Search results for "Microscopy"

showing 10 items of 3390 documents

In vitro degradation of porous PLLA/pearl powder composite scaffolds

2013

Abstract The in vitro degradation behavior of poly- l -lactide (PLLA), PLLA/aragonite pearl powder and PLLA/vaterite pearl powder scaffolds was investigated. The scaffolds were soaked in phosphate buffer solution (PBS) up to 200 days. Scanning electron microscopy (SEM), gel permeation chromatography (GPC), and differential scanning calorimetry (DSC) were used to observe any degradation of the scaffolds. Degradation behaviors such as changes in pH, porosity, bulk density, water absorption, weight loss and mechanical properties were discussed. The results show that a gradual increase of the pH in composite scaffolds can decrease the rate of hydrolysis of PLLA. PLLA/vaterite and PLLA/aragonite…

Time FactorsMaterials scienceAbsorption of waterCompressive StrengthScanning electron microscopePolyestersComposite numberBioengineeringBuffersAbsorptionCalcium CarbonateBiomaterialsGel permeation chromatographyHydrolysischemistry.chemical_compoundDifferential scanning calorimetryVateriteAnimalsTransition TemperatureComposite materialLactideCalorimetry Differential ScanningTissue ScaffoldsWaterHydrogen-Ion ConcentrationMolecular WeightSolutionsChemical engineeringchemistryMechanics of MaterialsMicroscopy Electron ScanningCalciumPowdersPorosityMaterials Science and Engineering: C
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Cariostatic effect of a light-cured, resin-reinforced glass-ionomer for bonding orthodontic brackets in vivo

1998

The aim of this study was to evaluate in vivo the cariostatic potential of the resin-reinforced glass-ionomer (Vitremer core build-up restorative; 3M Dental Product Division) when used as a bonding agent for orthodontic brackets. The mineral distribution and topography of the enamel surface adjacent to the bracket base was determined by quantitative microradiography (TMR) and confocal laser scanning microscopy (CLSM). The study was designed in split-mouth technique using 9 pairs of premolars to be extracted for orthodontic reasons. One tooth of each pair was bonded with the resin-reinforced glass-ionomer, and the control contralateral premolar with the non-fluoridated composite (Concise, 3M…

Time FactorsMaterials scienceLightOrthodontic BracketsSurface PropertiesComposite numberGlass ionomer cementOrthodonticsDental bondingComposite ResinsStatistics Nonparametricstomatognathic systemIn vivoConfocal laser scanning microscopyPremolarmedicineHumansBicuspidBisphenol A-Glycidyl MethacrylateChildDental EnamelOrthodonticsMicroscopy ConfocalEnamel paintBracketDental BondingMicroradiographyCariostatic Agentsstomatognathic diseasesmedicine.anatomical_structureGlass Ionomer Cementsvisual_artvisual_art.visual_art_mediumOral SurgeryJournal of Orofacial Orthopedics / Fortschritte der Kieferorthop�die
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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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In human endothelial cells rapamycin causes mTORC2 inhibition and impairs cell viability and function.

2008

Aim Drug-eluting stents are widely used to prevent restenosis but are associated with late endothelial damage. To understand the basis for this effect, we have studied the consequences of a prolonged incubation with rapamycin on the viability and functions of endothelial cells. Methods and results Human umbilical vein or aorta endothelial cells were exposed to rapamycin in the absence or in the presence of tumour necrosis factor α (TNFα). After a 24 h-incubation, rapamycin (100 nM) caused a significant cell loss associated with the increase of both apoptosis and necrosis, as quantified by propidium iodide staining, caspase 3 activity, and lactate dehydrogenase release. Rapamycin also impair…

Time FactorsPhysiologyApoptosismTORC1Polymerase Chain Reactionchemistry.chemical_compoundCell MovementStress FibersMicroscopy ConfocalCaspase 3TOR Serine-Threonine KinasesNitric Oxide Synthase Type IIIRibosomal Protein S6 Kinases 70-kDaUp-RegulationEndothelial stem cellmedicine.anatomical_structureBiochemistryCardiology and Cardiovascular MedicineE-SelectinEndotheliumNitric Oxide Synthase Type IIICell SurvivalBlotting WesternEnzyme-Linked Immunosorbent AssayBiologyMechanistic Target of Rapamycin Complex 1Nitric OxideTacrolimusNecrosisTheophyllinePhysiology (medical)medicineHumansImmunoprecipitationViability assayPropidium iodideProtein kinase BAdaptor Proteins Signal TransducingSirolimusDose-Response Relationship DrugL-Lactate DehydrogenaseTumor Necrosis Factor-alphaEndothelial CellsProteinsCardiovascular AgentsRegulatory-Associated Protein of mTORMolecular biologyRapamycin-Insensitive Companion of mTOR ProteinchemistryMultiprotein ComplexesTOR Serine-Threonine KinasesCarrier ProteinsProtein KinasesTranscription FactorsCardiovascular research
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Fennel waste-based films suitable for protecting cultivations.

