2005
Molecular Diversity and Regulation of Renal Potassium Channels
Hebert SC, Desir G, Giebisch G, Wang W. Molecular Diversity and Regulation of Renal Potassium Channels. Physiological Reviews 2005, 85: 319-371. PMID: 15618483, PMCID: PMC2838721, DOI: 10.1152/physrev.00051.2003.Peer-Reviewed Original ResearchConceptsRenal potassium channelsAnimal cellsCell movementDistinct functionsMolecular diversitySuccessful cloningRenal tubule epithelial cellsExcitable cellsSingle-channel analysisBiophysical propertiesMembrane potentialTubule epithelial cellsEpithelial cellsPotassium channelsRegulationCell volumeCellsImportant roleCloningTubule cellsPlantsDiversitySignificant progressFunction
2004
The voltage-gated potassium channel Kv1.3 regulates peripheral insulin sensitivity
Xu J, Wang P, Li Y, Li G, Kaczmarek LK, Wu Y, Koni PA, Flavell RA, Desir GV. The voltage-gated potassium channel Kv1.3 regulates peripheral insulin sensitivity. Proceedings Of The National Academy Of Sciences Of The United States Of America 2004, 101: 3112-3117. PMID: 14981264, PMCID: PMC365752, DOI: 10.1073/pnas.0308450100.Peer-Reviewed Original ResearchMeSH KeywordsAdipose TissueAnimalsBiological TransportFastingGlucoseInsulinInterleukin-6JNK Mitogen-Activated Protein KinasesKineticsKv1.3 Potassium ChannelMaleMiceMice, Inbred C57BLMice, KnockoutMice, ObeseMitogen-Activated Protein KinasesModels, BiologicalMuscle, SkeletalPotassium ChannelsPotassium Channels, Voltage-GatedTumor Necrosis Factor-alphaConceptsKv1.3-/- micePeripheral glucose homeostasisPeripheral insulin sensitivityPlasma membraneGene inactivationInsulin sensitivityAmount of GLUT4Skeletal muscleTerminal kinase (JNK) activityGlucose homeostasisAdipose tissueLower blood insulin levelsVoltage-gated potassium channelsInsulin-stimulated glucose uptakeVoltage-gated potassium channel Kv1.3Tumor necrosis factor productionExperimental autoimmune encephalitisBlood insulin levelsHigh-fat dietPotassium channel Kv1.3Tumor necrosis factor secretionPeripheral T lymphocytesKinase activityNecrosis factor productionNumber of tissues
2003
The voltage-gated potassium channel Kv1.3 regulates energy homeostasis and body weight
Xu J, Koni PA, Wang P, Li G, Kaczmarek L, Wu Y, Li Y, Flavell RA, Desir GV. The voltage-gated potassium channel Kv1.3 regulates energy homeostasis and body weight. Human Molecular Genetics 2003, 12: 551-559. PMID: 12588802, DOI: 10.1093/hmg/ddg049.Peer-Reviewed Original ResearchConceptsBody weightBasal metabolic rateKv1.3 channelsDiet-induced obesityHigh-fat dietBody weight regulationT cell activationVoltage-gated potassium channel Kv1.3Voltage-gated potassium channelsPotassium channel Kv1.3Control littermatesFood intakeLittermate controlsKnockout miceWeight regulationIndirect calorimetryMetabolic rateChannel inhibitionCell activationEnergy homeostasisKnockout animalsPotassium channelsCell membrane potentialMiceChannel Kv1.3
2002
Expression of KCNA10, a voltage-gated K channel, in glomerular endothelium and at the apical membrane of the renal proximal tubule.
