2006
THE REGULATION AND PHARMACOLOGY OF ENDOTHELIAL NITRIC OXIDE SYNTHASE
Dudzinski DM, Igarashi J, Greif D, Michel T. THE REGULATION AND PHARMACOLOGY OF ENDOTHELIAL NITRIC OXIDE SYNTHASE. The Annual Review Of Pharmacology And Toxicology 2006, 46: 235-276. PMID: 16402905, DOI: 10.1146/annurev.pharmtox.44.101802.121844.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsEnzyme InhibitorsGene Expression Regulation, DevelopmentalHumansIsoenzymesNitric OxideNitric Oxide Synthase Type III
2004
KLF2 Is a Novel Transcriptional Regulator of Endothelial Proinflammatory Activation
SenBanerjee S, Lin Z, Atkins GB, Greif DM, Rao RM, Kumar A, Feinberg MW, Chen Z, Simon DI, Luscinskas FW, Michel TM, Gimbrone MA, García-Cardeña G, Jain MK. KLF2 Is a Novel Transcriptional Regulator of Endothelial Proinflammatory Activation. Journal Of Experimental Medicine 2004, 199: 1305-1315. PMID: 15136591, PMCID: PMC2211816, DOI: 10.1084/jem.20031132.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceCells, CulturedDNA PrimersEndothelium, VascularE-SelectinGene Expression RegulationGlutathione TransferaseHumansInflammationIntercellular Adhesion Molecule-1Interleukin-1Kruppel-Like Transcription FactorsNF-kappa BNitric Oxide SynthaseNitric Oxide Synthase Type IIIOligonucleotide Array Sequence AnalysisPolymerase Chain ReactionPromoter Regions, GeneticStress, MechanicalTrans-ActivatorsTranscription, GeneticUmbilical VeinsZinc FingersConceptsUmbilical vein endothelial cellsVein endothelial cellsProinflammatory cytokinesEndothelial nitric oxide synthase expressionVascular cell adhesion molecule-1Nitric oxide synthase expressionInflammatory cytokines interleukin-1betaEndothelial cellsCell adhesion molecule-1Endothelial proinflammatory activationOxide synthase expressionCultured human umbilical vein endothelial cellsCytokine interleukin-1betaVascular disease statesEndothelial adhesion molecules EAdhesion molecule-1Adhesion molecules EOverexpression of KLF2Human umbilical vein endothelial cellsAMP response element binding proteinCyclic AMP response element binding proteinResponse element-binding proteinT cell attachmentEndothelial functionEndothelial activationCalmodulin phosphorylation and modulation of endothelial nitric oxide synthase catalysis
Greif DM, Sacks DB, Michel T. Calmodulin phosphorylation and modulation of endothelial nitric oxide synthase catalysis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2004, 101: 1165-1170. PMID: 14736917, PMCID: PMC337024, DOI: 10.1073/pnas.0306377101.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalmodulinCasein Kinase IICatalysisCattleCells, CulturedEnzyme ActivationNitric Oxide SynthaseNitric Oxide Synthase Type IIIPhosphorylationProtein Serine-Threonine KinasesConceptsPhosphorylation of CaMBovine aortic endothelial cellsCaM phosphorylationCaM mutantsCalcium regulatory protein calmodulinBiosynthetic labelingRegulation of eNOSProtein kinase pathwayEndothelial NO synthaseSer-81Regulatory protein calmodulinKinase CK2Kinase pathwayEndothelial cellsCK2Protein calmodulinMutantsCalmodulin phosphorylationPhosphorylationAortic endothelial cellsPhenyl-SepharoseUnique pathwayENOS activationMutant CaMPathway
2002
Site-Specific Dephosphorylation of Endothelial Nitric Oxide Synthase by Protein Phosphatase 2A: Evidence for Crosstalk between Phosphorylation Sites †
Greif DM, Kou R, Michel T. Site-Specific Dephosphorylation of Endothelial Nitric Oxide Synthase by Protein Phosphatase 2A: Evidence for Crosstalk between Phosphorylation Sites †. Biochemistry 2002, 41: 15845-15853. PMID: 12501214, DOI: 10.1021/bi026732g.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCattleCell LineCOS CellsEnzyme ActivationEnzyme InhibitorsMarine ToxinsMutagenesis, Site-DirectedNitric Oxide SynthaseNitric Oxide Synthase Type IIIOkadaic AcidOxazolesPhosphatesPhosphoprotein PhosphatasesPhosphorus RadioisotopesPhosphorylationProtein Phosphatase 2SerineSignal TransductionThreonineTransfectionConceptsProtein phosphatase 2ASerine 116Bovine aortic endothelial cellsCOS-7 cellsENOS dephosphorylationENOS mutantPhosphatase 2ASerine 1179Phosphorylation sitesThreonine 497Calcium/calmodulin-dependent enzymesInhibitor of PP2ASite-specific dephosphorylationProtein kinase pathwayWild-type eNOSEnzyme activityNitric oxide-dependent signaling pathwaysCalmodulin-dependent enzymesProtein phosphatasePosttranslational modificationsEpitope tagENOS phosphorylationKinase pathwayEndothelial cellsRecombinant proteinsDephosphorylation of Endothelial Nitric-oxide Synthase by Vascular Endothelial Growth Factor IMPLICATIONS FOR THE VASCULAR RESPONSES TO CYCLOSPORIN A*
Kou R, Greif D, Michel T. Dephosphorylation of Endothelial Nitric-oxide Synthase by Vascular Endothelial Growth Factor IMPLICATIONS FOR THE VASCULAR RESPONSES TO CYCLOSPORIN A*. Journal Of Biological Chemistry 2002, 277: 29669-29673. PMID: 12050171, DOI: 10.1074/jbc.m204519200.Peer-Reviewed Original ResearchConceptsENOS dephosphorylationSerine 116MAP kinase pathway inhibitor U0126Protein phosphatase pathwaysPhosphorylation-deficient mutantDependent protein phosphatasePhosphorylation state-specific antibodiesWild-type enzymeVascular endothelial growth factorProtein kinase C inhibitor calphostinPathway inhibitor U0126Activation of calcineurinProtein phosphataseInhibitor of calcineurinPhosphatase pathwaysENOS agonistsProtein kinaseEndothelial cellsAlanine residuesDephosphorylationDependent enzymesInhibitor U0126Dephosphorylation of eNOSCultured endothelial cellsEnzyme activity