2000
Heterologous expression of a mammalian epithelial sodium channel in yeast
Gupta S, Canessa C. Heterologous expression of a mammalian epithelial sodium channel in yeast. FEBS Letters 2000, 481: 77-80. PMID: 10984619, DOI: 10.1016/s0014-5793(00)01977-3.Peer-Reviewed Original ResearchMeSH KeywordsAmilorideAnimalsBlotting, WesternCarrier ProteinsCell DivisionCell MembraneCytoplasmic GranulesEpithelial Sodium ChannelsGene Expression Regulation, FungalHot TemperatureMembrane ProteinsMicrobial Sensitivity TestsMutationOsmolar ConcentrationRatsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSodium Channel BlockersSodium ChannelsSodium ChlorideVesicular Transport ProteinsConceptsEpithelial sodium channelYeast SaccharomycesHeterologous expressionSecretory pathwayBeta-ENaCPlasma membraneSodium channelsRat epithelial sodium channelBeta subunitSecretory systemYeast strainYeastParent strainWestern blotting techniquesENaCBlotting techniquesSalt sensitivityMutantsSaccharomycesStructure and Regulation of Amiloride-Sensitive Sodium Channels
de la Rosa D, Canessa C, Fyfe G, Zhang P. Structure and Regulation of Amiloride-Sensitive Sodium Channels. Annual Review Of Physiology 2000, 62: 573-594. PMID: 10845103, DOI: 10.1146/annurev.physiol.62.1.573.Peer-Reviewed Original Research
1999
sgk 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
1998
Subunit Composition Determines the Single Channel Kinetics of the Epithelial Sodium Channel
Fyfe G, Canessa C. Subunit Composition Determines the Single Channel Kinetics of the Epithelial Sodium Channel. The Journal Of General Physiology 1998, 112: 423-432. PMID: 9758861, PMCID: PMC2229421, DOI: 10.1085/jgp.112.4.423.Peer-Reviewed Original ResearchIn vivo phosphorylation of the epithelial sodium channel
Shimkets R, Lifton R, Canessa C. In vivo phosphorylation of the epithelial sodium channel. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 3301-3305. PMID: 9501257, PMCID: PMC19736, DOI: 10.1073/pnas.95.6.3301.Peer-Reviewed Original ResearchMeSH KeywordsAldosteroneAmilorideAmino Acid SequenceAnimalsColforsinCyclic AMP-Dependent Protein KinasesDogsEpithelial CellsEpithelial Sodium ChannelsInsulinMolecular Sequence DataNephronsPeptide MappingPhosphopeptidesPhosphorylationProtein Kinase CRatsSodium Channel AgonistsSodium ChannelsTransfectionConceptsCarboxyl terminusEpithelial sodium channelAlpha subunitGamma subunitsDe novo phosphorylationSubunit of ENaC.Stable cotransfectionVivo phosphorylationProtein kinaseEpithelial cell lineSodium channelsMolecular mechanismsActivity of ENaCPhosphorylationSubunitsCell linesTerminusProteinBetaKinaseCotransfectionBasal stateSerineThreonineENaC.
1997
The Activity of the Epithelial Sodium Channel Is Regulated by Clathrin-mediated Endocytosis*
Shimkets R, Lifton R, Canessa C. The Activity of the Epithelial Sodium Channel Is Regulated by Clathrin-mediated Endocytosis*. Journal Of Biological Chemistry 1997, 272: 25537-25541. PMID: 9325269, DOI: 10.1074/jbc.272.41.25537.Peer-Reviewed Original ResearchConceptsWild-type channelsDynamin mutantPlasma membraneEpithelial sodium channelClathrin-coated pit-mediated endocytosisLiddle mutationClathrin-coated pit pathwayDominant-negative dynamin mutantPit-mediated endocytosisChannel activityLoss of endocytosisActivity of channelsLiddle's syndromePy domainsCarboxyl terminusSodium channelsWild-type ENaCBrefeldin APit pathwayEndocytosisCell surfaceSpecific inhibitorXenopus oocytesNormal turnoverMutationsDiversity of Channels Generated by Different Combinations of Epithelial Sodium Channel Subunits
McNicholas C, Canessa C. Diversity of Channels Generated by Different Combinations of Epithelial Sodium Channel Subunits. The Journal Of General Physiology 1997, 109: 681-692. PMID: 9222895, PMCID: PMC2217047, DOI: 10.1085/jgp.109.6.681.Peer-Reviewed Original ResearchMeSH KeywordsAmilorideAnimalsEpitheliumIon TransportOocytesPatch-Clamp TechniquesSodium ChannelsXenopus
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 ResearchA mutation in the epithelial sodium channel causing Liddle disease increases channel activity in the Xenopus laevis oocyte expression system.
Schild L, Canessa C, Shimkets R, Gautschi I, Lifton R, Rossier B. A mutation in the epithelial sodium channel causing Liddle disease increases channel activity in the Xenopus laevis oocyte expression system. Proceedings Of The National Academy Of Sciences Of The United States Of America 1995, 92: 5699-5703. PMID: 7777572, PMCID: PMC41764, DOI: 10.1073/pnas.92.12.5699.Peer-Reviewed Original ResearchConceptsLiddle's diseaseSalt-sensitive hypertensionSalt-sensitive formsChannel activityXenopus laevis oocyte expression systemDirect physiological evidenceChannel beta subunitsEpithelial sodium channelChannel hyperactivityOocyte expression systemPharmacological propertiesSodium channelsGamma subunitsMolecular targetsBeta subunitDiseaseXenopus laevis oocytesHypertensionPremature stop codonPhysiological evidenceHeritable formTruncation mutationsOverall channel activityFunctional consequencesLaevis oocytes
1994
Membrane topology of the epithelial sodium channel in intact cells
Canessa C, Merillat A, Rossier B. Membrane topology of the epithelial sodium channel in intact cells. American Journal Of Physiology 1994, 267: c1682-c1690. PMID: 7810611, DOI: 10.1152/ajpcell.1994.267.6.c1682.Peer-Reviewed Original ResearchConceptsLarge hydrophilic loopHydrophilic loopIntact cellsMembrane topologyEpithelial sodium channelPutative transmembrane domainsStop-transfer signalAmiloride-sensitive epithelial sodium channelCell-free translation assaysShort NH2Transmembrane domainMembrane insertionHomologous subunitsXenopus laevis oocytesTranslation assaysSodium channelsGlycosylation sitesCOOH terminusCytoplasmic sideFunctional expressionTerminal endSubunitsHydrophilic NH2Laevis oocytesAlpha-rENaCThe amiloride receptor
Horisberger J, Puoti A, Canessa C, Rossier B. The amiloride receptor. Journal Of Molecular Medicine 1994, 72: 695-697. PMID: 7531520, DOI: 10.1007/bf00212992.Peer-Reviewed Original ResearchAmiloride-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