Yao X, Tian S, Chan HY, Biemesderfer D, Desir GV. Expression of KCNA10, a voltage-gated K channel, in glomerular endothelium and at the apical membrane of the renal proximal tubule. Journal Of The American Society Of Nephrology 2002, 13: 2831-9. PMID: 12444201, DOI: 10.1097/01.asn.0000036866.37886.c5.Peer-Reviewed Original ResearchConceptsVascular smooth muscle cellsProximal tubular cellsSmooth muscle cellsApical membraneImportant cellular functionsSitu hybridization experimentsVascular toneVoltage-activated K channelsTubular cellsMuscle cellsImmunocytochemical studyCellular functionsHuman proximal tubular cellsRat proximal tubular cellsSubcellular localizationHybridization experimentsVoltage-gated K channelsK channelsNorthern blotRenal proximal tubulesCell membrane voltageVascular endothelial cellsKCNA10Cell membrane potentialVascular tissueRegulation of the voltage-gated K+ channel KCNA10 by KCNA4B, a novel β-subunit
Tian S, Liu W, Wu Y, Rafi H, Segal AS, Desir GV. Regulation of the voltage-gated K+ channel KCNA10 by KCNA4B, a novel β-subunit. American Journal Of Physiology. Renal Physiology 2002, 283: f142-f149. PMID: 12060596, DOI: 10.1152/ajprenal.00258.2001.Peer-Reviewed Original Research
2000
KCNA10: a novel ion channel functionally related to both voltage-gated potassium and CNG cation channels
Lang R, Lee G, Liu W, Tian S, Rafi H, Orias M, Segal A, Desir G. KCNA10: a novel ion channel functionally related to both voltage-gated potassium and CNG cation channels. American Journal Of Physiology. Renal Physiology 2000, 278: f1013-f1021. PMID: 10836990, DOI: 10.1152/ajprenal.2000.278.6.f1013.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceCyclic Nucleotide-Gated Cation ChannelsDNA PrimersFemaleHumansIn Vitro TechniquesIon Channel GatingIon ChannelsMembrane PotentialsOocytesPatch-Clamp TechniquesPotassium Channel BlockersPotassium ChannelsPotassium Channels, Voltage-GatedRabbitsRecombinant ProteinsSecond Messenger SystemsShaker Superfamily of Potassium ChannelsXenopus laevisClose Association of the N Terminus of Kv1.3 with the Pore Region*
Yao X, Liu W, Tian S, Rafi H, Segal A, Desir G. Close Association of the N Terminus of Kv1.3 with the Pore Region*. Journal Of Biological Chemistry 2000, 275: 10859-10863. PMID: 10753881, DOI: 10.1074/jbc.275.15.10859.Peer-Reviewed Original ResearchConceptsN-terminusPore regionSteady-state protein levelsLarge single-channel conductanceVoltage-gated potassium channelsWild-type channelsShaker proteinCertain amino acidsChannel assemblyWild typeChannel proteinsChannel functionAmino acidsSingle-channel conductancePore blockersSpeed of inactivationTerminusProtein levelsDomain leadPore selectivityPotassium channelsProteinType channelsKinetic propertiesChannel conductance
1999
The T0 Domain of Rabbit KV1.3 Regulates Steady State Channel Protein Level
Segal A, Yao X, Desir G. The T0 Domain of Rabbit KV1.3 Regulates Steady State Channel Protein Level. Biochemical And Biophysical Research Communications 1999, 254: 54-64. PMID: 9920732, DOI: 10.1006/bbrc.1998.9801.Peer-Reviewed Original ResearchConceptsN-terminal regulatory regionVoltage-gated potassium channelsWild-type channelsRegulatory regionsPlasma membraneAmino terminusChannel assemblyChannel proteinsRecognition domainSingle-channel conductanceKv channelsChannel protein levelsProtein levelsProtein densityPotassium channelsOpen probabilityType channelsChannel conductanceKv1.3Fast inactivationDomainMembraneTerminusProteinInactivation
1998
