2001
Expression of Tumor Necrosis Factor Receptors in Normal Kidney and Rejecting Renal Transplants
Al-Lamki R, Wang J, Skepper J, Thiru S, Pober J, Bradley J. Expression of Tumor Necrosis Factor Receptors in Normal Kidney and Rejecting Renal Transplants. Laboratory Investigation 2001, 81: 1503-1515. PMID: 11706058, DOI: 10.1038/labinvest.3780364.Peer-Reviewed Original ResearchMeSH KeywordsAcute DiseaseAntigens, CDColoring AgentsEosine Yellowish-(YS)Fluorescent DyesGene ExpressionGraft RejectionHematoxylinHumansKidneyKidney Failure, ChronicKidney TransplantationMicroscopy, ImmunoelectronReceptors, Tumor Necrosis FactorReceptors, Tumor Necrosis Factor, Type IReceptors, Tumor Necrosis Factor, Type IITumor Necrosis Factor-alphaConceptsDistal convoluted tubuleNormal kidneyTubular epithelial cellsTNFR-1Renal transplantEpithelial cellsTNFR-2Acute cellular rejectionTNFR-1 expressionAcute transplant rejectionTumor necrosis factor receptorEndothelium of glomeruliNecrosis factor receptorInteraction of TNFAcute rejectionCellular rejectionTNFR expressionTransplant rejectionCultured cellsConvoluted tubulesRenal kidneyTNF receptorTNFKidneyHuman kidneyTumor necrosis factor receptor-associated factors (TRAFs)
Bradley J, Pober J. Tumor necrosis factor receptor-associated factors (TRAFs). Oncogene 2001, 20: 6482-6491. PMID: 11607847, DOI: 10.1038/sj.onc.1204788.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsMeSH KeywordsAmino Acid MotifsAnimalsHumansInterleukin-1Protein BindingProtein Structure, TertiaryProteinsReceptors, Tumor Necrosis FactorSignal TransductionTNF Receptor-Associated Factor 1TNF Receptor-Associated Factor 2TNF Receptor-Associated Factor 3TNF Receptor-Associated Factor 4TNF Receptor-Associated Factor 5TNF Receptor-Associated Factor 6Transcription Factor AP-1Tumor Necrosis Factor Receptor-Associated Peptides and ProteinsConceptsTRAF proteinsNecrosis factor receptor-associated factorReceptor-associated factorZinc finger motifsToll/interleukinTumor necrosis factor receptor familyTRAFs 2Finger motifTRAF domainAdaptor proteinCytoplasmic domainFactor receptor familyHomology regionTRAF familyRegulated fashionDownstream eventsSignal transducerCellular responsesCell deathImportant regulatorReceptor familyProteinPathological processesNF-κBDiseased tissues
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 action
1999
Recent advances in the molecular basis of TNF signal transduction.
Ledgerwood EC, Pober JS, Bradley JR. Recent advances in the molecular basis of TNF signal transduction. Laboratory Investigation 1999, 79: 1041-50. PMID: 10496522.Peer-Reviewed Original ResearchMeSH KeywordsApoptosisCell DeathGene Expression RegulationHumansInflammationReceptors, Tumor Necrosis FactorSignal TransductionSphingomyelin PhosphodiesteraseTumor Necrosis Factor-alphaApoptosis-inducing Agents Cause Rapid Shedding of Tumor Necrosis Factor Receptor 1 (TNFR1) A NONPHARMACOLOGICAL EXPLANATION FOR INHIBITION OF TNF-MEDIATED ACTIVATION*
Madge L, Sierra-Honigmann M, Pober J. Apoptosis-inducing Agents Cause Rapid Shedding of Tumor Necrosis Factor Receptor 1 (TNFR1) A NONPHARMACOLOGICAL EXPLANATION FOR INHIBITION OF TNF-MEDIATED ACTIVATION*. Journal Of Biological Chemistry 1999, 274: 13643-13649. PMID: 10224136, DOI: 10.1074/jbc.274.19.13643.Peer-Reviewed Original ResearchMeSH KeywordsApoptosisCalcium-Calmodulin-Dependent Protein KinasesCaspasesCells, CulturedDNA-Binding ProteinsEndothelium, VascularEnzyme ActivationEnzyme InhibitorsHumansI-kappa B ProteinsInterleukin-1Mitogen-Activated Protein KinasesNF-KappaB Inhibitor alphaP38 Mitogen-Activated Protein KinasesProteinsReceptors, Tumor Necrosis FactorSignal TransductionTNF Receptor-Associated Factor 1Tumor Necrosis Factor-alphaConceptsTumor necrosis factor receptor 1Apoptogenic drugsIkappaBalpha degradationTNF-dependent recruitmentBroad spectrum caspase inhibitor zVADfmkInitiation of apoptosisCaspase inhibitor zVADfmkApoptotic cell deathApoptosis-inducing agentsEndothelial cellsTumour necrosis factor signalFactor signalsP38 kinaseTNF signalingEvidence of apoptosisCell deathFactor receptor 1Necrosis factor receptor 1Inhibition of TNFArachidonyl trifluoromethylketoneVascular endothelial cellsApoptosisTRADDEC apoptosisPutative inhibitorsTNF 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
Tumor necrosis factor is delivered to mitochondria where a tumor necrosis factor-binding protein is localized.
