2002
On the natriuretic effect of verapamil: inhibition of ENaC and transepithelial sodium transport
Segal AS, Hayslett JP, Desir GV. On the natriuretic effect of verapamil: inhibition of ENaC and transepithelial sodium transport. American Journal Of Physiology. Renal Physiology 2002, 283: f765-f770. PMID: 12217868, DOI: 10.1152/ajprenal.00253.2001.Peer-Reviewed Original ResearchMeSH KeywordsAldosteroneAnimalsBiological Transport, ActiveCalcium Channel BlockersCells, CulturedDose-Response Relationship, DrugElectrophysiologyEpithelial Sodium ChannelsEpitheliumIn Vitro TechniquesInsulinKidneyKidney Tubules, CollectingNatriuresisNifedipineOocytesPatch-Clamp TechniquesSodiumSodium Channel BlockersSodium ChannelsVasopressinsVerapamilXenopus laevisConceptsNatriuretic effectDirect tubular effectAdministration of verapamilRemoval of extracellularTubular effectsTransepithelial sodium transportHemodynamic changesInhibition of ENaCSurrogate markerChannel blockersMicroM verapamilDistal tubulesA6 cellsMicroM amilorideUssing chambersVerapamilL-typeSodium transportBasolateral sideTransepithelial resistanceSignificant increaseApical sidePermeable supportsInhibitionTransepithelialRegulation 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
Defective processing and expression of thiazide-sensitive Na-Cl cotransporter as a cause of Gitelman’s syndrome
Kunchaparty S, Palcso M, Berkman J, Velázquez H, Desir G, Bernstein P, Reilly R, Ellison D. Defective processing and expression of thiazide-sensitive Na-Cl cotransporter as a cause of Gitelman’s syndrome. American Journal Of Physiology 1999, 277: f643-f649. PMID: 10516289, DOI: 10.1152/ajprenal.1999.277.4.f643.Peer-Reviewed Original ResearchConceptsWild-type cloneTransport proteinsWild-type proteinWild-type geneUnglycosylated proteinProtein processingNa-Cl cotransporterUnglycosylated formEndoplasmic reticulumMutant clonesFunctional expressionDisease mutationsDefective processingXenopus oocytesProteinClonesThiazide-sensitive Na-Cl cotransporterSodium uptakeMutationsOocytesMembrane stainingAutosomal recessive disorderWestern blot
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
1996
Molecular 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