1998
The N-terminal domains target TNF receptor-associated factor-2 to the nucleus and display transcriptional regulatory activity.
Min W, Bradley JR, Galbraith JJ, Jones SJ, Ledgerwood EC, Pober JS. The N-terminal domains target TNF receptor-associated factor-2 to the nucleus and display transcriptional regulatory activity. The Journal Of Immunology 1998, 161: 319-24. PMID: 9647239, DOI: 10.4049/jimmunol.161.1.319.Peer-Reviewed Original ResearchMeSH KeywordsBiological TransportCell NucleusCells, CulturedCytoplasmEndothelium, VascularFluorescent Antibody Technique, IndirectHumansPeptide FragmentsProtein BiosynthesisProtein Structure, TertiaryProteinsReceptors, Tumor Necrosis FactorTNF Receptor-Associated Factor 2Transcription, GeneticTransfectionUmbilical VeinsConceptsFinger domainAmino-terminal RING finger domainNuclear localizationTNF receptor-associated factor 2Cytoplasmic signal transductionReceptor-associated factor 2Zinc finger domainTranscriptional regulatory activityAmino-terminal halfC-Jun N-terminal kinase (JNK) activationRING finger domainProminent nuclear localizationConfocal immunofluorescence microscopyWestern blottingTRAF2 moleculeAdaptor proteinDeletion mutantsSignal transductionSubcellular localizationGene transcriptionKinase activationHuman endothelial cellsTRAF2 proteinCell extractsHuman endothelial cell line
1996
A Sustained Reduction in IκB-β May Contribute to Persistent NF-κB Activation in Human Endothelial Cells*
Johnson D, Douglas I, Jahnke A, Ghosh S, Pober J. A Sustained Reduction in IκB-β May Contribute to Persistent NF-κB Activation in Human Endothelial Cells*. Journal Of Biological Chemistry 1996, 271: 16317-16322. PMID: 8663191, DOI: 10.1074/jbc.271.27.16317.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceBinding SitesCell Adhesion MoleculesCell MembraneCell NucleusCells, CulturedConsensus SequenceCytosolDNADNA-Binding ProteinsEndothelium, VascularGene ExpressionHistocompatibility Antigens Class IHumansI-kappa B ProteinsIntercellular Adhesion Molecule-1Interleukin-1KineticsMolecular Sequence DataNF-kappa BOligodeoxyribonucleotidesTetradecanoylphorbol AcetateTumor Necrosis Factor-alphaUmbilical VeinsVascular Cell Adhesion Molecule-1ConceptsAdhesion molecule-1Vascular cell adhesion molecule-1Intercellular adhesion molecule-1Cell adhesion molecule-1Phorbol myristate acetateInterleukin-1alphaNF-kappaB activationMolecule-1Sustained reductionNF-kappaBEndothelial cellsIkappaB-alphaIkappaB-betaHuman endothelial cellsHuman leukocyte antigen (HLA) class INF-kappaB.Inhibitory protein IkappaB-alphaCell surface molecule expressionIkappaB-beta degradationPersistent NF-κB activationSurface molecule expressionAntigen class INF-κB activationIkappaB-beta levelsDe novo expression"Cytosolic" phospholipase A2 is in the nucleus of subconfluent endothelial cells but confined to the cytoplasm of confluent endothelial cells and redistributes to the nuclear envelope and cell junctions upon histamine stimulation.
Sierra-Honigmann MR, Bradley JR, Pober JS. "Cytosolic" phospholipase A2 is in the nucleus of subconfluent endothelial cells but confined to the cytoplasm of confluent endothelial cells and redistributes to the nuclear envelope and cell junctions upon histamine stimulation. Laboratory Investigation 1996, 74: 684-95. PMID: 8600319.Peer-Reviewed Original ResearchConceptsSubconfluent endothelial cellsConfluent endothelial cellsNuclear envelopeNuclear localizationConfocal immunofluorescence microscopyEndothelial cellsDose-dependent redistributionGrowth-arrested cellsSubcellular localizationCell density dependencePlasma membraneCell cycleCytoplasmic enzymeNuclear extractsCell junctionsPhospholipase A2 enzymeBovine endothelial cellsHeLa cellsImmunofluorescence microscopyCell lysatesCell nucleiIntercellular junctionsSubconfluent cellsPredominant MrAcid metabolismTranscriptional Regulation of the Interleukin-2 Gene in Normal Human Peripheral Blood T Cells CONVERGENCE OF COSTIMULATORY SIGNALS AND DIFFERENCES FROM TRANSFORMED T CELLS (∗)
Hughes C, Pober J. Transcriptional Regulation of the Interleukin-2 Gene in Normal Human Peripheral Blood T Cells CONVERGENCE OF COSTIMULATORY SIGNALS AND DIFFERENCES FROM TRANSFORMED T CELLS (∗). Journal Of Biological Chemistry 1996, 271: 5369-5377. PMID: 8621390, DOI: 10.1074/jbc.271.10.5369.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceBinding SitesB-LymphocytesCD3 ComplexCell Line, TransformedCell NucleusCells, CulturedFlow CytometryGene Expression RegulationHumansInterleukin-2KineticsLuciferasesLymphocyte ActivationMolecular Sequence DataNF-kappa BPromoter Regions, GeneticRecombinant ProteinsRegulatory Sequences, Nucleic AcidSignal TransductionT-LymphocytesTranscription FactorsTranscription, GeneticTransfectionTumor Cells, CulturedConceptsNormal T cellsT cellsCostimulatory signalsDifferent costimulatory signalsT cell receptorActivated T-cells (NFAT) sitesNormal human T cellsHuman T cellsT cell sitesTransformed T cellsCD2 antibodiesNF-kappaB siteAccessory cellsTumor cell linesCell receptorInterleukin-2 geneNuclear factorPrimary activationIL-2 promoterJurkat T cellsProximal AP-1 siteCell linesAntibodiesAP-1 siteTranscriptional regulation
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
1990
Tumor necrosis factor and immune interferon synergistically increase transcription of HLA class I heavy- and light-chain genes in vascular endothelium.
Johnson DR, Pober JS. Tumor necrosis factor and immune interferon synergistically increase transcription of HLA class I heavy- and light-chain genes in vascular endothelium. Proceedings Of The National Academy Of Sciences Of The United States Of America 1990, 87: 5183-5187. PMID: 2164225, PMCID: PMC54286, DOI: 10.1073/pnas.87.13.5183.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceCell NucleusCells, CulturedDrug SynergismEndothelium, VascularFlow CytometryGenes, MHC Class IHistocompatibility Antigens Class IHumansInterferon Type IInterferon-gammaMacromolecular SubstancesMolecular Sequence DataReceptors, Cell SurfaceReceptors, Tumor Necrosis FactorRecombinant ProteinsRNA, MessengerSequence Homology, Nucleic AcidTranscription, GeneticTumor Necrosis Factor-alphaConceptsNecrosis factorHuman endothelial cellsEndothelial cellsClass IInterferon gammaImmune interferonMRNA levelsMajor histocompatibility complex moleculesTumor necrosis factorHLA class IClass I major histocompatibility complex moleculesCultured human endothelial cellsHistocompatibility complex moleculesUntreated endothelial cellsSynergistic increase