2010
Renalase deficiency aggravates ischemic myocardial damage
Wu Y, Xu J, Velazquez H, Wang P, Li G, Liu D, Sampaio-Maia B, Quelhas-Santos J, Russell K, Russell R, Flavell RA, Pestana M, Giordano F, Desir GV. Renalase deficiency aggravates ischemic myocardial damage. Kidney International 2010, 79: 853-860. PMID: 21178975, DOI: 10.1038/ki.2010.488.Peer-Reviewed Original ResearchConceptsChronic kidney diseaseWild-type miceRenalase deficiencyKnockout micePlasma blood urea nitrogenLevels of renalaseMild ventricular hypertrophyRenalase knockout mouseNormal systolic functionTraditional risk factorsPlasma catecholamine levelsIschemic myocardial damageBlood urea nitrogenCardiac complicationsCardiovascular complicationsSystolic functionVentricular hypertrophyCardioprotective effectsCatecholamine levelsKidney diseaseMyocardial damageMyocardial necrosisRecombinant renalaseRisk factorsCardiac ischemia
2002
Regulation 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
1998
Rabbit distal convoluted tubule coexpresses NaCl cotransporter and 11β-hydroxysteroid dehydrogenase II mRNA
Velázquez H, Náray-Fejes-Tóth A, Silva T, Andújar E, Reilly RF, Desir GV, Ellison DH. Rabbit distal convoluted tubule coexpresses NaCl cotransporter and 11β-hydroxysteroid dehydrogenase II mRNA. Kidney International 1998, 54: 464-472. PMID: 9690213, DOI: 10.1046/j.1523-1755.1998.00036.x.Peer-Reviewed Original ResearchConceptsProximal tubulesNaCl cotransporterNephron segmentsDissected nephron segmentsTarget tissuesAction of aldosteroneAldosterone target tissuesSame nephron segmentsPolymerase chain reaction techniqueReverse transcriptase/polymerase chain reaction techniqueChain reaction techniqueDietary NaClDistal nephronBeta-HSDCCD samplesMRNA expressionNaCl cotransportRecent evidenceSimilar extentAldosteroneCotransporterHigh ratePrincipal targetTubulesTissue
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 role
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
Isolation 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