Search results for "Fluorescence"

showing 10 items of 2463 documents

Truncated TrkB receptor-induced outgrowth of dendritic filopodia involves the p75 neurotrophin receptor.

2004

The Trk family of receptor tyrosine kinases and the p75 receptor (p75NTR) mediate the effects of neurotrophins on neuronal survival, differentiation and synaptic plasticity. The neurotrophin BDNF and its cognate receptor tyrosine kinase, TrkB.FL, are highly expressed in neurons of the central nervous system. At later stages in postnatal development the truncated TrkB splice variants (TrkB.T1, TrkB.T2) become abundant. However, the signalling and function of these truncated receptors remained largely elusive.We show that overexpression of TrkB.T1 in hippocampal neurons induces the formation of dendritic filopodia, which are known precursors of synaptic spines. The induction of filopodia by T…

Time FactorsGreen Fluorescent ProteinsReceptors Nerve Growth FactorTropomyosin receptor kinase ATransfectionTropomyosin receptor kinase CHippocampusModels BiologicalPC12 CellsReceptor Nerve Growth FactorReceptor tyrosine kinaseLow-affinity nerve growth factor receptorAnimalsReceptor trkBNerve Growth FactorsPseudopodiaCloning MolecularNeuronsbiologyDose-Response Relationship Drugmusculoskeletal neural and ocular physiologyCell DifferentiationCell BiologyDendritesImmunohistochemistryDendritic filopodiaCell biologyProtein Structure TertiaryRatsnervous systemMicroscopy FluorescenceTrk receptorembryonic structuresNeurotrophin bindingCOS Cellsbiology.proteinsense organsNeurotrophinProtein BindingSignal TransductionJournal of cell science
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Induction of apoptosis in human osteosarcoma Saos-2 cells by the proteasome inhibitor MG132 and the protective effect of pRb

2003

Induction of apoptosis in human osteosarcoma Saos-2 cells by the proteasome inhibitor MG132 and the protective effect of pRb

Time FactorsLeupeptinsApoptosisRetinoblastoma ProteinAntioxidantsAmino Acid Chloromethyl KetonesMembrane Potentialschemistry.chemical_compoundSettore BIO/10 - BiochimicaMG132Caspase 8OsteosarcomaChemistryCaspase 3Cytochromes cFlow CytometryMitochondriaCysteine EndopeptidasesProto-Oncogene Proteins c-bcl-2CaspasesOsteosarcomamedicine.drugmusculoskeletal diseasesProteasome Endopeptidase ComplexCell SurvivalBlotting Westernbcl-X Proteinmacromolecular substancesTransfectionMultienzyme ComplexesCell Line Tumorparasitic diseasesmedicineHumansProtease InhibitorsneoplasmsMolecular BiologySaos-2 cellsDose-Response Relationship DrugCell Biologymedicine.diseaseAcetylcysteineApoptosis osteosarcoma proteasome inhibitorsMicroscopy FluorescenceApoptosisCancer researchProteasome inhibitorTumor Suppressor Protein p53Reactive Oxygen Specieshuman activities
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Excited State Dynamics in Recombinant Water-Soluble Chlorophyll Proteins (WSCP) from Cauliflower Investigated by Transient Fluorescence Spectroscopy

2008

The present study describes the fluorescence emission properties of recombinant water-soluble chlorophyll (Chl) protein (WSCP) complexes reconstituted with either Chl a or Chl b alone (Chl a only or Chl b only WSCP, respectively) or mixtures of both pigments at different stoichiometrical ratios. Detailed investigations were performed with time and space correlated ps fluorescence spectroscopy within the temperature range from 10 to 295 K. The following points were found: (a) The emission spectra at room temperature (295 K) are well characterized by bands with a dominating Lorentzian profile broadened due to phonon scattering and peak positions located at 677, 684 and 693 nm in the case of C…

