Search results for "Fluorescent"

showing 10 items of 863 documents

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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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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Intracellular pH-dependent efflux of the fluorescent probe pyranine in the yeast Yarrowia lipolytica.

2001

International audience; 8-Hydroxypyrene-1,3,6-trisulfonic acid (pyranine) can be used as a vital intracellular pH (pH(i)) indicator. In the yeast Yarrowia lipolytica, a partial efflux of the probe was detected by using the pH-independent wavelength of 415 nm. A simplified correction of the fluorescent signals was applied, enabling to show for this species a good near-neutral pH(i) maintenance capacity in a pH 3.9 medium. Octanoic acid, which is known to have toxic effects on yeast, decreased the pH(i) and increased the 260-nm-absorbing compounds leakage. However, this acid inhibited the fluorescent probe efflux linearly with its concentration suggesting a pH(i)-dependent efflux of pyranine …

CytoplasmMESH: Hydrogen-Ion ConcentrationCell Membrane Permeability[SDV.BIO]Life Sciences [q-bio]/BiotechnologyOctanoic Acidschemistry.chemical_compoundMESH : Fluorescent DyesMESH: Cell Membrane PermeabilityArylsulfonates[INFO.INFO-BT]Computer Science [cs]/BiotechnologyMESH: ArylsulfonatesMESH : Octanoic AcidsbiologyCaprylic acidHydrogen-Ion ConcentrationMESH: Fluorescent DyesFluorescenceBiochemistryEffluxCaprylates[ INFO.INFO-BT ] Computer Science [cs]/BiotechnologyIntracellularMESH : CytoplasmIntracellular pHMESH: Biological Transport[SDV.BC]Life Sciences [q-bio]/Cellular BiologyMicrobiologyPyranineMESH : ArylsulfonatesMESH : Hydrogen-Ion ConcentrationGeneticsMESH: SaccharomycetalesMolecular Biology[SDV.BC] Life Sciences [q-bio]/Cellular BiologyFluorescent Dyes[ SDV.BC ] Life Sciences [q-bio]/Cellular BiologyMESH: Cytoplasm[ SDV.BIO ] Life Sciences [q-bio]/BiotechnologyYarrowiaBiological TransportMESH : Saccharomycetalesbiology.organism_classificationMESH: Octanoic AcidsYeast[SDV.BIO] Life Sciences [q-bio]/BiotechnologyMESH : Biological Transport[INFO.INFO-BT] Computer Science [cs]/BiotechnologychemistryMESH : Cell Membrane PermeabilitySaccharomycetales
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Identification and characterization of amphiphysin II as a novel cellular interaction partner of the hepatitis C virus NS5A protein.

2003

The hepatitis C virus (HCV) NS5A protein is highly phosphorylated by cellular protein kinases. To study how NS5A might be integrated in cellular kinase signalling, we isolated phosphoproteins from HuH-7 hepatoma cells that specifically interacted with recombinant NS5A protein. Subsequent mass spectrometry identified the adaptor protein amphiphysin II as a novel interaction partner of NS5A. Mutational analysis revealed that complex formation is primarily mediated by a proline-rich region in the C-terminal part of NS5A, which interacts with the amphiphysin II Src homology 3 domain. Importantly, we could further demonstrate specific co-precipitation and cellular co-localization of endogenous a…

CytoplasmProlinevirusesImmunoblottingNerve Tissue ProteinsHepacivirusBiologyProtein Serine-Threonine KinasesViral Nonstructural ProteinsVirus ReplicationSH3 domainVirologyTumor Cells CulturedHumansRepliconNS5AFluorescent Antibody Technique IndirectSubgenomic mRNALeucine ZippersKinasevirus diseasesSignal transducing adaptor proteinbiochemical phenomena metabolism and nutritionMAP Kinase Kinase KinasesRNA-Dependent RNA PolymeraseVirologyMolecular biologydigestive system diseasesRecombinant ProteinsViral replicationMutationPhosphorylationRepliconProtein BindingThe Journal of general virology
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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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Molecular basis of the functional distinction between Cln1 and Cln2 cyclins

2012

Cln1 and Cln2 are very similar but not identical cyclins. In this work, we tried to describe the molecular basis of the functional distinction between Cln1 and Cln2. We constructed chimeric cyclins containing different fragments of Cln1 and Cln2 and performed several functional analysis that make it possible to distinguish between Cln1 or Cln2. We identified that region between amino acids 225 and 299 of Cln2 is not only necessary but also sufficient to confer Cln2 specific functionality compared with Cln1. We also studied Cln1 and Cln2 subcellular localization identifying additional differences between them. Both cyclins are distributed between the nucleus and the cytoplasm, but Cln1 shows…

CytoplasmSaccharomyces cerevisiae ProteinsTranscription GeneticBlotting WesternGenes FungalGenetic VectorsGreen Fluorescent ProteinsActive Transport Cell NucleusSaccharomyces cerevisiaeKaryopherinsBiologyReportCyclinsGene Expression Regulation FungalmedicineAmino Acid SequenceNuclear export signalMolecular BiologyPeptide sequenceCyclinKaryopherinCell Nucleuschemistry.chemical_classificationCell Cycle CheckpointsCell BiologySubcellular localizationCell nucleusmedicine.anatomical_structureBiochemistrychemistryCytoplasmNuclear transportCDC28 Protein Kinase S cerevisiaePlasmidsDevelopmental BiologyCell Cycle
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Automatic Counting of Intra-Cellular Ribonucleo-Protein Aggregates in Saccharomyces cerevisiae Using a Textural Approach.

