2013
Paracrine exchanges of molecular signals between alginate-encapsulated pericytes and freely suspended endothelial cells within a 3D protein gel
Andrejecsk JW, Cui J, Chang WG, Devalliere J, Pober JS, Saltzman WM. Paracrine exchanges of molecular signals between alginate-encapsulated pericytes and freely suspended endothelial cells within a 3D protein gel. Biomaterials 2013, 34: 8899-8908. PMID: 23973174, PMCID: PMC3839675, DOI: 10.1016/j.biomaterials.2013.08.008.Peer-Reviewed Original ResearchConceptsHuman umbilical vein endothelial cellsParacrine signalsFunctioning of tissuesProper survivalEndothelial cellsUmbilical vein endothelial cellsMolecular signalsRegulated deliveryVein endothelial cellsVessel-like structuresLiving cellsProtein gelsHepatocyte growth factorTherapeutic proteinsParacrine exchangesGrowth factorMicrovascular pericytesProteinAngiogenic proteinsCellsVascular tissue engineeringHUVEC behaviorTissue constructsPericytesLocal environment
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 tissuesInterleukin-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
1999
Recent advances in the molecular basis of TNF signal transduction.
Ledgerwood EC, Pober JS, Bradley JR. Recent advances in the molecular basis of TNF signal transduction. Laboratory Investigation 1999, 79: 1041-50. PMID: 10496522.Peer-Reviewed Original Research
1998
Tumor necrosis factor is delivered to mitochondria where a tumor necrosis factor-binding protein is localized.
Ledgerwood EC, Prins JB, Bright NA, Johnson DR, Wolfreys K, Pober JS, O'Rahilly S, Bradley JR. Tumor necrosis factor is delivered to mitochondria where a tumor necrosis factor-binding protein is localized. Laboratory Investigation 1998, 78: 1583-9. PMID: 9881958.Peer-Reviewed Original ResearchMeSH KeywordsAdipocytesAntibodies, MonoclonalCarrier ProteinsCells, CulturedHumansImmunohistochemistryIntracellular MembranesIodine RadioisotopesLysosomesMicroscopy, ImmunoelectronMitochondriaReceptors, Tumor Necrosis FactorReceptors, Tumor Necrosis Factor, Type ITumor Necrosis Factor Decoy ReceptorsTumor Necrosis Factor-alphaU937 CellsConceptsInner mitochondrial membraneExtracellular ligandsMitochondrial membraneTumor necrosis factor receptorIsolated mitochondriaBinding proteinNecrosis factor receptorMitochondriaCell surfaceImmunoelectron microscopyProteinFactor receptorSubcellular fractionsWestern blottingFactor binding proteinTNF effectsPathwayDiverse actionsExogenous TNFTNFR-IIMonoclonal antibodiesTumor necrosis factor binding proteinLysosomesTumor necrosis factorBlotting
1994
cAMP and tumor necrosis factor competitively regulate transcriptional activation through and nuclear factor binding to the cAMP-responsive element/activating transcription factor element of the endothelial leukocyte adhesion molecule-1 (E-selectin) promoter.
De Luca LG, Johnson DR, Whitley MZ, Collins T, Pober JS. cAMP and tumor necrosis factor competitively regulate transcriptional activation through and nuclear factor binding to the cAMP-responsive element/activating transcription factor element of the endothelial leukocyte adhesion molecule-1 (E-selectin) promoter. Journal Of Biological Chemistry 1994, 269: 19193-19196. PMID: 7518452, DOI: 10.1016/s0021-9258(17)32150-6.Peer-Reviewed Original ResearchConceptsConsensus cAMP-responsive elementCRE-binding proteinTranscription factor elementsTranscriptional activationCRE/ATF elementElectrophoretic mobility shift assaysMobility shift assaysTransient transfection assaysAntibody supershift assaysCAMP-responsive elementMigrating formPromoter elementsDNA sequencesFastest migrating formBovine aortic endothelial cellsShift assaysTransfection assaysPromoter responseSupershift assaysGene expressionFactor elementsC-JunAortic endothelial cellsEffects of TNFProtein
1990
Molecular Studies of von Willebrand Disease: Reduced von Willebrand Factor Biosynthesis, Storage, and Release in Endothelial Cells Derived From Patients With Type I von Willebrand Disease
Ewenstein B, Inbal A, Pober J, Handin R. Molecular Studies of von Willebrand Disease: Reduced von Willebrand Factor Biosynthesis, Storage, and Release in Endothelial Cells Derived From Patients With Type I von Willebrand Disease. Blood 1990, 75: 1466-1472. DOI: 10.1182/blood.v75.7.1466.1466.Peer-Reviewed Original ResearchMessenger RNALess messenger RNAVon Willebrand factorEndothelial cellsCultured umbilical vein endothelial cellsRegulated secretionForms of vWDUmbilical vein endothelial cellsStorage organellesFactor biosynthesisVein endothelial cellsMRNA transcriptionVWF proteinMolecular defectsMolecular studiesVWF alleleVon Willebrand diseaseSubsequent translationProteinStorage poolCellsWillebrand diseaseType I von Willebrand diseaseWillebrand factorTranscription
1982
Expression of Ia-like antigens by human vascular endothelial cells is inducible in vitro: demonstration by monoclonal antibody binding and immunoprecipitation.
Pober JS, Gimbrone MA. Expression of Ia-like antigens by human vascular endothelial cells is inducible in vitro: demonstration by monoclonal antibody binding and immunoprecipitation. Proceedings Of The National Academy Of Sciences Of The United States Of America 1982, 79: 6641-6645. PMID: 6815654, PMCID: PMC347184, DOI: 10.1073/pnas.79.21.6641.Peer-Reviewed Original ResearchConceptsHuman vascular endothelial cellsCell shape changesVascular endothelial cellsEndothelial cellsMembrane proteinsCell divisionRadioiodinated membrane proteinsHuman endothelial cellsStandard culture conditionsIntact cellsCultured human endothelial cellsBiochemical demonstrationImmunoprecipitationCulture conditionsConfluent culturesExpressionMonoclonal antibody bindingCellsPrimary culturesShape changesMonoclonal antibodiesLectin phytohemagglutininProteinRegulationImportant implications
1979
Selective labelling of the hydrophobic segments of intrinsic membrane proteins with a lipophilic photogenerated carbene
GOLDMAN D, POBER J, WHITE J, BAYLEY H. Selective labelling of the hydrophobic segments of intrinsic membrane proteins with a lipophilic photogenerated carbene. Nature 1979, 280: 841-843. PMID: 471056, DOI: 10.1038/280841a0.Peer-Reviewed Original ResearchConceptsIntrinsic membrane proteinsMembrane proteinsLipid bilayersCarbon-hydrogen bondsMembrane-associated regionsHydrophobic amino acidsProtein segmentsAryl azidesCarbeneHydrophobic peptidesReactive speciesAryl nitrenesBiological membranesNitreneAmino acidsHydrophobic segmentsHydrocarbon regionProteinGlycophorin ASelective labelingBilayersReagentsLipophilicReactivityAttractive candidate