2015
Efficient Gene Disruption in Cultured Primary Human Endothelial Cells by CRISPR/Cas9
Abrahimi P, Chang WG, Kluger MS, Qyang Y, Tellides G, Saltzman WM, Pober JS. Efficient Gene Disruption in Cultured Primary Human Endothelial Cells by CRISPR/Cas9. Circulation Research 2015, 117: 121-128. PMID: 25940550, PMCID: PMC4490936, DOI: 10.1161/circresaha.117.306290.Peer-Reviewed Original ResearchAnimalsCD4-Positive T-LymphocytesCell SeparationCells, CulturedCRISPR-Cas SystemsEndothelial Progenitor CellsFemaleFetal BloodGene DeletionGene Knockout TechniquesGenes, MHC Class IIGenetic VectorsHLA-DR AntigensHumansIntracellular Signaling Peptides and ProteinsLentivirusLymphocyte ActivationLymphocyte Culture Test, MixedMiceMice, SCIDNuclear ProteinsPrimary Cell CultureProteinsTetracyclineTrans-ActivatorsVesicular Transport Proteins
2001
Tumor 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 tissuesSuppression of Vascular Endothelial Growth Factor-Mediated Endothelial Cell Protection by Survivin Targeting
Mesri M, Morales-Ruiz M, Ackermann E, Bennett C, Pober J, Sessa W, Altieri D. Suppression of Vascular Endothelial Growth Factor-Mediated Endothelial Cell Protection by Survivin Targeting. American Journal Of Pathology 2001, 158: 1757-1765. PMID: 11337373, PMCID: PMC1891951, DOI: 10.1016/s0002-9440(10)64131-4.Peer-Reviewed Original ResearchApoptosisCell MovementCells, CulturedDNADNA, AntisenseDose-Response Relationship, DrugEndothelial Growth FactorsEndothelium, VascularGene Expression RegulationHumansInhibitor of Apoptosis ProteinsLymphokinesMicrotubule-Associated ProteinsNeoplasm ProteinsProteinsRNA, MessengerSurvivinVascular Endothelial Growth Factor AVascular Endothelial Growth FactorsInterleukin-11 Up-Regulates Survivin Expression in Endothelial Cells through a Signal Transducer and Activator of Transcription-3 Pathway
Mahboubi K, Li F, Plescia J, Kirkiles-Smith N, Mesri M, Du Y, Carroll J, Elias J, Altieri D, Pober J. Interleukin-11 Up-Regulates Survivin Expression in Endothelial Cells through a Signal Transducer and Activator of Transcription-3 Pathway. Laboratory Investigation 2001, 81: 327-334. PMID: 11310826, DOI: 10.1038/labinvest.3780241.Peer-Reviewed Original ResearchMeSH KeywordsDNA-Binding ProteinsEndothelium, VascularGene ExpressionHumansInhibitor of Apoptosis ProteinsInterleukin-11Microtubule-Associated ProteinsNeoplasm ProteinsPhosphorylationProteinsRNA, MessengerSerineSignal TransductionSTAT1 Transcription FactorSTAT3 Transcription FactorSurvivinTrans-ActivatorsTranscription, GeneticTransgenesUmbilical VeinsConceptsSignal transducerProtein kinase B/AktDominant-negative STAT3 mutantActivator of transcriptionSurvivin mRNA expressionTranscription 3 (STAT3) pathwayIL-11Survivin protein expressionSTAT3 mutantStimulation of serumProtein expression levelsSurvivin inductionSurvivin expressionAntiapoptotic proteinsInduces expressionMRNA expressionExpression levelsSurvivin proteinProtein expressionCritical mediatorMaximal inductionExpressionSurvivin mRNAProteinDose-dependent manner
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 cellsControl of Apoptosis during Angiogenesis by Survivin Expression in Endothelial Cells
