2015
Tumor Necrosis Factor Disrupts Claudin-5 Endothelial Tight Junction Barriers in Two Distinct NF-κB-Dependent Phases
Clark PR, Kim RK, Pober JS, Kluger MS. Tumor Necrosis Factor Disrupts Claudin-5 Endothelial Tight Junction Barriers in Two Distinct NF-κB-Dependent Phases. PLOS ONE 2015, 10: e0120075. PMID: 25816133, PMCID: PMC4376850, DOI: 10.1371/journal.pone.0120075.Peer-Reviewed Original ResearchCell Membrane PermeabilityCells, CulturedClaudin-5DermisEndothelium, VascularHuman Umbilical Vein Endothelial CellsHumansMicroscopy, FluorescenceMyosin Light ChainsMyosin-Light-Chain KinaseNF-kappa BPhosphorylationRho-Associated KinasesRNA, Small InterferingSignal TransductionTight JunctionsTumor Necrosis Factor-alpha
2014
Rapamycin antagonizes TNF induction of VCAM-1 on endothelial cells by inhibiting mTORC2
Wang C, Qin L, Manes TD, Kirkiles-Smith NC, Tellides G, Pober JS. Rapamycin antagonizes TNF induction of VCAM-1 on endothelial cells by inhibiting mTORC2. Journal Of Experimental Medicine 2014, 211: 395-404. PMID: 24516119, PMCID: PMC3949571, DOI: 10.1084/jem.20131125.Peer-Reviewed Original ResearchMeSH KeywordsAnalysis of VarianceBlotting, WesternCell AdhesionChromatin ImmunoprecipitationDNA PrimersEndothelial CellsFlow CytometryHumansImmunoblottingMechanistic Target of Rapamycin Complex 2Microscopy, FluorescenceMultiprotein ComplexesOncogene Protein v-aktReal-Time Polymerase Chain ReactionSirolimusT-LymphocytesTOR Serine-Threonine KinasesTumor Necrosis Factor-alphaVascular Cell Adhesion Molecule-1ConceptsVascular cell adhesion molecule-1VCAM-1 expressionEndothelial cellsActivation of ERK1/2Cell adhesion molecule-1TNF inductionInfiltration of leukocytesAdhesion molecule-1Inhibition of TNFPotential therapeutic targetAbility of rapamycinAbility of TNFTranscription factor IRF-1Hyperactivation of ERK1/2Inhibition of ERK1/2Venular flowT cellsEndothelial expressionInflamed tissuesVascular endotheliumMolecule-1Therapeutic targetRapamycin pretreatmentRenal glomeruliTNF
1998
11 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 Research
1996
"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 metabolism
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 ResearchConceptsTumor 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
1988
Tumor necrosis factor and immune interferon act in concert to slow the lateral diffusion of proteins and lipids in human endothelial cell membranes.
Stolpen AH, Golan DE, Pober JS. Tumor necrosis factor and immune interferon act in concert to slow the lateral diffusion of proteins and lipids in human endothelial cell membranes. Journal Of Cell Biology 1988, 107: 781-789. PMID: 3138247, PMCID: PMC2115232, DOI: 10.1083/jcb.107.2.781.Peer-Reviewed Original ResearchClass I major histocompatibility complex proteins diffuse isotropically on immune interferon-activated endothelial cells despite anisotropic cell shape and cytoskeletal organization: application of fluorescence photobleaching recovery with an elliptical beam.
Stolpen AH, Pober JS, Brown CS, Golan DE. Class I major histocompatibility complex proteins diffuse isotropically on immune interferon-activated endothelial cells despite anisotropic cell shape and cytoskeletal organization: application of fluorescence photobleaching recovery with an elliptical beam. Proceedings Of The National Academy Of Sciences Of The United States Of America 1988, 85: 1844-1848. PMID: 3126497, PMCID: PMC279877, DOI: 10.1073/pnas.85.6.1844.Peer-Reviewed Original Research