Search results for "membrane proteins"

showing 10 items of 713 documents

The Mitochondrial Targeting Chaperone 14-3-3ε Regulates a RIG-I Translocon that Mediates Membrane Association and Innate Antiviral Immunity

2012

SummaryRIG-I is a cytosolic pathogen recognition receptor that initiates immune responses against RNA viruses. Upon viral RNA recognition, antiviral signaling requires RIG-I redistribution from the cytosol to membranes where it binds the adaptor protein, MAVS. Here we identify the mitochondrial targeting chaperone protein, 14-3-3ε, as a RIG-I-binding partner and essential component of a translocation complex or “translocon” containing RIG-I, 14-3-3ε, and the TRIM25 ubiquitin ligase. The RIG-I translocon directs RIG-I redistribution from the cytosol to membranes where it mediates MAVS-dependent innate immune signaling during acute RNA virus infection. 14-3-3ε is essential for the stable inte…

TRIM25Cancer ResearchUbiquitin-Protein Ligasesviruseschemical and pharmacologic phenomenaHepacivirusMicrobiologyAntiviral AgentsModels BiologicalArticleCell LineDEAD-box RNA HelicasesTripartite Motif Proteins03 medical and health sciences0302 clinical medicineVirologyImmunology and Microbiology(all)Protein Interaction MappingHumansReceptors ImmunologicDEAD Box Protein 58Molecular Biology030304 developmental biology0303 health sciencesInnate immune systembiologyRIG-IRNAMembrane Proteinsvirus diseasesRNA virusbiochemical phenomena metabolism and nutritionbiology.organism_classificationTranslocon3. Good healthCell biology14-3-3 Proteins030220 oncology & carcinogenesisChaperone (protein)biology.proteinDEAD Box Protein 58Parasitologybiological phenomena cell phenomena and immunityMolecular ChaperonesProtein BindingTranscription FactorsCell Host & Microbe
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Binding properties and stability of the Ras-association domain of Rap1-GTP interacting adapter molecule (RIAM).

2012

The Rap1-GTP interacting adapter protein (RIAM) is an important protein in Rap1-mediated integrin activation. By binding to both Rap1 GTPase and talin, RIAM recruits talin to the cell membrane, thus facilitating talin-dependent integrin activation. In this article, we studied the role of the RIAM Ras-association (RA) and pleckstrin-homology (PH) domains in the interaction with Rap1. We found that the RA domain was sufficient for GTP-dependent interaction with Rap1B, and the addition of the PH domain did not change the binding affinity. We also detected GTP-independent interaction of Rap1B with the N-terminus of RIAM. In addition, we found that the PH domain stabilized the RA domain both in …

TalinIntegrinsGTP'lcsh:MedicineGTPaseSignal transductionBiochemistryProtein structureMolecular cell biologyRIAMlcsh:Science0303 health sciencesMultidisciplinarybiologyProtein Stability030302 biochemistry & molecular biologySignal transducing adaptor proteinrap1 GTP-Binding ProteinssitoutuminenCell biologyPleckstrin homology domainRap1Research Articleendocrine systemvuorovaikutusProtein domainIntegrinSignaling in cellular processesPhosphoinositide Signal TransductionSignaling Pathways03 medical and health sciencesCell AdhesionHumansProtein InteractionsBiologyGTPase signaling030304 developmental biologyRas signalingAdaptor Proteins Signal Transducingintegriinitlcsh:RProteinsMembrane ProteinsRegulatory ProteinsProtein Structure TertiaryCytoskeletal Proteinsenzymes and coenzymes (carbohydrates)rap GTP-Binding ProteinsCell movement signalingbiology.proteinta1181lcsh:QPLoS ONE
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Synaptic tetraspan vesicle membrane proteins are conserved but not needed for synaptogenesis and neuronal function in Caenorhabditis elegans

