2001
Effects of the Serine/Threonine Kinase SGK1 on the Epithelial Na+ Channel (ENaC) and CFTR: Implications for Cystic Fibrosis
Wagner C, Ott M, Klingel K, Beck S, Melzig J, Friedrich B, Wild K, Bröer S, Moschen I, Albers A, Waldegger S, Tümmler B, Egan M, Geibel J, Kandolf R, Lang F. Effects of the Serine/Threonine Kinase SGK1 on the Epithelial Na+ Channel (ENaC) and CFTR: Implications for Cystic Fibrosis. Cellular Physiology And Biochemistry 2001, 11: 209-218. PMID: 11509829, DOI: 10.1159/000051935.Peer-Reviewed Original ResearchMeSH Keywords1-Methyl-3-isobutylxanthineAmino Acid SubstitutionAnimalsBronchiCell LineCystic FibrosisCystic Fibrosis Transmembrane Conductance RegulatorEpithelial CellsEpithelial Sodium ChannelsHumansIn Situ HybridizationLungMacrophages, AlveolarMutationOocytesPatch-Clamp TechniquesProtein Serine-Threonine KinasesPulmonary AlveoliRNA, ComplementaryRNA, MessengerSodiumSodium ChannelsXenopus laevisConceptsSerine/threonine kinase SGK1Lung tissueCystic fibrosisCF patientsKinase SGK1CF lung tissueXenopus oocytesLoss of CFTRLung epithelial cell lineCoexpression of CFTREffect of SGK1Pathophysiological factorsEpithelial cell lineRespiratory epitheliumLung phenotypeVariety of stimuliCl(-) secretionSGK1 expressionInhibitor amilorideInhibitory effectEpithelial cellsEnhanced expressionChannel ENaC.CFTR mutationsChannel activity
1999
A Novel Sulfonylurea Receptor Family Member Expressed in the Embryonic Drosophila Dorsal Vessel and Tracheal System*
Nasonkin I, Alikasifoglu A, Ambrose C, Cahill P, Cheng M, Sarniak A, Egan M, Thomas P. A Novel Sulfonylurea Receptor Family Member Expressed in the Embryonic Drosophila Dorsal Vessel and Tracheal System*. Journal Of Biological Chemistry 1999, 274: 29420-29425. PMID: 10506204, DOI: 10.1074/jbc.274.41.29420.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsATP-Binding Cassette TransportersCloning, MolecularDrosophilaDrosophila ProteinsGene Expression Regulation, DevelopmentalGlyburideHumansIn Situ HybridizationMolecular Sequence DataOocytesPatch-Clamp TechniquesPhylogenyPotassium ChannelsPotassium Channels, Inwardly RectifyingReceptors, DrugRNA, MessengerSulfonylurea ReceptorsXenopus laevisConceptsDrosophila embryogenesisPotassium channel activityTracheal systemNovel Drosophila geneDrosophila dorsal vesselDorsal vesselABC transporter familyChannel activityReceptor family membersDrosophila genesGene duplicationPotassium channelsDrosophila systemTransporter familyGenetic approachesATP-sensitive potassium channel activityGenesFunctional studiesSulfonylurea receptorKir6.2 subunitEmbryogenesisATP-sensitive potassium channelsSURxSubunitsDistinctive sequence
1998
Chloride channel and chloride conductance regulator domains of CFTR, the cystic fibrosis transmembrane conductance regulator
Schwiebert E, Morales M, Devidas S, Egan M, Guggino W. Chloride channel and chloride conductance regulator domains of CFTR, the cystic fibrosis transmembrane conductance regulator. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 2674-2679. PMID: 9482946, PMCID: PMC19458, DOI: 10.1073/pnas.95.5.2674.Peer-Reviewed Original ResearchMeSH Keywords4,4'-Diisothiocyanostilbene-2,2'-Disulfonic AcidAnimalsBase SequenceBronchiCells, CulturedChloride ChannelsChloridesCyclic AMPCystic FibrosisCystic Fibrosis Transmembrane Conductance RegulatorDNA, ComplementaryEpithelial CellsFemaleHumansMembrane PotentialsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedOligodeoxyribonucleotidesOocytesPatch-Clamp TechniquesPoint MutationProtein ConformationRecombinant