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 activation
2002
Dephosphorylation 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