2006

Tetraspan vesicle membrane proteins (TVPs) comprise a major portion of synaptic vesicle proteins, yet their contribution to the synaptic vesicle cycle is poorly understood. TVPs are grouped in three mammalian gene families: physins, gyrins, and secretory carrier-associated membrane proteins (SCAMPs). In Caenorhabditis elegans , only a single member of each of these families exists. These three nematode TVPs colocalize to the same vesicular compartment when expressed in mammalian cells, suggesting that they could serve overlapping functions. To examine their function, C. elegans null mutants were isolated for each gene, and a triple mutant was generated. Surprisingly, these animals develop …

TetraspaninsMutantSynaptogenesisSynaptic vesicleEvolution MolecularAnimalsHumansCloning MolecularCaenorhabditis elegansIntegral membrane proteinCells CulturedCaenorhabditis elegansNeuronsMultidisciplinaryModels GeneticbiologyChemotaxisCell MembraneMembrane ProteinsBiological Sciencesbiology.organism_classificationSynaptic vesicle cycleCell biologyElectrophysiologyMembrane proteinMutationSynapsesSynaptophysinbiology.proteinProceedings of the National Academy of Sciences
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A novel mutation (Thr116IIe) in the presenilin 1 gene in a patient with early-onset Alzheimer's disease

2004

We report a novel presenilin 1 (PSN1) mutation (Thr116Ile) in a woman with early onset Alzheimer's disease (AD). This mutation was not found in 100 healthy controls, indicating that this is not a common polymorphism. The patient presented with forgetfulness at age 45, followed over the next 3 years by a worsening of the memory loss and frequent episodes of confusion and spatial disorientation. Neuroimaging studies were consistent with AD. The analysis of the family's pedigree showed that the proband was apparently the only member affected. Because the early death of several close relatives (i.e. the mother and the grandmother) and the demonstration that the father is not a mutation carrier,…

ThreonineProbandDNA Mutational AnalysisDiseaseBioinformaticsGenetic analysisPresenilinMutation CarrierAlzheimer DiseasePolymorphism (computer science)Presenilin-1medicineHumansEarly-onset Alzheimer's diseaseIsoleucineGeneticsbusiness.industryMembrane ProteinsMiddle Agedmedicine.diseaseNeurologyMutationMutation (genetic algorithm)FemaleSettore MED/26 - NeurologiaNeurology (clinical)businessAlzheimer's Disease Novel mutation Presenilin 1
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Caspase-3 contributes to ZO-1 and Cl-5 tight-junction disruption in rapid anoxic neurovascular unit damage.

2011

BACKGROUND: Tight-junction (TJ) protein degradation is a decisive step in hypoxic blood-brain barrier (BBB) breakdown in stroke. In this study we elucidated the impact of acute cerebral ischemia on TJ protein arrangement and the role of the apoptotic effector protease caspase-3 in this context. METHODOLOGY/PRINCIPAL FINDINGS: We used an in vitro model of the neurovascular unit and the guinea pig whole brain preparation to analyze with immunohistochemical methods the BBB properties and neurovascular integrity. In both methodological approaches we observed rapid TJ protein disruptions after 30 min of oxygen and glucose deprivation or middle cerebral artery occlusion, which were accompanied by…

Time FactorsAnatomy and Physiologylcsh:MedicineMiceMolecular Cell BiologyPathologySignaling in Cellular ProcessesHypoxia Brainlcsh:ScienceCells CulturedNeuropathologyApoptotic SignalingMultidisciplinaryTight junctionCaspase 3ChemistryAnimal ModelsCell biologyTransport proteinProtein Transportmedicine.anatomical_structureNeurologyBlood-Brain BarrierMedicineResearch ArticleSignal TransductionClinical Research DesignCerebrovascular DiseasesGuinea PigsIschemiaContext (language use)Caspase 3Protein degradationBlood–brain barrierNeurological SystemTight JunctionsCapillary PermeabilityModel OrganismsDiagnostic MedicinemedicineAnimalsTransient Ischemic AttacksAnimal Models of DiseaseClaudinBiologyIschemic Strokelcsh:REndothelial CellsMembrane ProteinsPhosphoproteinsmedicine.diseaseAnatomical PathologyClaudinsImmunologyZonula Occludens-1 ProteinNervous System Componentslcsh:QPLoS ONE
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Interactions of silica nanoparticles with lung epithelial cells and the association to flotillins