ProteinsSequence DeletionTranscription, GeneticTransfectionXenopus laevisConceptsCl- channel functionConductance regulatorDomains of CFTRCystic fibrosis transmembrane conductance regulatorChloride channelsFibrosis transmembrane conductance regulatorFirst transmembrane domainC-terminal truncationsIndividual amino acid substitutionsTransmembrane conductance regulatorCl- channel poreCl- channelsAmino acid substitutionsRegulator domainTransmembrane domainTwo-electrode voltage-clamp recordingsRegulatory domainMutant CFTRAcid substitutionsRegulator functionHuman airway epithelial cellsCFTRXenopus oocytesRegulatorRelease of ATP[49] Assays of dynamics, mechanisms, and regulation of ATP transport and release: Implications for study of ABC transporter function
Schwiebert E, Egan M, Guggino W. [49] Assays of dynamics, mechanisms, and regulation of ATP transport and release: Implications for study of ABC transporter function. Methods In Enzymology 1998, 292: 664-675. PMID: 9711590, DOI: 10.1016/s0076-6879(98)92051-1.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAdenosine TriphosphateAnimalsATP-Binding Cassette TransportersCells, CulturedColforsinCystic Fibrosis Transmembrane Conductance RegulatorElectrophysiologyEpithelial CellsHumansIonomycinLuminescent MeasurementsMembrane PotentialsMiceModels, BiologicalOocytesOsmolar ConcentrationPatch-Clamp TechniquesSignal TransductionTritiumConceptsCystic fibrosis transmembrane conductance regulatorABC transportersATP-binding cassette (ABC) transportersSulfonylurea receptorFibrosis transmembrane conductance regulatorTransport of ATPABC transporter functionTransmembrane conductance regulatorImportance of ATPRegulatory machineryPancreatic β-cellsATP transportCassette transportersConductance regulatorTransporter functionTransporter moleculesBiological significanceATP sensorATPAgonist functionTransportersRelease of ATPΒ-cellsPowerful approachRegulator
1997
A functional CFTR-NBF1 is required for ROMK2-CFTR interaction
McNicholas C, Nason M, Guggino W, Schwiebert E, Hebert S, Giebisch G, Egan M. A functional CFTR-NBF1 is required for ROMK2-CFTR interaction. American Journal Of Physiology 1997, 273: f843-f848. PMID: 9374850, DOI: 10.1152/ajprenal.1997.273.5.f843.Peer-Reviewed Original ResearchAmino Acid SubstitutionAnimalsBase SequenceBinding SitesCystic Fibrosis Transmembrane Conductance RegulatorFemaleGlyburideMembrane PotentialsModels, MolecularMutagenesis, Site-DirectedOligodeoxyribonucleotidesOocytesPatch-Clamp TechniquesPotassium ChannelsPotassium Channels, Inwardly RectifyingProtein Structure, SecondaryRecombinant ProteinsXenopus laevis
1996
Sensitivity of a renal K+ channel (ROMK2) to the inhibitory sulfonylurea compound glibenclamide is enhanced by coexpression with the ATP-binding cassette transporter cystic fibrosis transmembrane regulator.
McNicholas C, Guggino W, Schwiebert E, Hebert S, Giebisch G, Egan M. Sensitivity of a renal K+ channel (ROMK2) to the inhibitory sulfonylurea compound glibenclamide is enhanced by coexpression with the ATP-binding cassette transporter cystic fibrosis transmembrane regulator. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 8083-8088. PMID: 8755607, PMCID: PMC38879, DOI: 10.1073/pnas.93.15.8083.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsChloride ChannelsCyclic AMP-Dependent Protein KinasesCystic Fibrosis Transmembrane Conductance RegulatorFemaleGlyburideKidneyMembrane PotentialsOocytesPatch-Clamp TechniquesPhosphorylationPotassium ChannelsPotassium Channels, Inwardly RectifyingSodium ChannelsXenopus laevis