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
1989
IL-1 and related cytokines enhance thrombin-stimulated PGI2 production in cultured endothelial cells without affecting thrombin-stimulated von Willebrand factor secretion or platelet-activating factor biosynthesis.
Zavoico GB, Ewenstein BM, Schafer AI, Pober JS. IL-1 and related cytokines enhance thrombin-stimulated PGI2 production in cultured endothelial cells without affecting thrombin-stimulated von Willebrand factor secretion or platelet-activating factor biosynthesis. The Journal Of Immunology 1989, 142: 3993-9. PMID: 2497185, DOI: 10.4049/jimmunol.142.11.3993.Peer-Reviewed Original ResearchMeSH KeywordsArachidonic AcidArachidonic AcidsCells, CulturedChromatography, Thin LayerCycloheximideDrug SynergismEndothelium, VascularEpoprostenolHistamineHumansInterleukin-1Platelet Activating FactorProstaglandin Endoperoxides, SyntheticProstaglandin H2Prostaglandins HThrombinVon Willebrand Factor