2005
Akt1/protein kinase Bα is critical for ischemic and VEGF-mediated angiogenesis
Ackah E, Yu J, Zoellner S, Iwakiri Y, Skurk C, Shibata R, Ouchi N, Easton RM, Galasso G, Birnbaum MJ, Walsh K, Sessa WC. Akt1/protein kinase Bα is critical for ischemic and VEGF-mediated angiogenesis. Journal Of Clinical Investigation 2005, 115: 2119-2127. PMID: 16075056, PMCID: PMC1180542, DOI: 10.1172/jci24726.Peer-Reviewed Original ResearchConceptsSerine-threonine protein kinaseAkt1/protein kinase BαProtein kinase BαProtein kinase BAkt1-/- miceIndividual Akt isoformsLoss of Akt1Substrate phosphorylationCellular functionsAkt substrateProtein kinaseAkt isoformsAkt1 knockout miceGene expressionGenetic lossKinase BBasal phosphorylationCell metabolismPostnatal angiogenesisCellular migrationVivo roleCell migrationAKT1Essential rolePhosphorylation
2004
Targeting of Endothelial Nitric-oxide Synthase to the Cytoplasmic Face of the Golgi Complex or Plasma Membrane Regulates Akt- Versus Calcium-dependent Mechanisms for Nitric Oxide Release*
Fulton D, Babbitt R, Zoellner S, Fontana J, Acevedo L, McCabe TJ, Iwakiri Y, Sessa WC. Targeting of Endothelial Nitric-oxide Synthase to the Cytoplasmic Face of the Golgi Complex or Plasma Membrane Regulates Akt- Versus Calcium-dependent Mechanisms for Nitric Oxide Release*. Journal Of Biological Chemistry 2004, 279: 30349-30357. PMID: 15136572, DOI: 10.1074/jbc.m402155200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, WesternCalciumCalmodulinCell MembraneCOS CellsCysteineCytoplasmEndothelium, VascularGolgi ApparatusHumansMicroscopy, FluorescenceMyristic AcidsNitric OxideNitric Oxide SynthaseNitric Oxide Synthase Type IIIPalmitic AcidsPhosphorylationProtein Serine-Threonine KinasesProtein Structure, TertiaryProto-Oncogene ProteinsProto-Oncogene Proteins c-aktSerineTransfectionUmbilical VeinsConceptsPlasma membraneGolgi complexAkt-dependent phosphorylationEndothelial nitricoxide synthasePool of enzymesCalcium-dependent activationCytoplasmic faceGolgi membranesENOS constructMembrane versionFusion proteinCytoplasmic aspectFunctional rolePhosphorylationENOS activationHeterogeneous localizationMembraneCalcium fluxCalcium-dependent mechanismSynthaseActivationEndothelial nitric oxide synthaseFurther activationComplexesNitricoxide synthase
2002
Phosphorylation of eNOS initiates excessive NO production in early phases of portal hypertension
Iwakiri Y, Tsai MH, McCabe TJ, Gratton JP, Fulton D, Groszmann RJ, Sessa WC. Phosphorylation of eNOS initiates excessive NO production in early phases of portal hypertension. AJP Heart And Circulatory Physiology 2002, 282: h2084-h2090. PMID: 12003815, DOI: 10.1152/ajpheart.00675.2001.Peer-Reviewed Original ResearchMeSH KeywordsAdrenergic alpha-1 Receptor AgonistsAndrostadienesAnimalsEnzyme InhibitorsHypertension, PortalLigationMaleMesenteric Artery, SuperiorMethoxamineNitric OxideNitric Oxide SynthaseNitric Oxide Synthase Type IIIOmega-N-MethylargininePhosphorylationPortal VeinProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktRatsRats, Sprague-DawleyVasoconstrictor AgentsWortmanninConceptsEndothelial nitric oxide synthasePortal vein ligationPhosphorylation of eNOSMesenteric arterial bedPortal hypertensionPVL groupArterial bedNO productionMale Sprague-Dawley ratsEarly portal hypertensionMonomethyl-L-arginineNitric oxide synthaseSprague-Dawley ratsExcessive NO productionG protein-coupled receptorsVivo perfusion studiesPVL ratsProtein-coupled receptorsPerfusion pressureSham groupVein ligationENOS expressionOxide synthaseReduced responsivenessKinase/Akt pathway