1995
Hypertension caused by a truncated epithelial sodium channel γ subunit: genetic heterogeneity of Liddle syndrome
Hansson J, Nelson-Williams C, Suzuki H, Schild L, Shimkets R, Lu Y, Canessa C, Iwasaki T, Rossier B, Lifton R. Hypertension caused by a truncated epithelial sodium channel γ subunit: genetic heterogeneity of Liddle syndrome. Nature Genetics 1995, 11: 76-82. PMID: 7550319, DOI: 10.1038/ng0995-76.Peer-Reviewed Original ResearchMeSH KeywordsAdolescentAdultAldosteroneAllelesAmino Acid SequenceAnimalsBase SequenceCodonEpithelial Sodium ChannelsGene Expression RegulationGenesGenes, DominantHumansHypertensionHypokalemiaIon Channel GatingKidney Tubules, ProximalMiddle AgedMolecular Sequence DataMutagenesis, Site-DirectedMutationOocytesPedigreeRatsRecombinant Fusion ProteinsReninSequence AlignmentSequence Homology, Amino AcidSodium ChannelsSodium, DietarySyndromeTerminator Regions, GeneticXenopus laevisConceptsLiddle's syndromeRenal epithelial sodium channelEpithelial Sodium Channel γ-SubunitSalt-sensitive formsChannel activityChannel γ subunitBlood pressureDietary saltEpithelial sodium channelHuman hypertensionSyndromeGenetic heterogeneityHypertensionSodium channelsIndependent roleConstitutive activationΓ subunitMendelian disordersNegative regulationMutationsCloning of a bovine renal epithelial Na+ channel subunit
Fuller C, Awayda M, Arrate M, Bradford A, Morris R, Canessa C, Rossier B, Benos D. Cloning of a bovine renal epithelial Na+ channel subunit. American Journal Of Physiology 1995, 269: c641-c654. PMID: 7573394, DOI: 10.1152/ajpcell.1995.269.3.c641.Peer-Reviewed Original ResearchConceptsChannel subunitsOpen reading frameProtein kinase A.Gamma-ENaC subunitsCDNA expression libraryProtein kinase CVitro translationCDNA clonesBovine cDNAXenopus laevis oocytesPancreatic microsomesAcid proteinReading frameNovel isoformBovine homologueExpression libraryConsensus sequenceKinase CBase pairsAlpha-hENaCXenopus oocytesChimeric channelsHuman counterpartLaevis oocytesSubunitsRelative expression of the human epithelial Na+ channel subunits in normal and cystic fibrosis airways
Burch L, Talbot C, Knowles M, Canessa C, Rossier B, Boucher R. Relative expression of the human epithelial Na+ channel subunits in normal and cystic fibrosis airways. American Journal Of Physiology 1995, 269: c511-c518. PMID: 7653534, DOI: 10.1152/ajpcell.1995.269.2.c511.Peer-Reviewed Original ResearchConceptsAirway epitheliumSuperficial epitheliumCF airwaysGamma-ENaC mRNACF airway diseaseENaC subunit mRNAsCystic fibrosis airway epitheliaCF airway epitheliaAirway diseaseSitu hybridization studiesDuctal epitheliumCF transmembrane conductance regulator (CFTR) proteinRibonuclease protection assaysAcinar epitheliumMolecular pathogenesisCystic fibrosisChannel mRNAInhibitory regulationSubunit mRNAsEpitheliumChannel subunitsRatio of alphaAirwayRelative expressionPathogenesisThe highly selective low-conductance epithelial Na channel of Xenopus laevis A6 kidney cells
Puoti A, May A, Canessa C, Horisberger J, Schild L, Rossier B. The highly selective low-conductance epithelial Na channel of Xenopus laevis A6 kidney cells. American Journal Of Physiology 1995, 269: c188-c197. PMID: 7631745, DOI: 10.1152/ajpcell.1995.269.1.c188.Peer-Reviewed Original Research
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 expressionSubunitsMutation of a cysteine in the first transmembrane segment of Na,K‐ATPase alpha subunit confers ouabain resistance.
Canessa C, Horisberger J, Louvard D, Rossier B. Mutation of a cysteine in the first transmembrane segment of Na,K‐ATPase alpha subunit confers ouabain resistance. The EMBO Journal 1992, 11: 1681-1687. PMID: 1316269, PMCID: PMC556624, DOI: 10.1002/j.1460-2075.1992.tb05218.x.Peer-Reviewed Original Research