Search results for "Transport Vesicles"

showing 10 items of 15 documents

Specific binding of radiolabeled Cry1Fa insecticidal protein from Bacillus thuringiensis to midgut sites in lepidopteran species

2012

ABSTRACT Cry1Fa insecticidal protein was successfully radiolabeled with 125 I-Na. Specific binding to brush border membrane vesicles was shown for the lepidopteran species Ostrinia nubilalis , Spodoptera frugiperda , Spodoptera exigua , Helicoverpa armigera , Heliothis virescens , and Plutella xylostella . Homologous competition assays were performed to obtain equilibrium binding parameters ( K d [dissociation constant] and R t [concentration of binding sites]) for these six insect species.

BioquímicavirusesBiotecnologia agrícolaBacillus thuringiensisHelicoverpa armigeraSpodopteraSpodopteraApplied Microbiology and BiotechnologyOstriniaIodine RadioisotopesHemolysin ProteinsPlagues ControlBacterial ProteinsSpecies SpecificityBacillus thuringiensisExiguaBotanyparasitic diseasesPlaguicidesInvertebrate MicrobiologyAnimalsBinding siteTransport VesiclesBinding SitesEcologybiologyHeliothis virescensBacillus thuringiensis ToxinsMicrovillifungiPlutellabiology.organism_classificationEndotoxinsLepidopteraBiochemistryDigestive SystemProteïnesFood ScienceBiotechnology
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Oligodendroglioma cells synthesize the differentiation-specific linker histone H1˚ and release it into the extracellular environment through shed ves…

2013

Chromatin remodelling can be involved in some of the epigenetic modifications found in tumor cells. One of the mechanisms at the basis of chromatin dynamics is likely to be synthesis and incorporation of replacement histone variants, such as the H1° linker histone. Regulation of the expression of this protein can thus be critical in tumorigenesis. In developing brain, H1° expression is mainly regulated at the post-transcriptional level and RNA-binding proteins (RBPs) are involved. In the past, attention mainly focused on the whole brain or isolated neurons and little information is available on H1° expression in other brain cells. Even less is known relating to tumor glial cells. In this st…

Cancer ResearchOligodendrogliomaGene Expressionmedicine.disease_causeHistonessheddingHistone H1Settore BIO/10 - BiochimicaGene expressionmedicineAnimalsRNA MessengerEpigeneticsRats WistarSettore BIO/06 - Anatomia Comparata E CitologiaTransport Vesicleshistone variantsCells CulturedCell NucleusMessenger RNAbiologyBrain NeoplasmsastrocytesBrainRNA-Binding ProteinsArticlesH1° histoneCell cycleChromatin Assembly and DisassemblyRatsChromatinCell biologyCell Transformation Neoplasticoligodendroglioma cellsHistoneOncologyoligodendroglioma cells astrocytes post-transcriptional regulation histone variants H1˚ histone RNA-binding proteins extracellular vesicles sheddingbiology.proteinextracellular vesiclesCarcinogenesispost-transcriptional regulation
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Release of canine parvovirus from endocytic vesicles

2003

Canine parvovirus (CPV) is a small nonenveloped virus with a single-stranded DNA genome. CPV enters cells by clathrin-mediated endocytosis and requires an acidic endosomal step for productive infection. Virion contains a potential nuclear localization signal as well as a phospholipase A(2) like domain in N-terminus of VP1. In this study we characterized the role of PLA(2) activity on CPV entry process. PLA(2) activity of CPV capsids was triggered in vitro by heat or acidic pH. PLA(2) inhibitors inhibited the viral proliferation suggesting that PLA(2) activity is needed for productive infection. The N-terminus of VP1 was exposed during the entry, suggesting that PLA(2) activity might have a …

Cell Membrane PermeabilityTransferrin receptorParvovirus CanineMembrane permeabilizationEndosomeanimal diseasesvirusesEndocytic cycleEntryBiologyEndocytosisPhospholipases AParvovirusAmiloridechemistry.chemical_compoundCapsidPhospholipase A2VirologyReceptors TransferrinmedicineAnimalsMonensinTransport VesiclesBrefeldin AVesicleBafilomycinDextransBrefeldin ALipid MetabolismEndocytosisAmilorideCell biologyEndocytic vesiclechemistryCatsCapsid ProteinsMacrolidesBafilomycin A1Lysosomesmedicine.drugVirology
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Extracellular Vesicles from Neural Stem Cells Transfer IFN-γ via Ifngr1 to Activate Stat1 Signaling in Target Cells

2014

The idea that stem cell therapies work only via cell replacement is challenged by the observation of consistent intercellular molecule exchange between the graft and the host. Here we defined a mechanism of cellular signaling by which neural stem/precursor cells (NPCs) communicate with the microenvironment via extracellular vesicles (EVs), and we elucidated its molecular signature and function. We observed cytokine-regulated pathways that sort proteins and mRNAs into EVs. We described induction of interferon gamma (IFN-γ) pathway in NPCs exposed to proinflammatory cytokines that is mirrored in EVs. We showed that IFN-γ bound to EVs through Ifngr1 activates Stat1 in target cells. Finally, we…

