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 sensitivityMutantsSaccharomyces
1999
The Second Hydrophobic Domain Contributes to the Kinetic Properties of Epithelial Sodium Channels*
Fyfe G, Zhang P, Canessa C. The Second Hydrophobic Domain Contributes to the Kinetic Properties of Epithelial Sodium Channels*. Journal Of Biological Chemistry 1999, 274: 36415-36421. PMID: 10593937, DOI: 10.1074/jbc.274.51.36415.Peer-Reviewed Original ResearchConceptsSecond hydrophobic domainEpithelial sodium channelBeta subunitHydrophobic domainWild-type subunitsSecond transmembrane domainENaC/Deg familyTransmembrane domainChimeric subunitsSodium channelsFunctional poresSubunit alphaAlpha subunitKinetic propertiesFunctional channelsSubunitsSingle-channel conductanceIon channelsSpecific sequencesXenopus oocytesSmall conductanceOpen probabilityChannel conductanceFunctional propertiesAmiloride affinitySodium transport systems in human chondrocytes. II. Expression of ENaC, Na+/K+/2Cl- cotransporter and Na+/H+ exchangers in healthy and arthritic chondrocytes.
Trujillo E, Alvarez de la Rosa D, Mobasheri A, González T, Canessa C, Martín-Vasallo P. Sodium transport systems in human chondrocytes. II. Expression of ENaC, Na+/K+/2Cl- cotransporter and Na+/H+ exchangers in healthy and arthritic chondrocytes. Cellular And Molecular Biology 1999, 14: 1023-31. PMID: 10506918, DOI: 10.14670/hh-14.1023.Peer-Reviewed Original ResearchConceptsRheumatoid arthritisHuman chondrocytesArthritic chondrocytesArthritic cartilageENaC protein levelsSodium-dependent transport systemExpression of ENaCSodium transport systemsEpithelial sodium channelHealthy individualsIntracellular pH regulationOA cartilageQuantities of alphaSodium channelsProtein levelsNHE isoformsBeta subunitSodium concentrationOsteoarthritisRelative expressionHuman cartilageAlphaCartilageEntry mechanismChondrocytes
1995
A 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
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