2019

AbstractIn the context of microbiology, recent studies show the importance of ribonucleo-protein aggregates (RNPs) for the understanding of mechanisms involved in cell responses to specific environmental conditions. The assembly and disassembly of aggregates is a dynamic process, the characterization of the stage of their evolution can be performed by the evaluation of their number. The aim of this study is to propose a method to automatically determine the count of RNPs. We show that the determination of a precise count is an issue by itself and hence, we propose three textural approaches: a classical point of view using Haralick features, a frequency point of view with generalized Fourier…

CytoplasmSaccharomyces cerevisiae ProteinsZernike polynomialsComputer scienceSaccharomyces cerevisiaeGreen Fluorescent Proteins0211 other engineering and technologiessub-cellular structuresContext (language use)02 engineering and technologySaccharomyces cerevisiaeProtein aggregationribonucleo-protein aggregatesCytoplasmic GranulesModels BiologicalPoly(A)-Binding Proteins03 medical and health sciencessymbols.namesakeProtein Aggregates[SDV.IDA]Life Sciences [q-bio]/Food engineeringGeneralized Fourier descriptorsInstrumentation030304 developmental biology021110 strategic defence & security studies0303 health sciencesFusionHaralickbiologyZernikeA proteinbiology.organism_classificationFourier transformMicroscopy FluorescenceRibonucleoproteinssymbolsBiological systemMicroscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada
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Selective targeting of avidin/mannose 6-phosphate receptor chimeras to early or late endosomes

2000

Summary In this study we have used the Semliki forest virus expression system to transiently express chimeric proteins that contain transmembrane and cytoplasmic domains of the cation-independent mannose 6-phosphate receptor (CI-MPR) fused to chicken avidin. Immunofluorescence and electron microscopy studies showed that the chimeric protein with the entire cytoplasmic domain of CI-MPR was transported to late endosomes, where it accumulated. We made use of the biotin-binding capacity of lumenal avidin, and found that, in agreement with this distribution, the chimeric protein could be labelled with biotinylated HRP endocytosed for a long, but not a brief, period of time. However, truncation o…

CytoplasmTime FactorsHistologyEndosomeRecombinant Fusion ProteinsAmino Acid MotifsGreen Fluorescent ProteinsEndosomesEndocytosisReceptor IGF Type 2Pathology and Forensic Medicine03 medical and health sciencesCationsCricetinaeAnimalsBiotinylation030304 developmental biologyProtein Synthesis Inhibitors0303 health sciencesBrefeldin AMannose 6-phosphate receptorbiologyCell Membrane030302 biochemistry & molecular biologyPovidoneBiological TransportCell BiologyGeneral MedicineAvidinSilicon DioxideSemliki forest virusFusion proteinMolecular biologyEndocytosisTransmembrane proteinProtein Structure TertiaryLuminescent ProteinsMicroscopy ElectronTransmembrane domainCross-Linking ReagentsMicroscopy FluorescenceBiotinylationbiology.proteinCattleChickensDimerizationAvidinEuropean Journal of Cell Biology
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Differential expression of Cryptosporidium parvum genes encoding sporozoite surface antigens in infected HCT-8 host cells.

2006

Intracellular replication of Cryptosporidium parvum (Apicomplexa) involves the generation of several asexual and sexual forms of the parasite. During the stage conversions, complex mechanisms lead to differential structural and functional properties of the parasite. These require a well tuned gene transcription machinery. For the first time the gene expression of four surface proteins of C. parvum sporozoites, CP15, CP17, P23, and GP900 were analysed in parallel by reverse transcription polymerase chain reaction. In addition, CP17 and P23 antigens were detected in infected host cells by immunofluorescence using antisera raised against recombinant forms of the proteins. The results show that…

CytoplasmTime FactorsTranscription GeneticImmunologyGenes ProtozoanProtozoan ProteinsFluorescent Antibody TechniqueAntigens ProtozoanBiologyImmunofluorescenceMicrobiologyApicomplexaAntigenCell Line Tumorparasitic diseasesGene expressionmedicineAnimalsHumansRNA MessengerGeneCryptosporidium parvumMembrane Glycoproteinsmedicine.diagnostic_testReverse Transcriptase Polymerase Chain Reactionbiology.organism_classificationMolecular biologyAdaptation PhysiologicalReverse transcription polymerase chain reactionInfectious DiseasesReal-time polymerase chain reactionCryptosporidium parvumGene Expression RegulationAntigens SurfaceRNA ProtozoanMicrobes and infection
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