1999
The Serum and Glucocorticoid Kinase sgk Increases the Abundance of Epithelial Sodium Channels in the Plasma Membrane of Xenopus Oocytes*
de la Rosa D, Zhang P, Náray-Fejes-Tóth A, Fejes-Tóth G, Canessa C. The Serum and Glucocorticoid Kinase sgk Increases the Abundance of Epithelial Sodium Channels in the Plasma Membrane of Xenopus Oocytes*. Journal Of Biological Chemistry 1999, 274: 37834-37839. PMID: 10608847, DOI: 10.1074/jbc.274.53.37834.Peer-Reviewed Original ResearchConceptsCarboxyl terminusPlasma membraneEpithelial sodium channelSerine/threonineXenopus oocytesNumber of ENaCsGlucocorticoid-induced kinaseRenal epithelial cellsThreonine kinaseSodium channelsMembrane abundanceTyrosine residuesGamma subunitsSGKAbundance of ENaCCell surfacePhosphorylationTerminusAmiloride-sensitive sodium transportAbundanceSodium transportKinaseENaC.Epithelial cellsSubunitssgk Is an Aldosterone-induced Kinase in the Renal Collecting Duct EFFECTS ON EPITHELIAL Na+ CHANNELS*
Náray-Fejes-Tóth A, Canessa C, Cleaveland E, Aldrich G, Fejes-Tóth G. sgk Is an Aldosterone-induced Kinase in the Renal Collecting Duct EFFECTS ON EPITHELIAL Na+ CHANNELS*. Journal Of Biological Chemistry 1999, 274: 16973-16978. PMID: 10358046, DOI: 10.1074/jbc.274.24.16973.Peer-Reviewed Original ResearchMeSH KeywordsAldosteroneAmilorideAmino Acid SequenceAndrostanolsAnimalsElectric ConductivityEnzyme InductionImmediate-Early ProteinsKidney Tubules, CollectingMolecular Sequence DataNuclear ProteinsProtein Serine-Threonine KinasesRabbitsReceptors, MineralocorticoidRecombinant ProteinsRNA, MessengerSequence Homology, Amino AcidConceptsAddition of aldosteroneTarget cellsAldosterone-induced geneAldosterone-induced kinaseApical sodium channelsEarly phaseMineralocorticoid target cellsSodium reabsorptionMineralocorticoid receptorNative target cellsImmediate early genesAldosteroneStimulatory effectDuct cellsSodium channelsMRNA levelsDe novo protein synthesisRenal epitheliumPolymerase chain reaction-based subtractive hybridizationNovo protein synthesisEarly genesCellsDifferential display techniqueProtein synthesisKinase
1995
Amiloride-sensitive sodium channels in confluent M-1 mouse cortical collecting duct cells
Letz B, Ackermann A, Canessa C, Rossier B, Korbmacher C. Amiloride-sensitive sodium channels in confluent M-1 mouse cortical collecting duct cells. The Journal Of Membrane Biology 1995, 148: 127-141. PMID: 8606362, DOI: 10.1007/bf00207269.Peer-Reviewed Original ResearchLabeling of a cysteine in the cardiotonic glycoside binding site by the steroid derivative HDMA
Antolovic R, Schoner W, Geering K, Canessa C, Rossier B, Horisberger J. Labeling of a cysteine in the cardiotonic glycoside binding site by the steroid derivative HDMA. FEBS Letters 1995, 368: 169-172. PMID: 7615075, DOI: 10.1016/0014-5793(95)00637-o.Peer-Reviewed Original Research
1994
Amiloride-sensitive epithelial Na+ channel is made of three homologous subunits
Canessa C, Schild L, Buell G, Thorens B, Gautschi I, Horisberger J, Rossier B. Amiloride-sensitive epithelial Na+ channel is made of three homologous subunits. Nature 1994, 367: 463-467. PMID: 8107805, DOI: 10.1038/367463a0.Peer-Reviewed Original ResearchConceptsEpithelial sodium channelRat epithelial sodium channelSodium channelsSodium reabsorptionSodium balanceDistal colonAmiloride-sensitive epithelial sodium channelPharmacological profileBlood volumeRenal tubulesRat epithelialExocrine glandsEpithelial cellsΑ-subunitDistal partNative channelsExpression cloningAldosteroneLungColon
1993
Mutation of a tyrosine in the H3-H4 ectodomain of Na,K-ATPase alpha subunit confers ouabain resistance.
Canessa C, Horisberger J, Rossier B. Mutation of a tyrosine in the H3-H4 ectodomain of Na,K-ATPase alpha subunit confers ouabain resistance. Journal Of Biological Chemistry 1993, 268: 17722-17726. PMID: 8394348, DOI: 10.1016/s0021-9258(17)46764-0.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsBase SequenceBinding SitesCell LineCloning, MolecularDogsFemaleKidneyKineticsMacromolecular SubstancesMolecular Sequence DataMutagenesis, Site-DirectedOligodeoxyribonucleotidesOocytesOuabainPeptide FragmentsPolymerase Chain ReactionProtein ConformationRecombinant ProteinsSequence Homology, Amino AcidSodium-Potassium-Exchanging ATPaseTime FactorsXenopus laevis
1992
Primary sequence and functional expression of a novel ouabain-resistant Na,K-ATPase. The beta subunit modulates potassium activation of the Na,K-pump.
Jaisser F, Canessa C, Horisberger J, Rossier B. Primary sequence and functional expression of a novel ouabain-resistant Na,K-ATPase. The beta subunit modulates potassium activation of the Na,K-pump. Journal Of Biological Chemistry 1992, 267: 16895-16903. PMID: 1380956, DOI: 10.1016/s0021-9258(18)41869-8.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBlotting, NorthernBufo marinusCell LineCloning, MolecularFemaleGene LibraryHumansIsoenzymesMacromolecular SubstancesMolecular Sequence DataOligodeoxyribonucleotidesOligonucleotides, AntisenseOocytesOuabainPotassiumRecombinant ProteinsRNASequence Homology, Nucleic AcidSodium-Potassium-Exchanging ATPaseTranscription, GeneticUrinary BladderXenopus laevisConceptsOuabain-resistant phenotypeAlpha 1 isoformBeta subunitAmino acidsK-ATPase alphaBeta 1Alpha 1Alpha 1 beta 1Oocyte expression systemXenopus laevis oocyte expression systemSequence comparisonBladder cell linesK pumpTerminal borderC-terminusExtracellular potassium ionsPrimary sequenceExpression systemMolecular mechanismsOuabain resistanceBeta 3 isoformsOuabain-resistant NaExtracellular loopFunctional expressionSubunits