2005
Kv1.3 potassium channel blockade as an approach to insulin resistance
Desir GV. Kv1.3 potassium channel blockade as an approach to insulin resistance. Expert Opinion On Therapeutic Targets 2005, 9: 571-579. PMID: 15948674, DOI: 10.1517/14728222.9.3.571.Peer-Reviewed Original ResearchConceptsInsulin resistanceInsulin sensitivityKv1.3 channel inhibitionPotassium channel blockadePeripheral insulin sensitivityPotential therapeutic targetDevastating metabolic diseaseType II diabetesVoltage-gated potassium channelsAbnormal glucoseDiabetes mellitusInsulin deficiencyDevelopment of drugsInflammatory cytokinesChannel blockadeGlucose metabolismTherapeutic targetCardinal featuresMetabolic diseasesChannel inhibitionII diabetesLipid metabolismHealthcare expendituresPotassium channelsPromising targetMolecular 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
2003
International Union of Pharmacology. XLI. Compendium of Voltage-Gated Ion Channels: Potassium Channels
Gutman GA, Chandy KG, Adelman JP, Aiyar J, Bayliss DA, Clapham DE, Covarriubias M, Desir GV, Furuichi K, Ganetzky B, Garcia ML, Grissmer S, Jan LY, Karschin A, Kim D, Kuperschmidt S, Kurachi Y, Lazdunski M, Lesage F, Lester HA, McKinnon D, Nichols CG, O'Kelly I, Robbins J, Robertson GA, Rudy B, Sanguinetti M, Seino S, Stuehmer W, Tamkun MM, Vandenberg CA, Wei A, Wulff H, Wymore RS. International Union of Pharmacology. XLI. Compendium of Voltage-Gated Ion Channels: Potassium Channels. Pharmacological Reviews 2003, 55: 583-586. PMID: 14657415, DOI: 10.1124/pr.55.4.9.Peer-Reviewed Original ResearchThe 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
2000
Close 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
1997
Genomic 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 ResearchMolecular Physiology of a Novel Cgmp-Gated Potassium Channel
Desir G. Molecular Physiology of a Novel Cgmp-Gated Potassium Channel. Medical Science Symposia Series 1995, 9: 237-245. DOI: 10.1007/978-94-011-0117-2_27.Peer-Reviewed Original Research
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 ResearchConceptsRenal potassium channelsExtensive physiological dataMolecular biological techniquesMolecular physiologyImportant disease statesEnormous diversityK channelsIon channelsMolecular informationCellular proliferationBiological techniquesPotassium channelsRecent appreciationPossible roleDisease statesK transportMajor rolePatch-clamp techniqueDiversityPhysiological dataChannel structurePhysiologyRegulationRoleProliferation
1991
Reconstitution and partial purification of an amiloride-sensitive, cation channel from rabbit kidney
Desir G. Reconstitution and partial purification of an amiloride-sensitive, cation channel from rabbit kidney. Biochimica Et Biophysica Acta 1991, 1067: 38-42. PMID: 1868102, DOI: 10.1016/0005-2736(91)90023-2.Peer-Reviewed Original ResearchConceptsBrush border membrane vesiclesCation channelsMembrane vesicle proteinsChannel activityAmiloride-sensitive cation channelVesicle proteinsBorder membrane vesiclesMembrane vesiclesRabbit brush border membrane vesiclesProteoliposomesNative brush border membranesBrush border membraneSensitive cation channelPotassium channelsProteinPartial purificationAcridine orangeRenal brush-border membrane vesiclesBorder membraneDiethylthiadicarbocyanine iodideReconstitutionRabbit kidney