteinsSquamous carcinomaOropharyngeal NeoplasmsHead and Neck NeoplasmsApoptosisCarcinoma Squamous CellCancer researchMouth NeoplasmsbusinessMicrotubule-Associated ProteinsThe Journal of Pathology
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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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Cytoglobin is a respiratory protein in connective tissue and neurons, which is up-regulated by hypoxia.

2004

Cytoglobin is a recently discovered vertebrate globin distantly related to myoglobin, and its function is unknown. Here we present the first detailed analysis of the distribution and expression of cytoglobin. Northern and Western blotting experiments show the presence of cytoglobin mRNA and protein in a broad range of tissues. Quantitative PCR demonstrates an up-regulation of cytoglobin mRNA levels in rat heart and liver under hypoxic conditions (22 and 44 h of 9% oxygen). Immunofluorescence studies with three antibodies directed against different epitopes of the protein consistently show cytoglobin in connective tissue fibroblasts as well as in hepatic stellate cells. Cytoglobin is also pr…

CytoplasmRespiratory SystemFluorescent Antibody TechniqueBiochemistryMiceAntibody SpecificityChlorocebus aethiopsRespiratory functionHypoxiaNeuronsMice Inbred BALB CReverse Transcriptase Polymerase Chain ReactionCytoglobinNuclear ProteinsImmunohistochemistryGlobinsRespiratory proteinTracheamedicine.anatomical_structureLiverConnective TissueNeuroglobinRecombinant Fusion ProteinsGreen Fluorescent ProteinsMolecular Sequence DataConnective tissueBiologyTransfectionAntibodiesBone and BonesmedicineAnimalsHumansGlobinAmino Acid SequenceRNA MessengerMolecular BiologyVero CellsCell NucleusMessenger RNAMyocardiumCytoglobinCell BiologyFibroblastsMolecular biologyPeptide FragmentsRatsOxygenLuminescent ProteinsGene Expression RegulationHepatic stellate cellHeLa CellsThe Journal of biological chemistry
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Regulation of ribonucleotide reductase in response to iron deficiency

2011

Ribonucleotide reductase (RNR) is an essential enzyme required for DNA synthesis and repair. Although iron is necessary for class Ia RNR activity, little is known about the mechanisms that control RNR in response to iron deficiency. In this work, we demonstrate that yeast cells control RNR function during iron deficiency by redistributing the Rnr2–Rnr4 small subunit from the nucleus to the cytoplasm. Our data support a Mec1/Rad53-independent mechanism in which the iron-regulated Cth1/Cth2 mRNA-binding proteins specifically interact with the WTM1 mRNA in response to iron scarcity, and promote its degradation. The resulting decrease in the nuclear-anchoring Wtm1 protein levels leads to the re…

CytoplasmSaccharomyces cerevisiae ProteinsDeoxyribonucleoside triphosphateRibonucleoside Diphosphate ReductaseRNA StabilityProtein subunitSaccharomyces cerevisiaeCell Cycle ProteinsSaccharomyces cerevisiaeProtein Serine-Threonine KinasesBiologyResponse ElementsArticleTristetraprolinGene Expression Regulation FungalRibonucleotide ReductasesHumansRNA MessengerMolecular BiologyTranscription factorCell NucleusDNA synthesisIntracellular Signaling Peptides and ProteinsFungal geneticsRNA-Binding ProteinsRNA FungalIron DeficienciesCell Biologybiology.organism_classificationDNA-Binding ProteinsRepressor ProteinsCheckpoint Kinase 2Protein SubunitsProtein TransportRibonucleotide reductaseBiochemistryCytoplasmTranscription Factors
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