2009
TNF Receptors Differentially Signal and Are Differentially Expressed and Regulated in the Human Heart
Al-Lamki R, Brookes AP, Wang J, Reid MJ, Parameshwar J, Goddard MJ, Tellides G, Wan T, Min W, Pober JS, Bradley JR. TNF Receptors Differentially Signal and Are Differentially Expressed and Regulated in the Human Heart. American Journal Of Transplantation 2009, 9: 2679-2696. PMID: 19788501, PMCID: PMC3517885, DOI: 10.1111/j.1600-6143.2009.02831.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisCell CycleCell DeathEndothelium, VascularEnzyme ActivationGraft RejectionHeart TransplantationHumansMAP Kinase Kinase Kinase 5MiceMice, KnockoutMyocardiumMyocytes, CardiacOrgan Culture TechniquesProtein-Tyrosine KinasesReceptors, Tumor Necrosis Factor, Type IReceptors, Tumor Necrosis Factor, Type IIRNA, MessengerTumor Necrosis Factor-alphaConceptsVascular endothelial cellsCardiac allograftsCell cycle entryApoptosis signal-regulating kinase 1Cycle entryExpression of TNFTNFR1 knockoutNecrosis factorTarget cell responseTNFTNF receptorCardiac fibroblastsCell responsesSignal-regulated kinases 1TNF responseASK1 activationMyocardiumEndothelial cellsEpithelial tyrosine kinaseTNFR2Human heartOrgan cultureTNFR1Etk activationAllografts
2001
TNF Signaling in Vascular Endothelial Cells
Madge L, Pober J. TNF Signaling in Vascular Endothelial Cells. Experimental And Molecular Pathology 2001, 70: 317-325. PMID: 11418010, DOI: 10.1006/exmp.2001.2368.Peer-Reviewed Original ResearchConceptsTumor necrosis factorEndothelial cellsProinflammatory cytokine tumor necrosis factorCytokines tumor necrosis factorCultured human endothelial cellsVascular endothelial cellsHuman endothelial cellsNecrosis factorVascular endotheliumIntracellular pathwaysMajor targetTNF signalingCell typesCells
2000
A Phosphatidylinositol 3-Kinase/Akt Pathway, Activated by Tumor Necrosis Factor or Interleukin-1, Inhibits Apoptosis but Does Not Activate NFκB in Human Endothelial Cells*
Madge L, Pober J. A Phosphatidylinositol 3-Kinase/Akt Pathway, Activated by Tumor Necrosis Factor or Interleukin-1, Inhibits Apoptosis but Does Not Activate NFκB in Human Endothelial Cells*. Journal Of Biological Chemistry 2000, 275: 15458-15465. PMID: 10748004, DOI: 10.1074/jbc.m001237200.Peer-Reviewed Original ResearchMeSH KeywordsAndrostadienesApoptosisCells, CulturedChromonesCulture Media, Serum-FreeEndothelium, VascularEnzyme ActivationEnzyme InhibitorsHumansInterleukin-1KineticsMorpholinesNF-kappa BPhosphatidylinositol 3-KinasesProtein Serine-Threonine KinasesProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktRecombinant ProteinsTumor Necrosis Factor-alphaUmbilical VeinsWortmanninConceptsHuman endothelial cellsProtein kinaseStress-activated protein kinaseAkt pathwayMitogen-activated protein kinaseProtein kinase AktPromoter-reporter geneInhibitor of phosphatidylinositolEndothelial cellsSerum-deprived endothelial cellsPhosphorylation of AktGrowth factorAnti-apoptotic pathwaysKinase AktGene productsAnti-apoptotic effectsInhibits ApoptosisSerum deprivationAktLY294002Phospho-AktPro-inflammatory gene productsTranscriptionKinasePhosphatidylinositolIL-11 Activates Human Endothelial Cells to Resist Immune-Mediated Injury
Mahboubi K, Biedermann B, Carroll J, Pober J. IL-11 Activates Human Endothelial Cells to Resist Immune-Mediated Injury. The Journal Of Immunology 2000, 164: 3837-3846. PMID: 10725745, DOI: 10.4049/jimmunol.164.7.3837.Peer-Reviewed Original ResearchMeSH KeywordsAntigens, CDCells, CulturedComplement System ProteinsCytokine Receptor gp130Cytotoxicity, ImmunologicDNA-Binding ProteinsDose-Response Relationship, ImmunologicEndothelium, VascularEnzyme ActivationHumansImmunity, InnateInflammation MediatorsInterleukin-11Interleukin-11 Receptor alpha SubunitMembrane GlycoproteinsMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesNF-kappa BPhosphorylationReceptors, InterleukinReceptors, Interleukin-11Signal TransductionSTAT1 Transcription FactorSTAT3 Transcription FactorT-Lymphocytes, CytotoxicTrans-ActivatorsTyrosineUmbilical VeinsConceptsIL-11Mitogen-activated protein kinaseP44 mitogen-activated protein kinaseImmune-Mediated InjuryCytolytic T lymphocytesNF-kappaB activationGp130-signaling cytokinesInflammatory injuryHuman endothelial cellsIL-11 receptorProinflammatory responseMolecule expressionT lymphocytesICAM-1Maximal responseE-selectinMHC AbsVivo modelNF-kappaBEndothelial cellsTyrosine phosphorylationPhospho-STAT3Cultured HUVECsInjuryKinase 1 inhibitor
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 inhibitors
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
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
Tumor necrosis factor induction of endothelial cell surface antigens is independent of protein kinase C activation or inactivation. Studies with phorbol myristate acetate and staurosporine.
Ritchie AJ, Johnson DR, Ewenstein BM, Pober JS. Tumor necrosis factor induction of endothelial cell surface antigens is independent of protein kinase C activation or inactivation. Studies with phorbol myristate acetate and staurosporine. The Journal Of Immunology 1991, 146: 3056-62. PMID: 1707932, DOI: 10.4049/jimmunol.146.9.3056.Peer-Reviewed Original ResearchMeSH Keywords1-(5-Isoquinolinesulfonyl)-2-MethylpiperazineAlkaloidsCell Adhesion MoleculesCell CompartmentationE-SelectinEndothelium, VascularEnzyme ActivationHistocompatibility Antigens Class IHumansIn Vitro TechniquesIntercellular Adhesion Molecule-1IsoquinolinesPhosphoproteinsPiperazinesProtein BiosynthesisProtein Kinase CRNA, MessengerSignal TransductionStaurosporineTetradecanoylphorbol AcetateTumor Necrosis Factor-alphaConceptsAdhesion molecule-1Intercellular adhesion molecule-1Molecule-1Endothelial leukocyte adhesion molecule-1 expressionProtein kinase CAdhesion molecule-1 expressionEndothelial leukocyte adhesion molecule-1Leukocyte adhesion molecule-1Surface Ag expressionMolecule-1 expressionClass I MHC moleculesClass I MHCEndothelial cell surface antigensAction of TNFI MHC moleculesCell surface antigensNecrosis factor inductionMechanism of actionPhorbol myristate acetatePKC activationTNF effectsI MHCSurface antigenProtein kinase C activationActivation of PKC
1979
Light-regulated enzymes of vertebrate retinal rods.
Pober JS, Bitensky MW. Light-regulated enzymes of vertebrate retinal rods. Advances In Second Messenger And Phosphoprotein Research 1979, 11: 265-301. PMID: 227247.Peer-Reviewed Original Research