2001
Akt-Mediated Phosphorylation of the G Protein-Coupled Receptor EDG-1 Is Required for Endothelial Cell Chemotaxis
Lee M, Thangada S, Paik J, Sapkota G, Ancellin N, Chae S, Wu M, Morales-Ruiz M, Sessa W, Alessi D, Hla T. Akt-Mediated Phosphorylation of the G Protein-Coupled Receptor EDG-1 Is Required for Endothelial Cell Chemotaxis. Molecular Cell 2001, 8: 693-704. PMID: 11583630, DOI: 10.1016/s1097-2765(01)00324-0.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsCell LineChemotaxisEndothelium, VascularEnzyme ActivationHumansImmediate-Early ProteinsLysophospholipidsModels, BiologicalNeovascularization, PhysiologicPhosphorylationProtein BindingProtein Serine-Threonine KinasesProtein Structure, TertiaryProto-Oncogene ProteinsProto-Oncogene Proteins c-aktRac GTP-Binding ProteinsReceptors, Cell SurfaceReceptors, G-Protein-CoupledReceptors, LysophospholipidRecombinant Fusion ProteinsSignal TransductionSphingosineConceptsG protein-coupled receptor Edg-1EDG-1Cell migrationRac activationAkt-Mediated PhosphorylationCortical actin assemblyProtein kinase AktThird intracellular loopAkt bindsActin assemblyEndothelial cell migrationKinase AktSpecificity switchEndothelial cell chemotaxisCellular phenomenaDependent signalingIntracellular loopAktCell chemotaxisTransactivationPhosphorylationGPCRsChemotaxisActivationMutantsAkt Down-regulation of p38 Signaling Provides a Novel Mechanism of Vascular Endothelial Growth Factor-mediated Cytoprotection in Endothelial Cells*
Gratton J, Morales-Ruiz M, Kureishi Y, Fulton D, Walsh K, Sessa W. Akt Down-regulation of p38 Signaling Provides a Novel Mechanism of Vascular Endothelial Growth Factor-mediated Cytoprotection in Endothelial Cells*. Journal Of Biological Chemistry 2001, 276: 30359-30365. PMID: 11387313, DOI: 10.1074/jbc.m009698200.Peer-Reviewed Original ResearchMeSH KeywordsAdenoviridaeAnimalsApoptosisBlotting, WesternCattleCell DeathCell LineCell SurvivalCells, CulturedDose-Response Relationship, DrugDown-RegulationEndothelial Growth FactorsEndothelium, VascularEnzyme ActivationEnzyme InhibitorsFlow CytometryHumansImidazolesLymphokinesMitogen-Activated Protein KinasesP38 Mitogen-Activated Protein KinasesPhosphatidylinositol 3-KinasesPhosphorylationProtein BindingProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktPyridinesSignal TransductionTime FactorsUmbilical VeinsVascular Endothelial Growth Factor AVascular Endothelial Growth FactorsConceptsMEKK3 phosphorylationP38 activationMEKK3 kinase activityMitogen-activated protein kinaseP38 mitogen-activated protein kinaseP38-dependent apoptosisP38 MAPK inhibitor SB203580Dominant-negative RacInhibition of PIActivation of MKK3/6Vascular endothelial growth factorMAPK inhibitor SB203580P38 MAPK pathwayP38 MAPK activationEndothelial cellsEndothelial cell survivalGrowth factorRac activationProtein kinaseActive AktPro-apoptotic effectsKinase activityInhibitor SB203580MAPK activationP38 signalingSphingosine 1-Phosphate Activates Akt, Nitric Oxide Production, and Chemotaxis through a GiProtein/Phosphoinositide 3-Kinase Pathway in Endothelial Cells*