2012

Amorphous silica nanoparticles (aSNPs) gain increasing popularity for industrial and therapeutic claims. The lung with its surface area of 100-140 m(2) displays an ideal target for therapeutic approaches, but it represents also a serious area of attack for harmful nanomaterials. The exact nature of the cytotoxic effects of NPs is still unknown. Furthermore, cellular pathways and the destiny of internalized NPs are still poorly understood. Therefore, we examined the cytotoxicity (MTS, LDH) and inflammatory responses (IL-8) for different-sized aSNPs (30, 70, 300 nm) on our lung epithelial cells line NCI H441 and endothelial cell line ISO-HAS-1. Additionally, colocalization studies have been c…

Time FactorsEndosomeCell SurvivalHealth Toxicology and MutagenesisEndothelial cellsCytotoxicityEndosomessilica nanoparticlesToxicologyEndocytosisTransfectionClathrinFlotillin-1siliciumFlotillin-2Alveolar-capillary barrierCell Line TumorAlveolar capillary barrierHumansInterleukin 8Inorganic CompoundsParticle SizeCytotoxicityLungbiologyDose-Response Relationship DrugL-Lactate DehydrogenaseInterleukin-8Membrane ProteinsInflammatory responseEpithelial CellsGeneral MedicineTransfectionSilicon DioxideEndocytosisCell biologyLung epithelial cellsEndothelial stem cellEndocytic vesiclebiology.proteinNanoparticlesRNA InterferenceInflammation Mediators
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Neurons and ECM regulate occludin localization in brain endothelial cells

2000

We report that extracellular matrix and neurons modulate the expression of occludin, one of the main components of tight junctions, by rat brain endothelial cells (RBE4.B). Of the three extracellular matrix proteins which we tested (collagen I, collagen IV, and laminin), collagen IV stimulated at the best the expression of occludin mRNA. The corresponding protein, however, was not synthesized. Significant amounts of occludin accumulated only when RBE4.B cells were cultured on collagen IV-coated inserts, in the presence of cortical neurons, plated on laminin-coated companion wells. Finally, occludin segregated at the cell periphery, only when endothelial cells were co- cultured with neurons …

Time FactorsEndothelial cellsCellOccludinTight JunctionsExtracellular matrixRats Sprague-DawleyFetusLamininNeurofilament ProteinsOccludinSettore BIO/10 - BiochimicaGlial Fibrillary Acidic ProteinmedicineAnimalsRNA MessengerCells CulturedBlood-brain barrierNeuronsbiologyTight junctionGeneral NeuroscienceBrainMembrane ProteinsCortical NeuronsExtracellular matrixImmunohistochemistryCell biologyRatsEndothelial stem cellmedicine.anatomical_structureMembrane proteinCell cultureSettore CHIM/09 - Farmaceutico Tecnologico ApplicativoCerebrovascular Circulationbiology.proteinSettore MED/26 - NeurologiaCollagenEndothelium VascularLamininNeuroscience
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Effects of cyclooxygenase-1/cyclooxygenase-2 inhibition on leukocyte/endothelial cell interactions in the rat mesentery.

2002

Nonsteroidal anti-inflammatory drugs (NSAID) inhibit cyclooxygenase activity and cause gastrointestinal damage in part by promoting leukocyte accumulation in the mucosa. Our aim was to evaluate the effects of selective blockade of the isoenzymes cyclooxygenase-1 and cyclooxygenase-2 on leukocyte adhesion in vivo. Leukocyte/endothelial cell interactions were examined in rat mesenteric venules before and after treatment with indomethacin, SC-560 (5-(4-chlorophenyl)-1-(4-methoxyphenyl)-3-trifluoromethylpyrazole, cyclooxygenase-1 inhibitor), DFP (5,5-dimethyl-3-(2-propoxy)-4-(4-methanesulfonyl)-2(5H)-furanone, cyclooxygenase-2 inhibitor), or SC-560 plus DFP (20 mg/kg, i.v. each). Indomethacin i…

