2016
Romk1 Knockout Mice Do Not Produce Bartter Phenotype but Exhibit Impaired K Excretion*
Dong K, Yan Q, Lu M, Wan L, Hu H, Guo J, Boulpaep E, Wang W, Giebisch G, Hebert SC, Wang T. Romk1 Knockout Mice Do Not Produce Bartter Phenotype but Exhibit Impaired K Excretion*. Journal Of Biological Chemistry 2016, 291: 5259-5269. PMID: 26728465, PMCID: PMC4777858, DOI: 10.1074/jbc.m115.707877.Peer-Reviewed Original Research
2010
Mouse cystic fibrosis transmembrane conductance regulator forms cAMP-PKA–regulated apical chloride channels in cortical collecting duct
Lu M, Dong K, Egan ME, Giebisch GH, Boulpaep EL, Hebert SC. Mouse cystic fibrosis transmembrane conductance regulator forms cAMP-PKA–regulated apical chloride channels in cortical collecting duct. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 6082-6087. PMID: 20231442, PMCID: PMC2851921, DOI: 10.1073/pnas.0902661107.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBenzoatesChloride ChannelsCyclic AMPCyclic AMP-Dependent Protein KinasesCystic Fibrosis Transmembrane Conductance RegulatorFemaleIn Vitro TechniquesKidney CortexKidney Tubules, CollectingKineticsMiceMice, Inbred C57BLMice, Inbred CFTRMice, KnockoutMice, TransgenicMutationOocytesPatch-Clamp TechniquesPotassium Channels, Inwardly RectifyingRecombinant ProteinsThiazolidinesXenopus laevisConceptsCystic fibrosis transmembrane conductance regulatorFibrosis transmembrane conductance regulatorTransmembrane conductance regulatorCl- channel activityConductance regulatorCl- channelsApical membrane proteinsExpression of CFTRChannel activityCFTR Cl- channelApical chloride channelApical cell membraneDeltaF508 CFTR mutationMembrane proteinsCatalytic subunitXenopus laevis oocytesForm proteinPrincipal cellsCFTR channelsROMK null miceApical patchesApical membraneSingle-channel conductanceChloride channelsCell membrane
2000
Regulation of volume‐activated chloride channels by P‐glycoprotein: phosphorylation has the final say!
Idriss H, Hannun Y, Boulpaep E, Basavappa S. Regulation of volume‐activated chloride channels by P‐glycoprotein: phosphorylation has the final say! The Journal Of Physiology 2000, 524: 629-636. PMID: 10790147, PMCID: PMC2269906, DOI: 10.1111/j.1469-7793.2000.00629.x.Peer-Reviewed Original ResearchConceptsProtein kinase CReversible phosphorylationChloride channelsChloride channel activityPhosphorylation of PgpSuch phosphorylationMultiple phosphorylationVolume-activated chloride channelsTransmembrane transportersKinase CPhosphorylationInhibition of transportCell volume changesPossible regulationChannel activityP-glycoproteinPotential involvementSuch regulationRegulation functionRegulationUnrelated drugsPgpProteinTransportersOverexpression
1998
Properties of an Inwardly Rectifying ATP-sensitive K+ Channel in the Basolateral Membrane of Renal Proximal Tubule
Mauerer U, Boulpaep E, Segal A. Properties of an Inwardly Rectifying ATP-sensitive K+ Channel in the Basolateral Membrane of Renal Proximal Tubule. The Journal Of General Physiology 1998, 111: 139-160. PMID: 9417141, PMCID: PMC1887768, DOI: 10.1085/jgp.111.1.139.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmbystomaAnimalsBariumBiological TransportCationsCells, CulturedCytidine TriphosphateDiazoxideDiureticsElectric ConductivityGlyburideGuanosine TriphosphateHypoglycemic AgentsInosine TriphosphateIon Channel GatingKidney Tubules, ProximalKineticsMicrovilliPatch-Clamp TechniquesPotassium ChannelsSodium Chloride Symporter InhibitorsSodium-Potassium-Exchanging ATPaseThalliumThymine NucleotidesUridine TriphosphateConceptsProximal tubule cellsProximal tubulesTubule cellsBasolateral membraneChannel opener diazoxideChannel activityPump-leak couplingRenal proximal tubulesPivotal physiological rolesOpener diazoxideMillimolar dosesMM ATPHigh dosesPotassium conductanceCell membrane potentialInternal Mg2Cytosolic additionATPase pumpRegulation of an Inwardly Rectifying ATP-sensitive K+ Channel in the Basolateral Membrane of Renal Proximal Tubule
Mauerer U, Boulpaep E, Segal A. Regulation of an Inwardly Rectifying ATP-sensitive K+ Channel in the Basolateral Membrane of Renal Proximal Tubule. The Journal Of General Physiology 1998, 111: 161-180. PMID: 9417142, PMCID: PMC1887764, DOI: 10.1085/jgp.111.1.161.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmbystomaAnimalsBiological TransportCalciumCell MembraneColforsinCyclic AMP-Dependent Protein KinasesEnzyme ActivationEpithelial CellsHydrogen-Ion ConcentrationIon Channel GatingKidney Tubules, ProximalPatch-Clamp TechniquesPhosphorylationPotassium ChannelsProtein Kinase CSodium-Potassium-Exchanging ATPaseConceptsBasolateral membraneProtein kinase AActin cytoskeletonATPase pumpOuter membraneProtein kinaseKinase ACellular metabolismKATP channelsSecond messengerStimulation of transportTransport activityPhysiological importanceMembrane stretchPhorbol esterChannel activityMembrane patchesRegulationIntracellularO patchesFunctional couplingHypotonic swellingCell-attached patchesCell depolarizationRenal proximal tubules
1995
Primary structure and functional expression of a cGMP-gated potassium channel.