O'Connor D, Schechner J, Adida C, Mesri M, Rothermel A, Li F, Nath A, Pober J, Altieri D. Control of Apoptosis during Angiogenesis by Survivin Expression in Endothelial Cells. American Journal Of Pathology 2000, 156: 393-398. PMID: 10666367, PMCID: PMC1850029, DOI: 10.1016/s0002-9440(10)64742-6.Peer-Reviewed Original ResearchMeSH KeywordsApoptosisCell DivisionCell SurvivalCells, CulturedEndothelial Growth FactorsEndothelium, VascularFibroblast Growth Factor 2HumansInhibitor of Apoptosis ProteinsLymphokinesMicrotubule-Associated ProteinsMitogensNeoplasm ProteinsNeovascularization, PhysiologicProteinsSurvivinVascular Endothelial Growth Factor AVascular Endothelial Growth FactorsConceptsTumor necrosis factor alpha/cycloheximideControl of apoptosisEndothelial cellsSurvivin expressionQuiescent endothelial cellsEndothelial cell survivalGrowth factorApoptosis inhibitor survivinTwo-dimensional cultureCaspase-3 activityRecombinant expressionFibroblast growth factorBasic fibroblast growth factorCell survivalStrong inductionProtein survivinPathological angiogenesisProtective genesRNA expressionVascular tubesSurvivinExpressionVascular endothelial growth factorApoptosisCells
1999
Apoptosis-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
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
1992
Thrombin and histamine rapidly stimulate the phosphorylation of the myristoylated alanine‐rich C‐kinase substrate in human umbilical vein endothelial cells: Evidence for distinct patterns of protein kinase activation
Jacobson B, Pober J, Fenton J, Ewenstein B. Thrombin and histamine rapidly stimulate the phosphorylation of the myristoylated alanine‐rich C‐kinase substrate in human umbilical vein endothelial cells: Evidence for distinct patterns of protein kinase activation. Journal Of Cellular Physiology 1992, 152: 166-176. PMID: 1320036, DOI: 10.1002/jcp.1041520121.Peer-Reviewed Original ResearchMeSH KeywordsCells, CulturedDose-Response Relationship, DrugElectrophoresis, Polyacrylamide GelEndothelium, VascularEnzyme ActivationHistamineHumansIntracellular Signaling Peptides and ProteinsMembrane ProteinsMolecular WeightMyristoylated Alanine-Rich C Kinase SubstratePhosphorylationPrecipitin TestsProtein KinasesProteinsReceptors, Cell SurfaceThrombin
1991
Identification of a novel high molecular weight protein preferentially expressed by sinusoidal endothelial cells in normal human tissues.
Goerdt S, Walsh LJ, Murphy GF, Pober JS. Identification of a novel high molecular weight protein preferentially expressed by sinusoidal endothelial cells in normal human tissues. Journal Of Cell Biology 1991, 113: 1425-1437. PMID: 2045420, PMCID: PMC2289031, DOI: 10.1083/jcb.113.6.1425.Peer-Reviewed Original ResearchConceptsSinusoidal endothelial cellsEndothelial cellsPeripheral blood mononuclear cellsMS-1 antigenDendritic cell populationsEndothelial cell antigensBlood mononuclear cellsHigh endothelial venulesHuman umbilical vein endothelial cellsUmbilical vein endothelial cellsVein endothelial cellsLymph nodesKG-1 cellsNormal human tissuesMononuclear cellsLymphoid tissueAdrenal cortexEndothelial venulesCell line KG-1Cell line U937Cell antigensSplenic tissueSinusoidal endotheliumSplenic extractSpleen
1986
Two distinct monokines, interleukin 1 and tumor necrosis factor, each independently induce biosynthesis and transient expression of the same antigen on the surface of cultured human vascular endothelial cells.
Pober JS, Bevilacqua MP, Mendrick DL, Lapierre LA, Fiers W, Gimbrone MA. Two distinct monokines, interleukin 1 and tumor necrosis factor, each independently induce biosynthesis and transient expression of the same antigen on the surface of cultured human vascular endothelial cells. The Journal Of Immunology 1986, 136: 1680-7. PMID: 3485132, DOI: 10.4049/jimmunol.136.5.1680.Peer-Reviewed Original Research