2006
Gating of Acid-sensitive Ion Channel-1: Release of Ca2+ Block vs. Allosteric Mechanism
Zhang P, Sigworth FJ, Canessa CM. Gating of Acid-sensitive Ion Channel-1: Release of Ca2+ Block vs. Allosteric Mechanism. The Journal Of General Physiology 2006, 127: 109-117. PMID: 16418400, PMCID: PMC2151491, DOI: 10.1085/jgp.200509396.Peer-Reviewed Original ResearchAcid Sensing Ion ChannelsAllosteric RegulationAnimalsBatrachoidiformesBinding SitesCalciumElectric ConductivityFemaleGene ExpressionIon Channel GatingMembrane ProteinsModels, BiologicalNerve Tissue ProteinsOocytesPatch-Clamp TechniquesProtein ConformationProtonsSodium ChannelsTime FactorsXenopus laevis
2001
Single-Channel Properties of Recombinant Acid-Sensitive Ion Channels Formed by the Subunits Asic2 and Asic3 from Dorsal Root Ganglion Neurons Expressed in Xenopus Oocytes
Zhang P, Canessa C. Single-Channel Properties of Recombinant Acid-Sensitive Ion Channels Formed by the Subunits Asic2 and Asic3 from Dorsal Root Ganglion Neurons Expressed in Xenopus Oocytes. The Journal Of General Physiology 2001, 117: 563-572. PMID: 11382806, PMCID: PMC2232399, DOI: 10.1085/jgp.117.6.563.Peer-Reviewed Original Research
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 cellsSubunits
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 Research
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 Research
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 ResearchExpression cloning of the epithelial sodium channel
Canessa C, Horisberger J, Schild L, Rossier B. Expression cloning of the epithelial sodium channel. Kidney International 1995, 48: 950-955. PMID: 8569104, DOI: 10.1038/ki.1995.376.Peer-Reviewed Original ResearchHypertension 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 oocytesSubunitsThe 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 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
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