Cell signalingCell CommunicationBiologyArticle3T3 cellsProinflammatory cytokineInterferon-gammaMiceTh2 CellsNeural Stem CellsPrecursor cellmedicineAnimalsInterferon gammaRNA MessengerTransport VesiclesMolecular BiologyReceptors InterferonInflammationBiological Transport3T3 CellsCell BiologyTh1 CellsNeural stem cellCell biologySTAT1 Transcription Factormedicine.anatomical_structureCellular MicroenvironmentSignal transductionStem cellSignal Transductionmedicine.drugMolecular Cell
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Comm Sorts Robo to Control Axon Guidance at the Drosophila Midline

2002

AbstractAxon growth across the Drosophila midline requires Comm to downregulate Robo, the receptor for the midline repellent Slit. We show here that comm is required in neurons, not in midline cells as previously thought, and that it is expressed specifically and transiently in commissural neurons. Comm acts as a sorting receptor for Robo, diverting it from the synthetic to the late endocytic pathway. A conserved cytoplasmic LPSY motif is required for endosomal sorting of Comm in vitro and for Comm to downregulate Robo and promote midline crossing in vivo. Axon traffic at the CNS midline is thus controlled by the intracellular trafficking of the Robo guidance receptor, which in turn depends…

Central Nervous SystemEmbryo NonmammalianEndosomeGrowth ConesMolecular Sequence DataEndocytic cycleDown-RegulationNerve Tissue ProteinsReceptors Cell SurfaceCell CommunicationEndosomesBiologyModels BiologicalFunctional LateralityGeneral Biochemistry Genetics and Molecular BiologySequence Homology Nucleic AcidEctodermmedicineAnimalsDrosophila ProteinsReceptors ImmunologicAxonTransport VesiclesReceptorSequence Homology Amino AcidBiochemistry Genetics and Molecular Biology(all)Stem CellsCell MembraneGraft SurvivalGene Expression Regulation DevelopmentalMembrane ProteinsCell DifferentiationAnatomyCommissureSlitProtein Structure TertiaryCell biologyProtein TransportDrosophila melanogastermedicine.anatomical_structureCOS CellsRoundaboutAxon guidanceStem Cell TransplantationCell
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Comprehensive analysis of expression, subcellular localization, and cognate pairing of SNARE proteins in oligodendrocytes

2009

Oligodendrocytes form the central nervous system myelin sheath by spiral wrapping of their plasma membrane around axons, necessitating a high rate of exocytic membrane addition to the growing myelin membrane. Membrane fusion is mediated by soluble N-ethylmaleimide-sensitive factor attachment protein receptor proteins (SNAREs), which act by specific pairing of vesicle (R)- and target (Q)-SNAREs. To characterize oligodendroglial SNAREs and their trafficking pathways, we performed a detailed expression analysis of SNAREs in differentiating cultured oligodendrocytes and myelin and determined their subcellular localization. Expression of the plasma membrane Q-SNAREs syntaxin 3, syntaxin 4, SNAP2…

Central Nervous SystemMaleVesicle-Associated Membrane Protein 3SynaptobrevinGolgi ApparatusBiologyMembrane FusionR-SNARE ProteinsMiceCellular and Molecular NeuroscienceSNAP23AnimalsSyntaxinQc-SNARE ProteinsTransport VesiclesCells CulturedMyelin SheathR-SNARE ProteinsQa-SNARE ProteinsVesicleCell MembraneLipid bilayer fusionQb-SNARE ProteinsSyntaxin 3Cell CompartmentationTransport proteinCell biologyOligodendrogliaProtein Transportnervous systemFemalebiological phenomena cell phenomena and immunitySNARE ProteinsDimerizationJournal of Neuroscience Research
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The retinitis pigmentosa protein RP2 links pericentriolar vesicle transport between the Golgi and the primary cilium.

2010

Photoreceptors are complex ciliated sensory neurons. The basal body and periciliary ridge of photoreceptors function in association with the Golgi complex to regulate the export of proteins from the inner segment to the outer segment sensory axoneme. Here, we show that the retinitis pigmentosa protein RP2, which is a GTPase activating protein (GAP) for Arl3, localizes to the ciliary apparatus, namely the basal body and the associated centriole at the base of the photoreceptor cilium. Targeting to the ciliary base was dependent on N-terminal myristoylation. RP2 also localized to the Golgi and periciliary ridge of photoreceptors, which suggested a role for RP2 in regulating vesicle traffic an…