Ledgerwood EC, Prins JB, Bright NA, Johnson DR, Wolfreys K, Pober JS, O'Rahilly S, Bradley JR. Tumor necrosis factor is delivered to mitochondria where a tumor necrosis factor-binding protein is localized. Laboratory Investigation 1998, 78: 1583-9. PMID: 9881958.Peer-Reviewed Original ResearchMeSH KeywordsAdipocytesAntibodies, MonoclonalCarrier ProteinsCells, CulturedHumansImmunohistochemistryIntracellular MembranesIodine RadioisotopesLysosomesMicroscopy, ImmunoelectronMitochondriaReceptors, Tumor Necrosis FactorReceptors, Tumor Necrosis Factor, Type ITumor Necrosis Factor Decoy ReceptorsTumor Necrosis Factor-alphaU937 CellsConceptsInner mitochondrial membraneExtracellular ligandsMitochondrial membraneTumor necrosis factor receptorIsolated mitochondriaBinding proteinNecrosis factor receptorMitochondriaCell surfaceImmunoelectron microscopyProteinFactor receptorSubcellular fractionsWestern blottingFactor binding proteinTNF effectsPathwayDiverse actionsExogenous TNFTNFR-IIMonoclonal antibodiesTumor necrosis factor binding proteinLysosomesTumor necrosis factorBlotting11 Tumour necrosis factor is trafficked to a mitochondrial tumour necrosis factor binding protein
Ledgerwood E, Prins J, Bright N, Johnson D, Wolfreys K, Pober J, O'Rahilly S, Bradley J. 11 Tumour necrosis factor is trafficked to a mitochondrial tumour necrosis factor binding protein. Biochemical Society Transactions 1998, 26: s316-s316. PMID: 10047830, DOI: 10.1042/bst026s316.Peer-Reviewed Original ResearchThe 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
1997
TNF initiates E-selectin transcription in human endothelial cells through parallel TRAF-NF-kappa B and TRAF-RAC/CDC42-JNK-c-Jun/ATF2 pathways.
Min W, Pober JS. TNF initiates E-selectin transcription in human endothelial cells through parallel TRAF-NF-kappa B and TRAF-RAC/CDC42-JNK-c-Jun/ATF2 pathways. The Journal Of Immunology 1997, 159: 3508-18. PMID: 9317150, DOI: 10.4049/jimmunol.159.7.3508.Peer-Reviewed Original ResearchMeSH KeywordsActivating Transcription Factor 2Antigens, SurfaceCalcium-Calmodulin-Dependent Protein KinasesCyclic AMP Response Element-Binding ProteinE-SelectinEndothelium, VascularGTP-Binding ProteinsHumansJNK Mitogen-Activated Protein KinasesMitogen-Activated Protein KinasesNF-kappa BPhosphorylationPromoter Regions, GeneticProto-Oncogene Proteins c-junRac GTP-Binding ProteinsReceptors, Tumor Necrosis FactorTranscription FactorsTranscription, GeneticTumor Necrosis Factor Receptor-Associated Peptides and ProteinsTumor Necrosis Factor-alphaUmbilical VeinsConceptsTransient overexpressionHuman endothelial cellsC-JunSelectin transcriptionATF2/c-JunN-terminalATF2 pathwayPromoter-reporter geneKappa B elementCAMP-responsive elementEndothelial cellsDomain phosphorylationEndogenous JNKAdaptor proteinInactive JNKNF-kappa BGene transcriptionGene promoterKappa BJNK activationKinase 1TranscriptionTRAF2 proteinCdc42JNK
1995
Disparate localization of 55-kd and 75-kd tumor necrosis factor receptors in human endothelial cells.