Characterization of a Regulatory Region in the N-Terminus of Rabbit Kv1.3
Yao X, Huang Y, Kwan HY, Chan P, Segal AS, Desir G. Characterization of a Regulatory Region in the N-Terminus of Rabbit Kv1.3. Biochemical And Biophysical Research Communications 1998, 249: 492-498. PMID: 9712724, DOI: 10.1006/bbrc.1998.9122.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsChemical PhenomenaChemistry, PhysicalDynaminsElectric ConductivityEndocytosisFemaleGene DeletionGene ExpressionGTP PhosphohydrolasesKv1.3 Potassium ChannelMolecular Sequence DataMutagenesisOocytesPeptide FragmentsPotassium ChannelsPotassium Channels, Voltage-GatedProtein Sorting SignalsRabbitsRNA, ComplementaryStructure-Activity RelationshipTransfectionXenopus laevis
1997
Cloning and localization of a double-pore K channel, KCNK1: exclusive expression in distal nephron segments
Orias M, Velázquez H, Tung F, Lee G, Desir G. Cloning and localization of a double-pore K channel, KCNK1: exclusive expression in distal nephron segments. American Journal Of Physiology 1997, 273: f663-f666. PMID: 9362344, DOI: 10.1152/ajprenal.1997.273.4.f663.Peer-Reviewed Original ResearchConceptsThick ascending limbAscending limbK channelsCortical thick ascending limbMedullary thick ascending limbDistal nephron segmentsReverse transcription-polymerase chain reactionDistal convoluted tubuleTranscription-polymerase chain reactionDistal tubulesConvoluted tubulesProximal tubulesNephron segmentsHigh expressionNephron segment localizationK homeostasisChain reactionHuman kidney cDNATubulesSegment localizationExclusive expressionKCNK1LimbPore regionKidney cDNAGenomic Localization of the Human Gene for KCNA10, a cGMP-Activated K Channel
Orias M, Bray-Ward P, Curran M, Keating M, Desir G. Genomic Localization of the Human Gene for KCNA10, a cGMP-Activated K Channel. Genomics 1997, 42: 33-37. PMID: 9177773, DOI: 10.1006/geno.1997.4712.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceChromosome MappingChromosomes, Artificial, YeastChromosomes, Human, Pair 1Cloning, MolecularCyclic GMPDNA PrimersHumansIn Situ Hybridization, FluorescenceMicrosatellite RepeatsMolecular Sequence DataPolymerase Chain ReactionPotassium ChannelsPotassium Channels, Voltage-GatedShaker Superfamily of Potassium ChannelsConceptsHuman genesK channel genesCandidate gene analysisGenomic localizationMicrosatellite lociCellular functionsGenetic intervalYAC clonesChromosome 1Channel genesFiner mappingGenesKCNA10Gene analysisSitu hybridizationK channelsCritical rolePotassium channelsIntracellular cGMPP13.1KCNA3CGMPImportant componentLociClones
1996
Genomic structure and regulation of Kcn1, a cGMP-gated potassium channel
Yao X, Liu Y, Tung F, Desir GV. Genomic structure and regulation of Kcn1, a cGMP-gated potassium channel. American Journal Of Physiology 1996, 271: f37-f41. PMID: 8760241, DOI: 10.1152/ajprenal.1996.271.1.f37.Peer-Reviewed Original ResearchConceptsCis-regulatory elementsPromoter regionEnhancer elementsNovel potassium channel geneMajor transcription initiation siteTypical TATA boxTranscription initiation sitePhorbol esterPotassium channel genesLuciferase reporter constructsPotassium channelsGenomic structurePorcine kidney cell lineDeletion analysisRabbit geneTATA boxAcid proteinGene transcriptionKidney cell lineReporter constructsChannel genesSequence analysisPrimer extensionInitiation siteNorthern blotMolecular cloning of a glibenclamide-sensitive, voltage-gated potassium channel expressed in rabbit kidney.