Time FactorsEndotheliumIndomethacinCell CommunicationPharmacologyRats Sprague-DawleyIn vivomedicineBenzene DerivativesCell AdhesionLeukocytesTumor Cells CulturedAnimalsHumansCyclooxygenase InhibitorsMesenteryFuransPharmacologybiologyCyclooxygenase 2 InhibitorsChemistryAnti-Inflammatory Agents Non-SteroidalMembrane ProteinsBiological activityDrug SynergismRatsEndothelial stem cellIsoenzymesmedicine.anatomical_structureMechanism of actionEnzyme inhibitorCyclooxygenase 2Prostaglandin-Endoperoxide SynthasesImmunologybiology.proteinCyclooxygenase 1PyrazolesCyclooxygenaseEndothelium Vascularmedicine.symptomBlood vesselEuropean journal of pharmacology
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IMMUNOGENICITY OF AN ACELLULAR PERTUSSIS VACCINE COMPOSED OF GENETICALLY INACTIVATED PERTUSSIS TOXIN COMBINED WITH FILAMENTOUS HEMAGGLUTININ AND PERT…

1993

We studied the immunogenicity of an acellular pertussis vaccine composed of genetically detoxified pertussis toxin (PT-9K/129G), filamentous haemagglutinin, and a 69-kilodalton protein, pertactin, in 30 children aged 12 to 24 months and in 80 infants aged 2 to 4 months. A significant increase of the neutralizing titer and of the titers against pertussis toxin, filamentous hemagglutinin, and pertactin, as determined by enzyme-linked immunosorbent assay, was achieved after three doses of vaccine in all the children; a significant increase of these antibody titers was obtained in 100%, 96.1%, 93.5%, and 98.7% of the infants, respectively.

Time FactorsFilamentous haemagglutinin adhesinPertussis toxincomplex mixturesBordetella pertussisMicrobiologyNeutralization TestsHumansMedicineVirulence Factors BordetellaAdhesins BacterialImmunization ScheduleWhooping coughPertussis VaccineAntigens Bacterialbusiness.industryImmunogenicitypertussisAntibody titerInfantmedicine.diseaseAntibodies BacterialVirologyVaccinationTiterHemagglutininsPertussis ToxinVaccines InactivatedChild PreschoolImmunoglobulin GPediatrics Perinatology and Child HealthDrug EvaluationPertactinbusinessVaccinepertussis; VaccineBacterial Outer Membrane Proteins
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LFA-1 activity state on dendritic cells regulates contact duration with T cells and promotes T-cell priming.

2010

AbstractA key event in the successful induction of adaptive immune responses is the antigen-specific activation of T cells by dendritic cells (DCs). Although LFA-1 (lymphocyte function–associated antigen 1) on T cells is considered to be important for antigen-specific T-cell activation, the role for LFA-1 on DCs remains elusive. Using 2 different approaches to activate LFA-1 on DCs, either by deletion of the αL-integrin cytoplasmic GFFKR sequence or by silencing cytohesin-1–interacting protein, we now provide evidence that DCs are able to make use of active LFA-1 and can thereby control the contact duration with naive T cells. Enhanced duration of DC/T-cell interaction correlates inversely …

Time FactorsT cellT-LymphocytesImmunologyReceptors Antigen T-CellPriming (immunology)chemical and pharmacologic phenomenaMice TransgenicCell CommunicationBiologyLymphocyte ActivationBiochemistryMiceImmune systemAntigenmedicineCell AdhesionAnimalsHypersensitivity DelayedLymphocyte function-associated antigen 1Antigen-presenting cellCells CulturedCell ProliferationMice KnockoutReverse Transcriptase Polymerase Chain ReactionMembrane Proteinshemic and immune systemsCell BiologyHematologyT lymphocyteDendritic cellDendritic CellsTh1 CellsFlow CytometryIntercellular Adhesion Molecule-1Lymphocyte Function-Associated Antigen-1Cell biologyMice Inbred C57BLmedicine.anatomical_structureImmunologyInterleukin-2RNA InterferenceCarrier ProteinsBlood
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