Bradley JR, Thiru S, Pober JS. Disparate localization of 55-kd and 75-kd tumor necrosis factor receptors in human endothelial cells. American Journal Of Pathology 1995, 146: 27-32. PMID: 7856733, PMCID: PMC1870772.Peer-Reviewed Original ResearchMeSH KeywordsAntibodies, MonoclonalCells, CulturedEndothelium, VascularHumansMicroscopy, FluorescenceMicroscopy, ImmunoelectronMolecular WeightReceptors, Tumor Necrosis FactorUmbilical VeinsConceptsTumor necrosis factor receptorNecrosis factor receptorCell surfaceFactor receptorConfocal immunofluorescence microscopyDisparate localizationUndergoes endocytosisCultured human umbilical vein endothelial cellsHuman umbilical vein endothelial cellsEndothelial cellsUmbilical vein endothelial cellsReceptor clusteringGolgi apparatusHuman endothelial cellsCoated vesiclesVein endothelial cellsImmunofluorescence microscopyCellular distributionTNF receptorEndothelial cell activationCell activationReceptorsCytoplasmic vacuolesCellsEndocytosis
1993
Tumor necrosis factor activates human endothelial cells through the p55 tumor necrosis factor receptor but the p75 receptor contributes to activation at low tumor necrosis factor concentration.
Slowik MR, De Luca LG, Fiers W, Pober JS. Tumor necrosis factor activates human endothelial cells through the p55 tumor necrosis factor receptor but the p75 receptor contributes to activation at low tumor necrosis factor concentration. American Journal Of Pathology 1993, 143: 1724-30. PMID: 7504889, PMCID: PMC1887273.Peer-Reviewed Original ResearchConceptsEndothelial leukocyte adhesion molecule-1Endothelial cellsHuman endothelial cellsTumor necrosis factor concentrationsMonoclonal antibodiesNecrosis factor concentrationsLeukocyte adhesion molecule-1Major histocompatibility complex moleculesActivation of ECTumor necrosis factorAdhesion molecule-1Class I major histocompatibility complex moleculesLeukocyte adhesion moleculesTumor necrosis factor receptorELAM-1 inductionRecombinant human TNFHistocompatibility complex moleculesNecrosis factor receptorCultured endothelial cellsP75 receptorTumor necrosisNecrosis factorMolecule-1Receptor typesTNF receptorFour different classes of inhibitors of receptor-mediated endocytosis decrease tumor necrosis factor-induced gene expression in human endothelial cells.
Bradley JR, Johnson DR, Pober JS. Four different classes of inhibitors of receptor-mediated endocytosis decrease tumor necrosis factor-induced gene expression in human endothelial cells. The Journal Of Immunology 1993, 150: 5544-55. PMID: 8390537, DOI: 10.4049/jimmunol.150.12.5544.Peer-Reviewed Original ResearchConceptsIFN-gamma-mediated inductionELAM-1Human endothelial cellsEndothelial cellsMHC moleculesReceptor-mediated endocytosisCytokine-inducible moleculesAnti-inflammatory therapyIL-1-induced increaseClass II MHC moleculesICAM-1 expressionClass I MHC moleculesVCAM-1 expressionCultured human endothelial cellsII MHC moleculesI MHC moleculesNew potential targetsICAM-1VCAM-1Levels of mRNADensity lipoproteinExposure of cellsTNFGene expressionTNF induction
1991
Tumor necrosis factor regulation of major histocompatibility complex gene expression
Johnson D, Pober J. Tumor necrosis factor regulation of major histocompatibility complex gene expression. Immunologic Research 1991, 10: 141. PMID: 1655923, DOI: 10.1007/bf02918161.Peer-Reviewed Original ResearchAnimalsBase SequenceGene Expression RegulationHumansMajor Histocompatibility ComplexMiceMolecular Sequence DataOncogenesReceptors, Cell SurfaceReceptors, Tumor Necrosis FactorRNA Processing, Post-TranscriptionalSecond Messenger SystemsSequence Homology, Nucleic AcidTranscription FactorsTranscription, GeneticTumor Necrosis Factor-alpha
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