2020
Complement Membrane Attack Complex New Roles, Mechanisms of Action, and Therapeutic Targets
Xie CB, Jane-Wit D, Pober JS. Complement Membrane Attack Complex New Roles, Mechanisms of Action, and Therapeutic Targets. American Journal Of Pathology 2020, 190: 1138-1150. PMID: 32194049, PMCID: PMC7280757, DOI: 10.1016/j.ajpath.2020.02.006.Peer-Reviewed Original ResearchConceptsMembrane attack complexMAC assemblyExpression of inhibitorMechanism of actionFacilitate secretionDependent transcriptionPlasma membraneIntracellular signalingComplement membrane attack complexAbsence of lysisSignalingRecent insightsBiophysical propertiesComplement-mediated diseasesAttack complexTherapeutic targetCell activationDisease pathogenesisAdaptive immunityNew roleIL-18IL-1βCytolytic effectorsProinflammatory effectsProinflammatory proteins
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
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
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