Yao X, Segal AS, Welling P, Zhang X, McNicholas CM, Engel D, Boulpaep EL, Desir GV. Primary structure and functional expression of a cGMP-gated potassium channel. Proceedings Of The National Academy Of Sciences Of The United States Of America 1995, 92: 11711-11715. PMID: 8524834, PMCID: PMC40472, DOI: 10.1073/pnas.92.25.11711.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCloning, MolecularCyclic GMPElectric ConductivityGene LibraryIon Channel GatingMolecular Sequence DataOocytesPhylogenyPotassiumPotassium ChannelsProtein BiosynthesisProtein ConformationRabbitsRNA, MessengerSequence Homology, Amino AcidTissue DistributionXenopusConceptsDeduced amino acid sequenceChannel protein phosphorylationCysteine-rich regionAmino acid sequenceNorthern blot analysisPotassium channel activityProtein phosphorylationAcid sequenceGene expressionPrimary structureFunctional expressionK channelsIon channelsChannel activityBlot analysisCyclic nucleotidesShaker K channelsPotassium channelsEffects of substancesKCN1Intracellular cGMPCGMPNitric oxideExpressionImportant roleA Calcium-activated and nucleotide-sensitive nonselective cation channel in M-1 mouse cortical collecting duct cells
Korbmacher C, Volk T, Segal A, Boulpaep E, Frömter E. A Calcium-activated and nucleotide-sensitive nonselective cation channel in M-1 mouse cortical collecting duct cells. The Journal Of Membrane Biology 1995, 146: 29-45. PMID: 7563035, DOI: 10.1007/bf00232678.Peer-Reviewed Original ResearchConceptsSensitive nonselective cation channelNSC channelNonselective cation channelsDuct cellsAmiloride-sensitive sodium absorptionCation channelsChannel activityAdenine nucleotidesVoltage-dependent blockCalcium entryNonselective cation channel activitySodium absorptionCation channel activityCytoplasmic calciumInhibitory effectSpecial physiological conditionsCytoplasmic applicationMiceCGMP-dependent protein kinaseFlufenamic acidSingle-channel current recordingsMajor routeVolume regulationCurrent recordingsCGMP
1992
Mouse cortical collecting duct cells show nonselective cation channel activity and express a gene related to the cGMP-gated rod photoreceptor channel.
Ahmad I, Korbmacher C, Segal A, Cheung P, Boulpaep E, Barnstable C. Mouse cortical collecting duct cells show nonselective cation channel activity and express a gene related to the cGMP-gated rod photoreceptor channel. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 10262-10266. PMID: 1279673, PMCID: PMC50318, DOI: 10.1073/pnas.89.21.10262.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceBlotting, NorthernCell LineCyclic GMPDNAIon Channel GatingIon ChannelsKidney CortexKidney Tubules, CollectingMembrane PotentialsMiceMolecular Sequence DataOligodeoxyribonucleotidesPhotoreceptor CellsPoly APolymerase Chain ReactionRatsRNARNA, MessengerSequence Homology, Nucleic AcidConceptsNonselective cation channelsPhotoreceptor channelDuct cellsCation channel probeCation channelsChannel activityPolymerase chain reactionNonselective cation channel activityCGMP decreaseCation channel activityChannel subunitsCytoplasmic applicationChain reactionRod photoreceptorsNorthern blot analysisRetinal cGMPBlot analysisCGMPRat kidney cDNA libraryChannel genesMiceSingle-channel conductanceOpen probabilityCellsCalcium removal
1986
Regulation of single potassium ion channels from apical membrane of rabbit collecting tubule
Hunter M, Lopes A, Boulpaep E, Giebisch G. Regulation of single potassium ion channels from apical membrane of rabbit collecting tubule. American Journal Of Physiology 1986, 251: f725-f733. PMID: 2429562, DOI: 10.1152/ajprenal.1986.251.4.f725.Peer-Reviewed Original ResearchConceptsCortical collecting tubuleCollecting tubuleRabbit cortical collecting tubuleBath calcium concentrationOpen probabilityPatch-clamp techniqueOne-half maximalApical membranePotassium secretionChannel open timeIntracellular calciumPotassium ion channelsChannel open probabilityCalcium concentrationMM calciumChannel activityTubulesIon channelsBath solutionSecretionOpen timeTransmembrane potentialCalciumFunction of calciumApparent Ki
1984
Single channel recordings of calcium-activated potassium channels in the apical membrane of rabbit cortical collecting tubules.
Hunter M, Lopes A, Boulpaep E, Giebisch G. Single channel recordings of calcium-activated potassium channels in the apical membrane of rabbit cortical collecting tubules. Proceedings Of The National Academy Of Sciences Of The United States Of America 1984, 81: 4237-4239. PMID: 6330754, PMCID: PMC345404, DOI: 10.1073/pnas.81.13.4237.Peer-Reviewed Original ResearchConceptsPotassium channelsRabbit cortical collecting tubuleCalcium concentrationCalcium-activated potassium channelsDose-dependent fashionCortical collecting tubulePatch-clamp techniqueCollecting tubuleSingle potassium channelsApical membraneOpen channel probabilitySingle-channel recordingsSlope conductanceChannel activityTubulesChannel recordingsRecordings