2009
Protein-protein interactions among ion channels regulate ion transport in the kidney.
Boulpaep E. Protein-protein interactions among ion channels regulate ion transport in the kidney. Bulletin Et Mémoires De L'Académie Royale De Médecine De Belgique 2009, 164: 133-41; discussion 141-2. PMID: 20120088.Peer-Reviewed Original ResearchConceptsAMP kinaseProtein CFTRCFTR channel gatingMembrane transport proteinsProtein-protein interactionsMembrane-attached proteinsSerine-threonine kinaseRegulation of transportKir 1.1Mg-ATPIon transportExtracellular agonistsMembrane proteinsTransport proteinsChannel gatingIntracellular ATP concentrationIntracellular messengerMembrane receptorsCFTRMetabolic signalsIon channelsChloride channelsEpithelial ion transportDirect interactionRenal K secretion
1997
Tubule electrophysiology: from single channels back to the renal epithelium.
Boulpaep E. Tubule electrophysiology: from single channels back to the renal epithelium. Wiener Klinische Wochenschrift 1997, 109: 489-92. PMID: 9261991.Peer-Reviewed Original ResearchConceptsMacroscopic membrane propertiesMicroscopic parametersSingle channel proteinsElectrical propertiesIon flowMacroscopic referenceSingle barrierMembrane patchesRenal epitheliumSingle channelRenal ion transportRenal ion channelsRegulatory domainExperimental errorChannel proteinsPore conductivityIon channelsWhole-cell conductancePatch-clamp technologyBasolateral membraneRenal tubule cellsCell membrane parametersIon selectivityIon transportOpen probability
1996
A novel preparation of dissociated renal proximal tubule cells that maintain epithelial polarity in suspension
Segal A, Boulpaep E, Maunsbach A. A novel preparation of dissociated renal proximal tubule cells that maintain epithelial polarity in suspension. American Journal Of Physiology 1996, 270: c1843-c1863. PMID: 8764170, DOI: 10.1152/ajpcell.1996.270.6.c1843.Peer-Reviewed Original ResearchConceptsEpithelial polarityFunctional polaritySingle cellsMembrane trafficking pathwaysCell surface polarityBasolateral membrane domainsIon channel proteinsBasolateral membraneApical brush borderCell polarityTrafficking pathwaysActin cytoskeletonMembrane domainsProximal tubule cellsMost epithelial cellsChannel proteinsZO-1 proteinTubule cellsJunctional complexesTight junctional complexesPolarized structureSingle cell modelEpithelial cellsRenal proximal tubule cellsZO-1
1995
A 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 ResearchMeSH KeywordsAnimalsCalciumElectric ConductivityFemaleIon ChannelsKidney CortexKidney TubulesKineticsPotassiumRabbitsConceptsPotassium 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
1983
Rheogenic transport in the renal proximal tubule.
Sackin H, Boulpaep E. Rheogenic transport in the renal proximal tubule. The Journal Of General Physiology 1983, 82: 819-851. PMID: 6319539, PMCID: PMC2228722, DOI: 10.1085/jgp.82.6.819.Peer-Reviewed Original Research
1979
Effect of amiloride on the apical cell membrane cation channels of a sodium-absorbing, potassium-secreting renal epithelium
O'Neil R, Boulpaep E. Effect of amiloride on the apical cell membrane cation channels of a sodium-absorbing, potassium-secreting renal epithelium. The Journal Of Membrane Biology 1979, 50: 365-387. PMID: 513119, DOI: 10.1007/bf01868898.Peer-Reviewed Original ResearchConceptsLumen-negative transepithelial potential differenceActive Na absorptionApical cell membraneEffects of amilorideEquivalent short-circuit currentTransepithelial potential differenceNa absorptionMaximum inhibitory concentrationAmilorideDiuretic amilorideCation channelsCell membraneNa channelsInhibitory concentrationRenal epitheliumMembrane cation channelsRemoval of NaAbsence of NaTight junctionsPerfusateK permeabilityTubulesLumenEquivalent electrical circuit analysis and rheogenic pumps in epithelia.
Boulpaep E, Sackin H. Equivalent electrical circuit analysis and rheogenic pumps in epithelia. The FASEB Journal 1979, 38: 2030-6. PMID: 437145.Peer-Reviewed Original Research
1978
Segmental heterogeneity and effects of organic solutes on ion transport across the Nectums proximal tubule studied with electrophysiological techniques
Steels P, Boulpaep E. Segmental heterogeneity and effects of organic solutes on ion transport across the Nectums proximal tubule studied with electrophysiological techniques. Archives Of Physiology And Biochemistry 1978, 86: 688-689. PMID: 83844, DOI: 10.3109/13813457809055945.Peer-Reviewed Original Research