2023
An optogenetic-phosphoproteomic study reveals dynamic Akt1 signaling profiles in endothelial cells
Zhou W, Li W, Wang S, Salovska B, Hu Z, Tao B, Di Y, Punyamurtula U, Turk B, Sessa W, Liu Y. An optogenetic-phosphoproteomic study reveals dynamic Akt1 signaling profiles in endothelial cells. Nature Communications 2023, 14: 3803. PMID: 37365174, PMCID: PMC10293293, DOI: 10.1038/s41467-023-39514-1.Peer-Reviewed Original ResearchConceptsPhosphorylation sitesSerine/threonine kinase AktMass spectrometry-based phosphoproteomicsThreonine kinase AktAkt-dependent phosphorylationAberrant Akt activationEndothelial cellsKinase substrateKinase AktCell signalingPhosphorylation profilePhenotypic outcomesDownstream signalingAkt activationAkt1 phosphorylationHuman diseasesSystem-level analysisAKT1Vascular endothelial cellsRich resourcePhosphorylationSignalingGrowth factorAktCells
2021
The loss of DHX15 impairs endothelial energy metabolism, lymphatic drainage and tumor metastasis in mice
Ribera J, Portolés I, Córdoba-Jover B, Rodríguez-Vita J, Casals G, González-de la Presa B, Graupera M, Solsona-Vilarrasa E, Garcia-Ruiz C, Fernández-Checa JC, Soria G, Tudela R, Esteve-Codina A, Espadas G, Sabidó E, Jiménez W, Sessa WC, Morales-Ruiz M. The loss of DHX15 impairs endothelial energy metabolism, lymphatic drainage and tumor metastasis in mice. Communications Biology 2021, 4: 1192. PMID: 34654883, PMCID: PMC8519955, DOI: 10.1038/s42003-021-02722-w.Peer-Reviewed Original ResearchConceptsKey cellular processesIntracellular ATP productionCellular processesZebrafish embryosDownstream substratesATP biosynthesisProteome analysisMitochondrial membraneEndothelial cellsDHX15ATP productionRegulatory functionsDifferential expressionComplex IVascular regulatory functionEnergy metabolismVascular biologyTumor metastasisTherapeutical targetGene deficiencyPrimary tumor growthLower oxygen consumptionVascular physiologyDownregulation of VEGFCells
2001
Distinction between signaling mechanisms in lipid rafts vs. caveolae
Sowa G, Pypaert M, Sessa W. Distinction between signaling mechanisms in lipid rafts vs. caveolae. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 14072-14077. PMID: 11707586, PMCID: PMC61169, DOI: 10.1073/pnas.241409998.Peer-Reviewed Original ResearchConceptsCav-1Raft domainsLipid raftsCholesterol-rich lipid raft domainsLipid raft domainsCaveolae assemblyEndothelial nitric oxide synthaseCaveolae biogenesisAcylated proteinsSignal transductionSpatial regulationPlasma membraneNegative regulationCaveolin-1CaveolaeFirst clear exampleRaftsPhysical interactionProteinCellsRegulationENOS functionBiogenesisDomainClear exampleDynamic regulation of metabolism and respiration by endogenously produced nitric oxide protects against oxidative stress
Paxinou E, Weisse M, Chen Q, Souza J, Hertkorn C, Selak M, Daikhin E, Yudkoff M, Sowa G, Sessa W, Ischiropoulos H. Dynamic regulation of metabolism and respiration by endogenously produced nitric oxide protects against oxidative stress. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 11575-11580. PMID: 11562476, PMCID: PMC58771, DOI: 10.1073/pnas.201293198.Peer-Reviewed Original ResearchConceptsEndothelial nitric oxide synthaseNitric oxideOxidative stressProtective effectNitric oxide protectsNitric oxide synthaseNitric oxide synthesisECV304 cellsSteady-state levelsMechanism of protectionOxide synthaseOxide synthesisENOS cDNAHuman ECV304 cellsMitochondria respirationDeathMitochondrial respirationExposureSame extentCellsCell metabolismDynamic regulationMetabolismLow steady-state levelsGlycolytic pathway
2000
In vivo delivery of the caveolin-1 scaffolding domain inhibits nitric oxide synthesis and reduces inflammation
Bucci M, Gratton J, Rudic R, Acevedo L, Roviezzo F, Cirino G, Sessa W. In vivo delivery of the caveolin-1 scaffolding domain inhibits nitric oxide synthesis and reduces inflammation. Nature Medicine 2000, 6: 1362-1367. PMID: 11100121, DOI: 10.1038/82176.Peer-Reviewed Original ResearchConceptsCaveolin-1Signal transductionSmall-molecule mimicryCaveolae assemblyInternalization sequenceCoat proteinEndothelial cellsPhysiological importanceEndothelial nitric oxide synthase (eNOS) inhibitorTransductionCholesterol transportNitric oxide synthase inhibitorChimeric peptideInhibits nitric oxide synthesisOxide synthase inhibitorNitric oxide synthesisNew therapeutic approachesNitric oxide productionSelective inhibitionDomainPeptidesCaveolinAcute inflammationCellsSystemic administrationAngiopoietin-1 Inhibits Endothelial Cell Apoptosis via the Akt/Survivin Pathway*