CentriolePhotoreceptor Connecting CiliumGolgi ApparatusBiologysymbols.namesakeMiceIntraflagellar transportGTP-Binding ProteinsGeneticsBasal bodyAnimalsHumansKIF3APhotoreceptor CellsCiliaEye ProteinsTransport VesiclesMolecular BiologyGenetics (clinical)Cells CulturedCentriolesADP-Ribosylation FactorsCiliumCiliary BodyIntracellular Signaling Peptides and ProteinsMembrane ProteinsBiological TransportGeneral MedicineGolgi apparatusCell biologysymbolssense organsCiliary baseRetinitis PigmentosaHuman molecular genetics
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Echovirus 1 Entry into Polarized Caco-2 Cells Depends on Dynamin, Cholesterol, and Cellular Factors Associated with Macropinocytosis

2013

ABSTRACT Enteroviruses invade their hosts by crossing the intestinal epithelium. We have examined the mechanism by which echovirus 1 (EV1) enters polarized intestinal epithelial cells (Caco-2). Virus binds to VLA-2 on the apical cell surface and moves rapidly to early endosomes. Using inhibitory drugs, dominant negative mutants, and small interfering RNAs (siRNAs) to block specific endocytic pathways, we found that virus entry requires dynamin GTPase and membrane cholesterol but is independent of both clathrin- and caveolin-mediated endocytosis. Instead, infection requires factors commonly associated with macropinocytosis, including amiloride-sensitive Na + /H + exchange, protein kinase C, …

DynaminsSodium-Hydrogen ExchangersEndosomeImmunologyEndocytic cycleEndocytosisMicrobiologyClathrinViral entryVirologyHumansTransport VesiclesProtein Kinase CDynaminbiologyPinocytosisEpithelial CellsVirus InternalizationIntestinal epitheliumEnterovirus B HumanVirus-Cell InteractionsCell biologyDNA-Binding ProteinsAlcohol OxidoreductasesCholesterolInsect ScienceHost-Pathogen Interactionsbiology.proteinPinocytosisCaco-2 CellsJournal of Virology
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Chitosomes loaded with cranberry proanthocyanidins attenuate the bacterial lipopolysaccharide-induced expression of iNOS and COX-2 in raw 264.7 macro…

2009

Chitosan binds to negatively charged soy lecithin liposomes by an electrostatic interaction driven by its positively charged amino group. This interaction allows stable covered vesicles (chitosomes) to be developed as a suitable targeted carrier and controlled release system. This study investigated the effect of chitosomes on the activation of cranberry proanthocyanidins (PAC) in Raw 264.7 macrophages. Chitosomes were characterized according to size, zeta potential, PAC-loading, and release properties. Results showed an increase in the net positive charge and size of the liposomes as the concentration of chitosan was increased, suggesting an effective covering of the vesicles by means of e…

LipopolysaccharidesLipopolysaccharideNitric Oxide Synthase Type IIPharmaceutical ScienceInflammationEndocytosisCell LineMicechemistry.chemical_compoundmedicineAnimalsMacrophageProanthocyanidinsTransport VesiclesChitosanLiposomeMolecular StructurebiologyMacrophagesVesicleControlled releaseMolecular biologyEnzyme ActivationNitric oxide synthaseVaccinium macrocarponchemistryBiochemistryCyclooxygenase 2Spectrometry Mass Matrix-Assisted Laser Desorption-Ionizationbiology.proteinmedicine.symptomJournal of Liposome Research
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Extracellular Membrane Vesicles as Vehicles for Brain Cell-to-Cell Interactions in Physiological as well as Pathological Conditions.

2015

Extracellular vesicles are involved in a great variety of physiological events occurring in the nervous system, such as cross talk among neurons and glial cells in synapse development and function, integrated neuronal plasticity, neuronal-glial metabolic exchanges, and synthesis and dynamic renewal of myelin. Many of these EV-mediated processes depend on the exchange of proteins, mRNAs, and noncoding RNAs, including miRNAs, which occurs among glial and neuronal cells. In addition, production and exchange of EVs can be modified under pathological conditions, such as brain cancer and neurodegeneration. Like other cancer cells, brain tumours can use EVs to secrete factors, which allow escaping…

Nervous systemectosomeCelllcsh:MedicineReview ArticleBiologyhorizontal transfer of pathological propertieGeneral Biochemistry Genetics and Molecular BiologySynapseExtracellular VesiclesMyelinextracellular membrane vesicles (EVs); ectosomes; exosomes; brain cancer; neuronal-glial unconventional cross-talk pathways; horizontal transfer of pathological properties; extracellular spreading of protein aggregates.Settore BIO/10 - BiochimicamedicineexosomeHumansSecretionextracellular membrane vesicles (EVs)Settore BIO/06 - Anatomia Comparata E CitologiaTransport Vesiclesbrain cancerNeuronsMembranesNeuronal PlasticityGeneral Immunology and Microbiologylcsh:RNeurodegenerationBrainBiological TransportGeneral Medicinemedicine.diseaseextracellular spreading of protein aggregates.Cell biologyMicroRNAsmedicine.anatomical_structureSynapsesCancer cellNeurogliaNeuroglianeuronal-glial unconventional cross-talk pathway
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