2015
Complement membrane attack complexes activate noncanonical NF-κB by forming an Akt+NIK+ signalosome on Rab5+ endosomes
Jane-wit D, Surovtseva YV, Qin L, Li G, Liu R, Clark P, Manes TD, Wang C, Kashgarian M, Kirkiles-Smith NC, Tellides G, Pober JS. Complement membrane attack complexes activate noncanonical NF-κB by forming an Akt+NIK+ signalosome on Rab5+ endosomes. Proceedings Of The National Academy Of Sciences Of The United States Of America 2015, 112: 9686-9691. PMID: 26195760, PMCID: PMC4534258, DOI: 10.1073/pnas.1503535112.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBaculoviral IAP Repeat-Containing 3 ProteinClathrinComplement Membrane Attack ComplexCoronary VesselsEndocytosisEndosomesEnzyme StabilityFlow CytometryHuman Umbilical Vein Endothelial CellsHumansHydrazonesInhibitor of Apoptosis ProteinsMice, SCIDNF-kappa BProtein BiosynthesisProtein Serine-Threonine KinasesProto-Oncogene Proteins c-aktRab5 GTP-Binding ProteinsRNA, Small InterferingSecretory VesiclesSignal TransductionTNF Receptor-Associated Factor 3Ubiquitin-Protein LigasesConceptsNF-κB-inducing kinaseMembrane attack complexNoncanonical NF-κBGenome-wide siRNA screenComplement membrane attack complexNIK stabilizationDynamin-dependent mannerNoncanonical NF-κB signalingEndothelial cellsActive Rab5Attack complexSiRNA screenNF-κBAkt activationCytokine-mediated activationNF-κB signalingIκB kinaseSignalosomeRab5EndosomesKinaseAktInternalizationCoronary endothelial cellsActivation
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
Cytokines increase transporter in antigen processing-1 expression more rapidly than HLA class I expression in endothelial cells.
Epperson DE, Arnold D, Spies T, Cresswell P, Pober JS, Johnson DR. Cytokines increase transporter in antigen processing-1 expression more rapidly than HLA class I expression in endothelial cells. The Journal Of Immunology 1992, 149: 3297-301. PMID: 1385520, DOI: 10.4049/jimmunol.149.10.3297.Peer-Reviewed Original Research
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 CompartmentationEndothelium, VascularEnzyme ActivationE-SelectinHistocompatibility 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
1985
Cultured human endothelial cells express platelet-derived growth factor B chain: cDNA cloning and structural analysis
Collins T, Ginsburg D, Boss J, Orkin S, Pober J. Cultured human endothelial cells express platelet-derived growth factor B chain: cDNA cloning and structural analysis. Nature 1985, 316: 748-750. PMID: 4033772, DOI: 10.1038/316748a0.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceBlood VesselsCells, CulturedCloning, MolecularDNAEndotheliumHumansPlatelet-Derived Growth FactorProtein BiosynthesisConceptsHuman endothelial cellsSequence analysisB chainComplementary DNA clonePDGF B-chainApparent relative molecular massEndothelial cellsChains of PDGFRelative molecular massNorthern blot analysisComplete sequence analysisNormal human endothelial cellsPlatelet-derived growth factorPlatelet-derived growth factor B-chainGrowth factor B-chainDNA clonesPrecursor polypeptideCDNA cloningStriking homologyVascular smooth muscle cellsProtein productsMolecular massPolypeptide chainMessenger RNACultured human endothelial cells