2013
Sustained delivery of proangiogenic microRNA‐132 by nanoparticle transfection improves endothelial cell transplantation
Devalliere J, Chang WG, Andrejecsk JW, Abrahimi P, Cheng CJ, Jane‐wit D, Saltzman WM, Pober JS. Sustained delivery of proangiogenic microRNA‐132 by nanoparticle transfection improves endothelial cell transplantation. The FASEB Journal 2013, 28: 908-922. PMID: 24221087, PMCID: PMC3898640, DOI: 10.1096/fj.13-238527.Peer-Reviewed Original ResearchConceptsHuman umbilical vein ECsEndothelial cellsMiR-132MicroRNA-132Cultured human umbilical vein endothelial cellsNumber of microvesselsGrowth factor-induced proliferationHuman umbilical vein endothelial cellsUmbilical vein endothelial cellsEndothelial cell transplantationCultured endothelial cellsEndogenous growth factorsEC transplantationVein endothelial cellsCell transplantationImmunodeficient miceTissue perfusionTransplantationMiR deliveryGrowth factorIntegrin αvβ3Endocytosed nanoparticlesSquare millimeterBiological effectsControl transfectionPericytes modulate endothelial sprouting
Chang WG, Andrejecsk JW, Kluger MS, Saltzman WM, Pober JS. Pericytes modulate endothelial sprouting. Cardiovascular Research 2013, 100: 492-500. PMID: 24042014, PMCID: PMC3826704, DOI: 10.1093/cvr/cvt215.Peer-Reviewed Original ResearchMeSH KeywordsBecaplerminCoculture TechniquesCulture Media, ConditionedHepatocyte Growth FactorHuman Umbilical Vein Endothelial CellsHumansMicrovesselsNeovascularization, PhysiologicParacrine CommunicationPericytesProto-Oncogene Proteins c-bcl-2Proto-Oncogene Proteins c-sisSignal TransductionSpheroids, CellularTime FactorsTransfectionVascular Endothelial Growth Factor A
2000
Caveolin-1 Associates with TRAF2 to Form a Complex That Is Recruited to Tumor Necrosis Factor Receptors*
Feng X, Gaeta M, Madge L, Yang J, Bradley J, Pober J. Caveolin-1 Associates with TRAF2 to Form a Complex That Is Recruited to Tumor Necrosis Factor Receptors*. Journal Of Biological Chemistry 2000, 276: 8341-8349. PMID: 11112773, DOI: 10.1074/jbc.m007116200.Peer-Reviewed Original ResearchConceptsCaveolin-1Confocal fluorescence microscopyIntracellular regionNecrosis factor receptor-associated factor 2TNF receptor 2Receptor-associated factor 2TNF receptor 1Promoter-reporter geneCaveolin-1 associatesFluorescence microscopyProtein caveolin-1Caveolin-1 proteinHuman embryonic kidney 293 cellsIntracellular adapter proteinEmbryonic kidney 293 cellsAbsence of ligandRegions of enrichmentKidney 293 cellsEndogenous TRAF2HEK-293 cellsAdapter proteinCultured human umbilical vein endothelial cellsHuman umbilical vein endothelial cellsPlasma membraneUmbilical vein endothelial cellsThe Death Domain of Tumor Necrosis Factor Receptor 1 Is Necessary but Not Sufficient for Golgi Retention of the Receptor and Mediates Receptor Desensitization
Gaeta M, Johnson D, Kluger M, Pober J. The Death Domain of Tumor Necrosis Factor Receptor 1 Is Necessary but Not Sufficient for Golgi Retention of the Receptor and Mediates Receptor Desensitization. Laboratory Investigation 2000, 80: 1185-1194. PMID: 10950109, DOI: 10.1038/labinvest.3780126.Peer-Reviewed Original ResearchConceptsDeath domainGolgi retentionPlasma membraneC-terminal death domainGolgi apparatusNF-kappaBDominant negative inhibitorWild-type receptorDisparate localizationTNF responseIntracellular domainC-terminusEndothelial cellsNegative inhibitorTNF signalsWild typeTumor necrosis factor receptor 1Chimeric receptorsFactor receptor 1Necrosis factor receptor 1Endogenous receptorsBasal expressionReceptor moleculesType receptorTNF actionCytoprotection of Human Umbilical Vein Endothelial Cells Against Apoptosis and CTL-Mediated Lysis Provided by Caspase-Resistant Bcl-2 Without Alterations in Growth or Activation Responses
Zheng L, Dengler T, Kluger M, Madge L, Schechner J, Maher S, Pober J, Bothwell A. Cytoprotection of Human Umbilical Vein Endothelial Cells Against Apoptosis and CTL-Mediated Lysis Provided by Caspase-Resistant Bcl-2 Without Alterations in Growth or Activation Responses. The Journal Of Immunology 2000, 164: 4665-4671. PMID: 10779771, DOI: 10.4049/jimmunol.164.9.4665.Peer-Reviewed Original ResearchMeSH KeywordsApoptosisCaspasesCell DivisionCell Line, TransformedCells, CulturedCulture Media, ConditionedCytotoxicity, ImmunologicEndothelial Growth FactorsEndothelium, VascularGenetic VectorsGreen Fluorescent ProteinsHumansLuminescent ProteinsProto-Oncogene Proteins c-bcl-2RetroviridaeT-Lymphocytes, CytotoxicTransduction, GeneticTransfectionUmbilical VeinsConceptsGraft endothelial cellsAllograft rejectionBcl-2Endothelial cellsAcute allograft rejectionClass I MHC moleculesNF-kappaB activationHuman umbilical vein endothelial cellsI MHC moleculesUmbilical vein endothelial cellsHost CTLVein endothelial cellsEndothelial injuryAnti-apoptotic gene Bcl-2MHC moleculesGene Bcl-2Induction of apoptosisBcl-2-transduced cellsClass IActivation responseApoptotic effectsCTLHUVECTNFGrowth factor withdrawal
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
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
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 VeinsTranscriptional 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 TNFProteinHLA class I heavy-chain gene promoter elements mediating synergy between tumor necrosis factor and interferons.
Johnson DR, Pober JS. HLA class I heavy-chain gene promoter elements mediating synergy between tumor necrosis factor and interferons. Molecular And Cellular Biology 1994, 14: 1322-1332. PMID: 8289810, PMCID: PMC358487, DOI: 10.1128/mcb.14.2.1322.Peer-Reviewed Original ResearchBase SequenceBinding SitesCloning, MolecularConsensus SequenceDNA PrimersDNA-Binding ProteinsDrug SynergismGene ExpressionGenes, MHC Class IHeLa CellsHLA-B7 AntigenHumansInterferon-betaInterferon-gammaLymphotoxin-alphaMolecular Sequence DataNF-kappa BNuclear ProteinsPolymerase Chain ReactionPromoter Regions, GeneticRecombinant ProteinsSequence DeletionSequence Homology, Nucleic AcidTransfection