Time FactorsLight-Harvesting Protein ComplexesTemperatureAnalytical chemistryWaterBrassicaAtmospheric temperature rangeFluorescenceRecombinant ProteinsSpectral lineFluorescence spectroscopySurfaces Coatings and FilmsPigmentchemistry.chemical_compoundSpectrometry FluorescenceSolubilitychemistryvisual_artExcited stateChlorophyllMaterials Chemistryvisual_art.visual_art_mediumEmission spectrumPhysical and Theoretical ChemistryPlant ProteinsThe Journal of Physical Chemistry B
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The effect of long-chain bases on polysialic acid-mediated membrane interactions

2011

AbstractNegatively-charged polysialic acid (polySia) chains are usually membrane-bound and are often expressed on the surface of neuroinvasive bacterial cells, neural cells, and tumor cells. PolySia can mediate both repulsive and attractive cis interactions between membrane components, and trans interactions between membranes. Positively-charged long-chain bases are widely present in cells, are often localized in membranes and can function as bioactive lipids. Here we use Langmuir monolayer technique, fluorescence spectroscopy and electron microscopy of lipid vesicles to study the role of a simple long-chain base, octadecylamine (ODA), in both cis and trans interactions mediated by polySia …

Time FactorsLipid BilayersBiophysicsPolysialic acidPhospholipid monolayerBiochemistryFluorescenceMembrane LipidsMicroscopy Electron TransmissionMonolayerPressureElectron microscopyMoleculeAminesLipid bilayerLiposomeModels StatisticalChemistryPolysialic acidVesicleCell MembraneOctadecylamineCell BiologyHydrogen-Ion ConcentrationHydrocarbonsLiposomeMicroscopy ElectronSpectrometry FluorescenceMembraneBiochemistryLiposomesPhosphatidylcholinesSialic AcidsBiophysicsThermodynamicsCis–trans isomerismBiochimica et Biophysica Acta (BBA) - Biomembranes
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Cholesterol Modulates the Interaction of β-Amyloid Peptide with Lipid Bilayers

2009

The interaction of an amphiphilic, 40-amino acid beta-amyloid (Abeta) peptide with liposomal membranes as a function of sterol mole fraction (X(sterol)) was studied based on the fluorescence anisotropy of a site-specific membrane sterol probe, dehydroergosterol (DHE), and fluorescence resonance energy transfer (FRET) from the native Tyr-10 residue of Abeta to DHE. Without Abeta, peaks or kinks in the DHE anisotropy versus X(sterol) plot were detected at X(sterol) approximately 0.25, 0.33, and 0.53. Monomeric Abeta preserved these peaks/kinks, but oligomeric Abeta suppressed them and created a new DHE anisotropy peak at X(sterol) approximately 0.38. The above critical X(sterol) values coinci…

Time FactorsLipid BilayersMolecular Sequence DataBiophysicsPeptideFluorescence Polarization7. Clean energy03 medical and health scienceschemistry.chemical_compound0302 clinical medicineAlzheimer DiseaseErgosterolFluorescence Resonance Energy TransferAmino Acid SequenceLipid bilayer030304 developmental biologychemistry.chemical_classification0303 health sciencesLiposomeAmyloid beta-PeptidesChemistryCholesterolSterolPeptide FragmentsCrystallographyFörster resonance energy transferMembraneCholesterolCell BiophysicsTyrosinelipids (amino acids peptides and proteins)030217 neurology & neurosurgeryFluorescence anisotropyProtein BindingBiophysical Journal
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De novo formation of cytokeratin filament networks originates from the cell cortex in A-431 cells

2001

Of the three major cytoskeletal filament systems, the intermediate filaments are the least understood. Since they differ fundamentally from the actin- and microtubulebased networks by their lack of polarity, it has remained a mystery how and where these principally endless filaments are formed. Using a recently established epithelial cell system in which fluorescently labeled intermediate filaments of the cytokeratin type can be monitored in living cells, we address these issues. By multidimensional time-lapse fluorescence microscopy, we examine de novo intermediate filament network formation from non-filamentous material at the end of mitosis and show that it mirrors disassembly. It is dem…