Morales-Ruiz M, Lee M, Zöllner S, Gratton J, Scotland R, Shiojima I, Walsh K, Hla T, Sessa W. Sphingosine 1-Phosphate Activates Akt, Nitric Oxide Production, and Chemotaxis through a GiProtein/Phosphoinositide 3-Kinase Pathway in Endothelial Cells*. Journal Of Biological Chemistry 2001, 276: 19672-19677. PMID: 11278592, DOI: 10.1074/jbc.m009993200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, NorthernBlotting, WesternCattleCell MovementChemotaxisCulture Media, Serum-FreeDose-Response Relationship, DrugEndothelial Growth FactorsEndothelium, VascularEnzyme ActivationGenes, DominantGTP-Binding Protein alpha Subunits, Gi-GoLungLymphokinesLysophospholipidsNeovascularization, PhysiologicNitric OxideNitric Oxide SynthaseNitric Oxide Synthase Type IIIPhosphatidylinositol 3-KinasesPhosphorylationProtein BindingProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktReceptors, Cell SurfaceSignal TransductionSphingosineTime FactorsVascular Endothelial Growth Factor AVascular Endothelial Growth FactorsVirulence Factors, BordetellaConceptsEndothelial differentiation gene familySerine/threonine kinase AktHeterotrimeric G proteinsThreonine kinase AktEDG-1 receptorGene familyAkt substrateKinase AktEndothelial cell chemotaxisActivates AktENOS phosphorylationAkt activationG proteinsCell survivalEndothelial nitric oxide synthasePhosphorylationAktCell chemotaxisSppSignalingGrowth factorVascular endothelial growth factorChemotaxisEndothelial cellsSphingosineThe Sonic Hedgehog Receptor Patched Associates with Caveolin-1 in Cholesterol-rich Microdomains of the Plasma Membrane* 210
Karpen H, Bukowski J, Hughes T, Gratton J, Sessa W, Gailani M. The Sonic Hedgehog Receptor Patched Associates with Caveolin-1 in Cholesterol-rich Microdomains of the Plasma Membrane* 210. Journal Of Biological Chemistry 2001, 276: 19503-19511. PMID: 11278759, DOI: 10.1074/jbc.m010832200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesBlotting, WesternCaveolin 1CaveolinsCell MembraneCholesterolCOS CellsDNA, ComplementaryDrosophila ProteinsElectrophoresis, Polyacrylamide GelGlutathione TransferaseHumansImmunohistochemistryMembrane MicrodomainsMembrane ProteinsMicroscopy, ConfocalModels, BiologicalMolecular Sequence DataMutationPatched ReceptorsPrecipitin TestsProtein BindingProtein Structure, TertiaryProtein TransportReceptors, Cell SurfaceReceptors, G-Protein-CoupledRecombinant Fusion ProteinsSignal TransductionSmoothened ReceptorSubcellular FractionsTime FactorsConceptsCholesterol-rich microdomainsRaft microdomainsCaveolin-1Receptor complexEarly embryonic patterningFractionation studiesHedgehog receptor complexCaveolin-enriched microdomainsBuoyant density fractionsEmbryonic patterningHh proteinsLipid raftsSubcellular localizationPlasma membranePatchedPlasmalemmal cholesterolProtein experimentsImmunoprecipitation studiesSmoothenedMicrodomainsConfocal microscopyImmunocytochemistry dataComplexesMembraneDrosophila
2000
Direct Interaction between Endothelial Nitric-oxide Synthase and Dynamin-2 IMPLICATIONS FOR NITRIC-OXIDE SYNTHASE FUNCTION*
Cao S, Yao J, McCabe T, Yao Q, Katusic Z, Sessa W, Shah V. Direct Interaction between Endothelial Nitric-oxide Synthase and Dynamin-2 IMPLICATIONS FOR NITRIC-OXIDE SYNTHASE FUNCTION*. Journal Of Biological Chemistry 2000, 276: 14249-14256. PMID: 11120737, DOI: 10.1074/jbc.m006258200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAortaBlotting, WesternCalcimycinCattleCell LineDose-Response Relationship, DrugDynamin IDynaminsEndothelium, VascularGlutathione TransferaseGolgi ApparatusGTP PhosphohydrolasesIonophoresKineticsMicroscopy, ConfocalMicroscopy, FluorescenceNitric Oxide SynthaseNitric Oxide Synthase Type IIIPrecipitin TestsProtein BindingProtein BiosynthesisRatsRecombinant Fusion ProteinsTransfectionConceptsDynamin 2Bovine aortic endothelial cellsRecombinant