Yao X, Chang AY, Boulpaep EL, Segal AS, Desir GV. Molecular cloning of a glibenclamide-sensitive, voltage-gated potassium channel expressed in rabbit kidney. Journal Of Clinical Investigation 1996, 97: 2525-2533. PMID: 8647945, PMCID: PMC507338, DOI: 10.1172/jci118700.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBrainCloning, MolecularDNA PrimersFemaleGenetic VariationGenomic LibraryGlyburideHumansKidney MedullaKv1.3 Potassium ChannelMiceModels, BiologicalMolecular Sequence DataOocytesPancreatitis-Associated ProteinsPhylogenyPolymerase Chain ReactionPotassium ChannelsPotassium Channels, Voltage-GatedRabbitsRecombinant ProteinsSequence Homology, Amino AcidXenopus laevisConceptsVoltage-gated potassium channelsMolecular cloningFunctional expressionShaker-like potassium channelsPotassium channelsShaker geneGRB-PAP1Novel memberAmino terminusMolecular evidenceShaker channelsAmino acidsXenopus oocytesRabbit kidneyRenal potassium transportCloningGenesPotassium transportChannel clonesFirst reportRabbit brainPotassium conductanceFamilyExpressionKidney
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 roleMolecular characterization of voltage and cyclic nucleotide-gated potassium channels in kidney
Desir G. Molecular characterization of voltage and cyclic nucleotide-gated potassium channels in kidney. Kidney International 1995, 48: 1031-1035. PMID: 8569064, DOI: 10.1038/ki.1995.386.Peer-Reviewed Original ResearchConceptsRenal K channelsMolecular characterizationInitial molecular characterizationPotassium channelsMammalian cellsMembrane proteinsMolecular biologyCell membraneK channelsDiverse groupPhysiologic roleKinetic propertiesPotential physiologic rolePassive movementBiologyProteinPhysiologyKidneyMembraneCharacterizationCellsExtensive dataThe structure, regulation and pathophysiology of potassium channels
Desir G. The structure, regulation and pathophysiology of potassium channels. Current Opinion In Nephrology & Hypertension 1995, 4: 402-405. PMID: 8564442, DOI: 10.1097/00041552-199509000-00005.Peer-Reviewed Original Research
1993
Identification of a novel K-channel gene (KC22) that is highly expressed in distal tubule of rabbit kidney
Desir GV, Velazquez H. Identification of a novel K-channel gene (KC22) that is highly expressed in distal tubule of rabbit kidney. American Journal Of Physiology 1993, 264: f128-f133. PMID: 7679255, DOI: 10.1152/ajprenal.1993.264.1.f128.Peer-Reviewed Original ResearchConceptsPolymerase chain reactionRabbit kidneyKidney cortexWhole kidney cortexShaker gene familyDistal tubule cellsVoltage-gated K channelsRenal tissueDistal tubulesTubule cellsRibonuclease protectionPrimary culturesKidneyChain reactionExpression levelsK channelsCortexTubulesPartial-length sequencesAbundant isoformIsoformsKidney cDNAK channel genes
1992
Molecular physiology of renal potassium channels.
Desir G. Molecular physiology of renal potassium channels. Seminars In Nephrology 1992, 12: 531-40. PMID: 1475548.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsHumansHypertensionIon Channel GatingKidneyMembrane PotentialsMolecular BiologyPotassium ChannelsConceptsRenal potassium channelsExtensive physiological dataMolecular biological techniquesMolecular physiologyImportant disease statesEnormous diversityK channelsIon channelsMolecular informationCellular proliferationBiological techniquesPotassium channelsRecent appreciationPossible roleDisease statesK transportMajor rolePatch-clamp techniqueDiversityPhysiological dataChannel structurePhysiologyRegulationRoleProliferationInhibition of Ca-activated K+ channels from renal microvillus membrane vesicles by amiloride analogs
Zweifach A, Desir G, Aronson P, Giebisch G. Inhibition of Ca-activated K+ channels from renal microvillus membrane vesicles by amiloride analogs. The Journal Of Membrane Biology 1992, 128: 115-122. PMID: 1501239, DOI: 10.1007/bf00231884.Peer-Reviewed Original ResearchIsolation of putative voltage-gated epithelial K-channel isoforms from rabbit kidney and LLC-PK1 cells
Desir GV, Hamlin HA, Puente E, Reilly RF, Hildebrandt F, Igarashi P. Isolation of putative voltage-gated epithelial K-channel isoforms from rabbit kidney and LLC-PK1 cells. American Journal Of Physiology 1992, 262: f151-f157. PMID: 1733291, DOI: 10.1152/ajprenal.1992.262.1.f151.Peer-Reviewed Original ResearchConceptsDeduced amino acid sequenceAmino acid sequenceAcid sequenceVoltage-gated K channelsRabbit genomic DNAPutative transmembrane segmentsShaker-like genesPutative voltage sensorShaker gene familyVoltage-gated potassium channelsGene familyShaker proteinRenal epithelial cellsTransmembrane segmentsSequence similarityRabbit cDNAEpithelial cell lineSouthern analysisProtein sequencesLLC-PK1 cellsDifferent genesGenomic DNAKidney cDNACDNAS4 segment