Time FactorsNeurofilamentGreen Fluorescent ProteinsMitosisArp2/3 complexmacromolecular substancesModels BiologicalCell LineProtein filamentStructural BiologyCell cortexTumor Cells CulturedHumansPhosphorylationCytoskeletonIntermediate filamentMicroscopy VideoDose-Response Relationship DrugbiologyCell BiologyCell biologyLuminescent ProteinsTreadmillingMicroscopy Fluorescencebiology.proteinKeratinsCell DivisionCytokinesisProtein BindingCell Motility and the Cytoskeleton
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Desmosomes: interconnected calcium-dependent structures of remarkable stability with significant integral membrane protein turnover

2002

Desmosomes are prominent cell adhesion structures that are major stabilizing elements, together with the attached cytoskeletal intermediate filament network, of the cytokeratin type in epithelial tissues. To examine desmosome dynamics in tightly coupled cells and in situations of decreased adhesion, fluorescent desmosomal cadherin desmocollin 2a (Dsc2a) chimeras were stably expressed in human hepatocellular carcinoma-derived PLC cells (clone PDc-13) and in Madin-Darby canine kidney cells (clone MDc-2) for the continuous monitoring of desmosomes in living cells. The hybrid polypeptides integrated specifically and without disturbance into normal-appearing desmosomes that occurred in associati…

Time FactorsRecombinant Fusion ProteinsBiologyCell LineCytokeratinDogsGenes ReporterDesmosomeCell AdhesionmedicineAnimalsHumansDesmosomal CadherinsCell adhesionIntermediate filamentCytoskeletonDesmocollinsMembrane GlycoproteinsCadherinCarcinomaCell CycleLiver NeoplasmsFluorescence recovery after photobleachingEpithelial CellsDesmosomesCell BiologyCell biologyMicroscopy Electronmedicine.anatomical_structureMicroscopy FluorescenceKeratinsCalciumJournal of Cell Science
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Partially Reversible Adsorption of Annexin A1 on POPC/POPS Bilayers Investigated by QCM Measurements, SFM, and DMC Simulations

2005

The kinetics of annexin A1 binding to solid-supported lipid bilayers consisting of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC)/1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoserine (POPS; 4:1) has been investigated as a function of the calcium ion concentration in the bulk phase. Quartz crystal microbalance measurements in conjunction with scanning force microscopy, fluorescence microscopy, and computer simulations indicate that at a given Ca2+ concentration annexin A1 adsorbs irreversibly on membrane domains enriched in POPS. By contrast, annexin A1 adsorbs reversibly on the POPC-enriched phase, which is composed of single POPS molecules embedded within a POPC matrix. The overall are…

Time FactorsSurface PropertiesLipid BilayersKineticsAnalytical chemistryBiosensing TechniquesPhosphatidylserinesMicroscopy Atomic ForceBiochemistrychemistry.chemical_compoundAdsorptionPhase (matter)MicroscopyComputer SimulationParticle SizeLipid bilayerMolecular BiologyPOPCAnnexin A1ChemistryOrganic Chemistrytechnology industry and agricultureMembranes ArtificialQuartz crystal microbalanceMembraneMicroscopy FluorescencePhosphatidylcholinesMolecular Medicinelipids (amino acids peptides and proteins)AdsorptionStress MechanicalMonte Carlo MethodChemBioChem
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Interaction of an odorant lactone with model phospholipid bilayers and its strong fluidizing action in yeast membrane

2003

International audience; Some odorant lactones are naturally present in fruits or in fermented products; they can also be used as food additives and can be produced by microorganisms at the industrial scale by biotechnological processes. Gamma-decalactone was previously shown to have antimicrobial properties. We determined by infrared spectroscopy measurements that this compound rapidly diffused into model phospholipid bilayers (within 2 min), modifying the general physical state of a dimyristoyl-L-alpha-phosphatidylcholine (DMPC) film. In vivo, the lactone strongly increased membrane fluidity in the model yeast Yarrowia lipolytica, as evaluated by fluorescence anisotropy measurements. This …

