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 productsTranscriptionKinasePhosphatidylinositol
1997
TNF initiates E-selectin transcription in human endothelial cells through parallel TRAF-NF-kappa B and TRAF-RAC/CDC42-JNK-c-Jun/ATF2 pathways.
Min W, Pober JS. TNF initiates E-selectin transcription in human endothelial cells through parallel TRAF-NF-kappa B and TRAF-RAC/CDC42-JNK-c-Jun/ATF2 pathways. The Journal Of Immunology 1997, 159: 3508-18. PMID: 9317150, DOI: 10.4049/jimmunol.159.7.3508.Peer-Reviewed Original ResearchMeSH KeywordsActivating Transcription Factor 2Antigens, SurfaceCalcium-Calmodulin-Dependent Protein KinasesCyclic AMP Response Element-Binding ProteinE-SelectinEndothelium, VascularGTP-Binding ProteinsHumansJNK Mitogen-Activated Protein KinasesMitogen-Activated Protein KinasesNF-kappa BPhosphorylationPromoter Regions, GeneticProto-Oncogene Proteins c-junRac GTP-Binding ProteinsReceptors, Tumor Necrosis FactorTranscription FactorsTranscription, GeneticTumor Necrosis Factor Receptor-Associated Peptides and ProteinsTumor Necrosis Factor-alphaUmbilical VeinsConceptsTransient overexpressionHuman endothelial cellsC-JunSelectin transcriptionATF2/c-JunN-terminalATF2 pathwayPromoter-reporter geneKappa B elementCAMP-responsive elementEndothelial cellsDomain phosphorylationEndogenous JNKAdaptor proteinInactive JNKNF-kappa BGene transcriptionGene promoterKappa BJNK activationKinase 1TranscriptionTRAF2 proteinCdc42JNK
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