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 laevis
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