Time Factors[SDV.BIO]Life Sciences [q-bio]/BiotechnologyLipid BilayersYarrowiaMESH : Models BiologicalLactonesMESH : Spectroscopy Fourier Transform InfraredMESH: Dimyristoylphosphatidylcholinechemistry.chemical_compoundMESH : DimyristoylphosphatidylcholineSpectroscopy Fourier Transform InfraredMembrane fluidityOrganic chemistryMESH : Anti-Bacterial Agents[INFO.INFO-BT]Computer Science [cs]/BiotechnologyAntibacterial agentMESH : Spectrometry FluorescencebiologyMESH: Lipid BilayersMESH: Indicators and Reagentsfood and beveragesGeneral MedicineAnti-Bacterial AgentsMESH : LactonesMembraneBenzyl alcoholDimyristoylphosphatidylcholine[ INFO.INFO-BT ] Computer Science [cs]/BiotechnologyMESH: LactonesMESH: Spectrometry FluorescenceMESH : Time FactorsMESH : YarrowiaPhospholipid[SDV.BC]Life Sciences [q-bio]/Cellular BiologyModels BiologicalMicrobiologyMESH: Spectroscopy Fourier Transform InfraredMESH : Indicators and ReagentsMESH: Anti-Bacterial Agents[ SDV.BC ] Life Sciences [q-bio]/Cellular BiologyMESH: Time FactorsMESH: Models Biological[ SDV.BIO ] Life Sciences [q-bio]/BiotechnologyYarrowiaBiological membranebiology.organism_classificationYeastSpectrometry FluorescencechemistryIndicators and ReagentsMESH: YarrowiaMESH : Lipid BilayersFood ScienceInternational Journal of Food Microbiology
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Role of tir and intimin in the virulence of rabbit enteropathogenic Escherichia coli serotype O103:H2.

2000

ABSTRACT Attaching and effacing (A/E) rabbit enteropathogenic Escherichia coli (REPEC) strains belonging to serogroup O103 are an important cause of diarrhea in weaned rabbits. Like human EPEC strains, they possess the locus of enterocyte effacement clustering the genes involved in the formation of the A/E lesions. In addition, pathogenic REPEC O103 strains produce an Esp-dependent but Eae (intimin)-independent alteration of the host cell cytoskeleton characterized by the formation of focal adhesion complexes and the reorganization of the actin cytoskeleton into bundles of stress fibers. To investigate the role of intimin and its translocated coreceptor (Tir) in the pathogenicity of REPEC, …

Time Factors[SDV]Life Sciences [q-bio]MutantAdministration OralPATHOGENICITEmedicine.disease_causeBacterial AdhesionMICROSCOPIE ELECTRONIQUE A TRANSMISSIONFecesCytoskeleton0303 health sciencesVirulenceEscherichia coli ProteinsEnterobacteriaceae3. Good health[SDV] Life Sciences [q-bio]IntestinesInfectious DiseasesMolecular and Cellular PathogenesisRabbitsLocus of enterocyte effacementBacterial Outer Membrane ProteinsImmunologyMolecular Sequence DataVirulenceReceptors Cell SurfaceBiologyMicrobiologydigestive systemMicrobiologyCell Line03 medical and health sciencesBacterial ProteinsIleummedicineEscherichia coliAnimalsHumansEnteropathogenic Escherichia coliAdhesins BacterialEscherichia coli030304 developmental biologyIntiminModels Genetic030306 microbiologyGenetic Complementation TestEpithelial Cellsbiochemical phenomena metabolism and nutritionbiology.organism_classificationActin cytoskeleton[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/BacteriologyActinsKineticsMicroscopy ElectronMicroscopy FluorescenceMutagenesisParasitologyCarrier ProteinsHeLa CellsInfection and immunity
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