eNOS proteinDirect protein-protein interactionDouble-label confocal immunofluorescenceProtein-protein interactionsSpecific protein interactionsDirect interactionClone 9 cellsEndothelial nitric oxide synthaseMembrane compartmentsLarge GTPaseGlutathione S-transferaseProtein interactionsNovel functionDynaminECV-304 cellsSynthase functionIntracellular signalsMembrane distributionConfocal immunofluorescenceFluorescent proteinENOS regulationGreen fluorescentProteinEstrogen Stimulates Heat Shock Protein 90 Binding to Endothelial Nitric Oxide Synthase in Human Vascular Endothelial Cells EFFECTS ON CALCIUM SENSITIVITY AND NO RELEASE*
Russell K, Haynes M, Caulin-Glaser T, Rosneck J, Sessa W, Bender J. Estrogen Stimulates Heat Shock Protein 90 Binding to Endothelial Nitric Oxide Synthase in Human Vascular Endothelial Cells EFFECTS ON CALCIUM SENSITIVITY AND NO RELEASE*. Journal Of Biological Chemistry 2000, 275: 5026-5030. PMID: 10671543, DOI: 10.1074/jbc.275.7.5026.Peer-Reviewed Original ResearchConceptsEndothelial nitric oxide synthaseNitric oxide synthaseHuman umbilical vein endothelial cellsENOS activationOxide synthaseEstrogen receptor antagonist ICINO releaseEndothelium-dependent vasodilationReceptor-mediated modulationReceptor antagonist ICINitric oxide releaseUmbilical vein endothelial cellsVein endothelial cellsAntagonist ICIHeat shock protein 90CGMP productionShock protein 90Oxide releaseEndothelial cellsEndothelial cell effectsCalcium sensitivityCalcium dependenceCell effectsEstrogenProtein 90
1997
Dissecting the Interaction between Nitric Oxide Synthase (NOS) and Caveolin FUNCTIONAL SIGNIFICANCE OF THE NOS CAVEOLIN BINDING DOMAININ VIVO *
Garcı́a-Cardeña G, Martasek P, Masters B, Skidd P, Couet J, Li S, Lisanti M, Sessa W. Dissecting the Interaction between Nitric Oxide Synthase (NOS) and Caveolin FUNCTIONAL SIGNIFICANCE OF THE NOS CAVEOLIN BINDING DOMAININ VIVO *. Journal Of Biological Chemistry 1997, 272: 25437-25440. PMID: 9325253, DOI: 10.1074/jbc.272.41.25437.Peer-Reviewed Original ResearchConceptsCaveolin-1Peripheral membrane proteinsInteraction of eNOSC-terminal tailAmino acids 310Direct interactionCo-transfection experimentsSite-directed mutagenesisNovel functional roleEndothelial nitric oxide synthaseMolecular chaperonesCytoplasmic domainCaveolin isoformsDeletion mutantsMammalian cellsEndothelial cell lysatesGlutathione S-transferaseMembrane proteinsCaveolin-2Coat proteinNegative regulationCaveolin-3Endothelial cellsDirect bindingGolgi region
1996
Endothelial Nitric Oxide Synthase Is Regulated by Tyrosine Phosphorylation and Interacts with Caveolin-1*
García-Cardeña G, Fan R, Stern D, Liu J, Sessa W. Endothelial Nitric Oxide Synthase Is Regulated by Tyrosine Phosphorylation and Interacts with Caveolin-1*. Journal Of Biological Chemistry 1996, 271: 27237-27240. PMID: 8910295, DOI: 10.1074/jbc.271.44.27237.Peer-Reviewed Original ResearchConceptsNovel regulatory mechanismTyrosine phosphorylationCaveolin-1Bovine aortic endothelial cellsRegulatory mechanismsProtein tyrosine phosphatase inhibitorCaveolin-interacting proteinsPhosphoamino acid analysisTyrosine phosphatase inhibitorTreatment of BAECBovine lung microvascular endothelial cellsEndothelial nitric oxide synthaseSubcellular traffickingPhosphatase inhibitorCoat proteinEndothelial cellsMetabolic labelingSodium orthovanadatePhosphorylationCaveolaeAortic endothelial cellsLung microvascular endothelial cellsProteinAcid analysisImmunoprecipitation