2008
A proton‐independent function of ASIC in Ciona intestinalis
Coric T, Passamaneck Y, Zhang P, Di Gregorio A, Canessa C. A proton‐independent function of ASIC in Ciona intestinalis. The FASEB Journal 2008, 22: 945.4-945.4. DOI: 10.1096/fasebj.22.1_supplement.945.4.Peer-Reviewed Original ResearchCiona intestinalisAcid-sensitive ion channelsChordate nervous systemAscidian Ciona intestinalisLarval nervous systemPhysiological genomicsAdult nervous systemSequence similarityHigher vertebratesHeterologous systemsLarval neuronsSpliced formsASIC functionNervous systemLarval swimmingIon channelsASIC genesExtracellular protonsSodium channelsProton sensitivityIntestinalisMost neuronsSynaptic transmissionCionaVertebrates
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
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 affinityThe 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 cellsSubunitsSodium 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 mechanismChondrocytessgk 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
In 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.Structure and function of the Mec-ENaC family of ion channels.
Fyfe G, Quinn A, Canessa C. Structure and function of the Mec-ENaC family of ion channels. Seminars In Nephrology 1998, 18: 138-51. PMID: 9541269.Peer-Reviewed Original ResearchConceptsIon channelsLittle amino acid identityCell type-dependent expressionAmino acid identityAcid identityDistinct tissuesEpithelial sodium channelFunction mutationsRecent discoveryProteinDifferential sensitivitySodium channelsSpecialized neuronsNew familyNociceptive painBlood pressureFamilyTissue injurySodium homeostasisSame common structureCommon ailmentsMechanical stimuliCloningTransductionDiuretic amiloride
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
Expression 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 regulationMutationsA 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-rENaCSCNN1, an Epithelial Cell Sodium Channel Gene in the Conserved Linkage Group on Mouse Chromosome 6 and Human Chromosome 12
Meisler M, Barrow L, Canessa C, Rossier B. SCNN1, an Epithelial Cell Sodium Channel Gene in the Conserved Linkage Group on Mouse Chromosome 6 and Human Chromosome 12. Genomics 1994, 24: 185-186. PMID: 7896277, DOI: 10.1006/geno.1994.1599.Peer-Reviewed Original ResearchEpithelial sodium channels
Rossier B, Canessa C, Schild L, Horisberger J. Epithelial sodium channels. Current Opinion In Nephrology & Hypertension 1994, 3: 487-496. PMID: 7804746, DOI: 10.1097/00041552-199409000-00003.Peer-Reviewed Original ResearchConceptsEpithelial sodium channelAmiloride-sensitive epithelial sodium channelSodium channelsNovel genesHeteromultimeric proteinsHomologous subunitsDistinct functionsRat epithelial sodium channelPrimary structureCation channelsBiophysical propertiesCritical roleTaste transductionTransductionGenesMechanotransductionSubunitsProteinCell distributionRegulationAmiloride-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