2007

Biodegradable, flexible, and moisture-resistant films were obtained by recycling fennel waste and adding to fennel homogenates the bean protein phaseolin that was modified or not modified by the enzyme transglutaminase. All films were analyzed for their morphology, mechanical properties, water vapor permeability, and susceptibility to biodegradation under soil-like conditions. Our experiments showed that transglutaminase treatment of the phaseolin-containing fennel waste homogenates allowed us to obtain films comparable in their mechanical properties and water vapor permeability to the commercial films Ecoflex and Mater-Bi. Furthermore, biodegradability tests demonstrated that the presence …

Time FactorsPolymers and PlasticsFennel waste-based filmFood HandlingOligonucleotidesIndustrial WasteBioengineeringBiocompatible MaterialsEnvironmentBioplasticIndustrial wasteBiomaterialschemistry.chemical_compoundBotanyMaterials ChemistryFood scienceCelluloseCellulosedegradationPlant ProteinsTransglutaminasesAgricultureFabaceaeBiodegradationEnvironmentally friendlyCarbonBacilluPhaseolinBiodegradation EnvironmentalchemistryFoeniculumPlant proteinMicroscopy Electron ScanningPectinsSpectrophotometry UltravioletValorisationPlasticsSettore AGR/16 - Microbiologia AgrariaBiomacromolecules
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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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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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Study of the dynamics of biomolecules by high speed atomic force microscopy and surface enhanced Raman spectroscopy

2015

This thesis focuses on the coupling of High–Speed Atomic Force Microscopy (HS-AFM) and Surface Enhanced Raman Spectroscopy (SERS) for biomolecule analysis. We have designed a fabrication protocol to manufacture “SERS-active” substrates. The efficacy of gold, silver and gold-silver bimetallic crystalline nanoparticle substrates were evaluated. We have investigated the impact of optical and morphological features of the substrates on Raman signal intensity by analyzing well-known samples such as bipyridine ethylene and methylene blue molecules. We took an interest in three distinct biological problematics with HS-AFM and SERS analyses. First, we have detected the chemical signature of cytochr…

Tip–Enhanced Raman Spectroscopy (TERS)Surface Enhanced Raman Spectroscopy (SERS)CellsProteinsDetergent resistant membrane domains (DRMs)ProtéinesSpectroscopie Raman exaltée de surface (SERS)Nanoparticle substratesNoroviruses (NoVs)Substrats de nanoparticulesHigh–Speed Atomic Force Microscopy (HS-AFM)Microscopie à force atomique haute-vitesse (HS-AFM)Diffusion Raman exaltée par effet de pointe (TERS)Détergent résistant membrane domaines (DRMs)Plasmons de Surface Localisé (LSP)Cellules[PHYS.PHYS] Physics [physics]/Physics [physics]Localized Surface Plasmons (LSP)
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Electron Microscopic Contrast of the Cytoskeleton and Junctional Complexes of Intestinal Epithelial Cells by Ethanolic Phosphotungstic Acid

2000

After glutaraldehyde fixation and treatment with ethanolic phosphotungstic acid (E-PTA) before plastic embedding, sections of rat large intestine showed a characteristic electron contrasting pattern in epithelial cells. The axis of microvilli, terminal web, a thin band below the luminal plasma membrane, centrioles and junctional complexes (tight junctions, adherens junctions, and desmosomes) appeared highly contrasted. In addition to protein components of microfilaments and intermediate filaments, proteins from the junctional complexes could also be implicated in the contrasting reaction with E-PTA. Mitochondrial membranes, chromatin masses, and nucleoli of enterocytes showed considerable e…

Tissue FixationBiologyMicrofilamentSpecimen HandlingAdherens junctionTerminal webGlycocalyxchemistry.chemical_compoundAnimalsIntestine LargePhosphotungstic acidIntestinal MucosaRats WistarCytoskeletonIntermediate filamentCytoskeletonEthanolMicrovilliStaining and LabelingTissue EmbeddingTight junctionEpithelial CellsPhosphotungstic AcidAgricultural and Biological Sciences (miscellaneous)ChromatinMitochondriaRatsCell biologySolutionsMicroscopy ElectronIntercellular JunctionschemistrySolventsAnatomyCell NucleolusEuropean Journal of Morphology
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