Papapetropoulos A, Fulton D, Mahboubi K, Kalb R, O'Connor D, Li F, Altieri D, Sessa W. Angiopoietin-1 Inhibits Endothelial Cell Apoptosis via the Akt/Survivin Pathway*. Journal Of Biological Chemistry 2000, 275: 9102-9105. PMID: 10734041, DOI: 10.1074/jbc.275.13.9102.Peer-Reviewed Original ResearchMeSH KeywordsAngiopoietin-1AnimalsApoptosisCattleCells, CulturedEndothelium, VascularFlow CytometryInhibitor of Apoptosis ProteinsMembrane GlycoproteinsMicrotubule-Associated ProteinsNeoplasm ProteinsPhosphorylationProtein Serine-Threonine KinasesProteinsProto-Oncogene ProteinsProto-Oncogene Proteins c-aktSurvivinConceptsAkt/survivin pathwaySerine-threonine kinaseDeath-inducing stimuliPost-natal angiogenesisDominant-negative survivinEndothelial cellsEndothelial cell survivalAnti-apoptotic pathwaysSurvival machineryEndothelial cell apoptosisSurvivin pathwayApoptosis inhibitorCell survivalCell apoptosisVascular stabilizationAktSurvivinTie-2 receptorAngiogenic responseApoptosisCellsPathwayAngiogenesisMorphogenesisKinase
1998
Neuronal nitric oxide synthase is expressed in principal cell of collecting duct
Wang X, Lu M, Gao Y, Papapetropoulos A, Sessa W, Wang W. Neuronal nitric oxide synthase is expressed in principal cell of collecting duct. American Journal Of Physiology 1998, 275: f395-f399. PMID: 9729512, DOI: 10.1152/ajprenal.1998.275.3.f395.Peer-Reviewed Original ResearchConceptsNeuronal nitric oxide synthaseEndothelial nitric oxide synthasePresence of nNOSNitric oxide synthaseOxide synthasePrincipal cellsImmunocytochemical studyPresence of mRNART-PCR techniqueRat neuronal nitric oxide synthaseNegative immunostainingNNOS antibodyRat CCDRat kidneyImmunocytochemical methodsRT-PCRImmunoreactivityRatsDietCellsLight microscopyDuctSynthaseGene-specific primersKidney
1996
Reduced Gene Expression of Vascular Endothelial NO Synthase and Cyclooxygenase-1 in Heart Failure
Smith C, Sun D, Hoegler C, Roth B, Zhang X, Zhao G, Xu X, Kobari Y, Pritchard K, Sessa W, Hintze T. Reduced Gene Expression of Vascular Endothelial NO Synthase and Cyclooxygenase-1 in Heart Failure. Circulation Research 1996, 78: 58-64. PMID: 8603506, DOI: 10.1161/01.res.78.1.58.Peer-Reviewed Original ResearchConceptsHeart failureCyclooxygenase-1Von Willebrand factorPacing-induced heart failureVentricular end-diastolic pressureEndothelial cellsEndothelium-dependent responsesEnd-diastolic pressureLeft ventricular pacingPeripheral blood vesselsDiastolic pressureVentricular pacingThoracic aortaClinical signsMongrel dogsWestern blottingBlood vesselsWillebrand factorArbitrary unitsEcNOSTotal RNADogsPresent studyFailureCellsPalmitoylation of Endothelial Nitric Oxide Synthase Is Necessary for Optimal Stimulated Release of Nitric Oxide: Implications for Caveolae Localization †
Liu J, García-Cardeña G, Sessa W. Palmitoylation of Endothelial Nitric Oxide Synthase Is Necessary for Optimal Stimulated Release of Nitric Oxide: Implications for Caveolae Localization †. Biochemistry 1996, 35: 13277-13281. PMID: 8873592, DOI: 10.1021/bi961720e.Peer-Reviewed Original ResearchConceptsPalmitoylation-deficient mutantMembrane associationN-myristoylationWT enzymeLocalization of eNOSActivation of eNOSEndothelial nitric oxide synthaseCaveolae membranesCaveolar localizationPalmitoylationCysteine palmitoylationWT proteinGolgi complexMutantsIntact cellsCaveolaeVivo significanceHigh saltEnzymeCellsSynthaseNitric oxide synthaseTriton XLocalizationImportant role
1995
The Golgi Association of Endothelial Nitric Oxide Synthase Is Necessary for the Efficient Synthesis of Nitric Oxide(∗)
Sessa W, Garca-Cardea G, Liu J, Keh A, Pollock J, Bradley J, Thiru S, Braverman I, Desai K. The Golgi Association of Endothelial Nitric Oxide Synthase Is Necessary for the Efficient Synthesis of Nitric Oxide(∗). Journal Of Biological Chemistry 1995, 270: 17641-17644. PMID: 7543089, DOI: 10.1074/jbc.270.30.17641.Peer-Reviewed Original ResearchConceptsHEK-293 cellsHeterologous expression systemEndothelial nitric oxide synthaseNovel GolgiGolgi associationExpression systemIntracellular signalsCultured endothelial cellsGolgiIntact blood vesselsEnzymeParticulate enzymeProteinEndothelial cellsCellsSynthaseNitric oxide synthaseOxide synthaseBlood vesselsCompartmentalizationNitric oxideTarget
1990
Inhibition by l‐glutamine of the release of endothelium‐derived relaxing factor from cultured endothelial cells
Hecker M, Mitchell J, Swierkosz T, Sessa W, Vane J. Inhibition by l‐glutamine of the release of endothelium‐derived relaxing factor from cultured endothelial cells. British Journal Of Pharmacology 1990, 101: 237-239. PMID: 2257431, PMCID: PMC1917688, DOI: 10.1111/j.1476-5381.1990.tb12693.x.Peer-Reviewed Original Research