1999
TNF recruits TRADD to the plasma membrane but not the trans-Golgi network, the principal subcellular location of TNF-R1.
Jones S, Ledgerwood E, Prins J, Galbraith J, Johnson D, Pober J, Bradley J. TNF recruits TRADD to the plasma membrane but not the trans-Golgi network, the principal subcellular location of TNF-R1. The Journal Of Immunology 1999, 162: 1042-8. PMID: 9916731, DOI: 10.4049/jimmunol.162.2.1042.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDAortaBrefeldin ACattleCell CompartmentationCell Line, TransformedCell MembraneEndothelium, VascularGolgi ApparatusHumansMicroscopy, ConfocalProteinsReceptors, Tumor Necrosis FactorReceptors, Tumor Necrosis Factor, Type ISubcellular FractionsTNF Receptor-Associated Factor 1TransfectionTumor Necrosis Factor-alphaU937 CellsConceptsTrans-Golgi networkPlasma membraneTNF-R1Golgi regionConfocal immunofluorescence microscopyHuman endothelial cell line ECV304Endothelial cell line ECV304Receptor-mediated endocytosisAdaptor proteinSubcellular localizationSubcellular locationCell fractionationBovine aortic endothelial cellsCoimmunoprecipitation studiesEndothelial cellsTRADDCell line U937Golgi apparatusSubcellular interactionsWestern blot analysisCell extractsMonocyte cell line U937Expression plasmidGolgiImmunofluorescence microscopy
1997
Mechanism of sustained E-selectin expression in cultured human dermal microvascular endothelial cells.
Kluger MS, Johnson DR, Pober JS. Mechanism of sustained E-selectin expression in cultured human dermal microvascular endothelial cells. The Journal Of Immunology 1997, 158: 887-96. PMID: 8993008, DOI: 10.4049/jimmunol.158.2.887.Peer-Reviewed Original Research
1996
Porcine endothelial CD86 is a major costimulator of xenogeneic human T cells: cloning, sequencing, and functional expression in human endothelial cells.
Maher SE, Karmann K, Min W, Hughes CC, Pober JS, Bothwell AL. Porcine endothelial CD86 is a major costimulator of xenogeneic human T cells: cloning, sequencing, and functional expression in human endothelial cells. The Journal Of Immunology 1996, 157: 3838-44. PMID: 8892613, DOI: 10.4049/jimmunol.157.9.3838.Peer-Reviewed Original ResearchAbataceptAmino Acid SequenceAnimalsAntigens, CDAntigens, DifferentiationAortaB7-2 AntigenBase SequenceCells, CulturedCHO CellsCloning, MolecularCricetinaeCricetulusCTLA-4 AntigenDNA, ComplementaryEndothelium, VascularHumansImmunoconjugatesInterleukin-2Lymphocyte ActivationMembrane GlycoproteinsMolecular Sequence DataSequence AlignmentSequence Homology, Amino AcidSpecies SpecificitySwineT-LymphocytesTransfectionUmbilical Veins
1994
cAMP and tumor necrosis factor competitively regulate transcriptional activation through and nuclear factor binding to the cAMP-responsive element/activating transcription factor element of the endothelial leukocyte adhesion molecule-1 (E-selectin) promoter.
De Luca LG, Johnson DR, Whitley MZ, Collins T, Pober JS. cAMP and tumor necrosis factor competitively regulate transcriptional activation through and nuclear factor binding to the cAMP-responsive element/activating transcription factor element of the endothelial leukocyte adhesion molecule-1 (E-selectin) promoter. Journal Of Biological Chemistry 1994, 269: 19193-19196. PMID: 7518452, DOI: 10.1016/s0021-9258(17)32150-6.Peer-Reviewed Original ResearchConceptsConsensus cAMP-responsive elementCRE-binding proteinTranscription factor elementsTranscriptional activationCRE/ATF elementElectrophoretic mobility shift assaysMobility shift assaysTransient transfection assaysAntibody supershift assaysCAMP-responsive elementMigrating formPromoter elementsDNA sequencesFastest migrating formBovine aortic endothelial cellsShift assaysTransfection assaysPromoter responseSupershift assaysGene expressionFactor elementsC-JunAortic endothelial cellsEffects of TNFProtein