2009
Inward rectifier channel, ROMK, is localized to the apical tips of glial‐like cells in mouse taste buds
Dvoryanchikov G, Sinclair M, Perea‐Martinez I, Wang T, Chaudhari N. Inward rectifier channel, ROMK, is localized to the apical tips of glial‐like cells in mouse taste buds. The Journal Of Comparative Neurology 2009, 517: 1-14. PMID: 19708028, PMCID: PMC3104395, DOI: 10.1002/cne.22152.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsFluorescent Antibody TechniqueGap JunctionsGlutamate DecarboxylaseGreen Fluorescent ProteinsImmunohistochemistryKidneyMiceMice, Inbred C57BLMice, KnockoutMice, TransgenicNeurogliaPhospholipase C betaPotassium Channels, Inwardly RectifyingProtein IsoformsReverse Transcriptase Polymerase Chain ReactionRNA, MessengerTaste BudsTight JunctionsConceptsTaste budsTaste cellsTight junctionsHyperpolarized resting membrane potentialInwardly rectifying K channelsMouse taste budsRT-PCRApical tight junctionsMouse taste cellsInward rectifier channelsFungiform taste budsReverse-transcription polymerase chain reactionGlial cell markersQuantitative (q)RT-PCRGlial-like cellsROMK mRNAApical tipExtracellular K(+Rectifier channelsCell markersPolymerase chain reactionK channelsTransgenic miceAction potentialsBuds
2006
Use of transgenic mice in acid-base balance studies.
Cantone A, Wang T, Pica A, Simeoni M, Capasso G. Use of transgenic mice in acid-base balance studies. Journal Of Nephrology 2006, 19 Suppl 9: s121-7. PMID: 16736435.Peer-Reviewed Original ResearchMeSH KeywordsAcid-Base EquilibriumAcid-Base ImbalanceAnimalsCation Transport ProteinsDisease Models, AnimalDNAGene ExpressionKidney TubulesMembrane ProteinsMiceMice, TransgenicNitric Oxide SynthaseSodium-Bicarbonate SymportersSodium-Hydrogen Exchanger 1Sodium-Hydrogen Exchanger 3Sodium-Hydrogen ExchangersConceptsNitric oxide synthaseAcid-base statusNa+/H+ exchangeBody acid-base statusTransgenic miceFunction of pendrinProximal tubule transportTransepithelial HCO3- absorptionPotassium-chloride cotransporterEndothelial isoform of nitric oxide synthaseIsoform of nitric oxide synthaseSubunit expression levelsKnockout animal modelsApical NHE3Basolateral NHE1HCO3- absorptionNa+/HCO3- cotransporterNatriuretic responseRegulation of acid-base balanceTubule transportDistal nephronProximal tubulesRenal diseaseChloride channelsAscending limb
2004
Mechanical stimuli induce cleavage and nuclear translocation of the polycystin-1 C terminus
Chauvet V, Tian X, Husson H, Grimm DH, Wang T, Hieseberger T, Igarashi P, Bennett AM, Ibraghimov-Beskrovnaya O, Somlo S, Caplan MJ. Mechanical stimuli induce cleavage and nuclear translocation of the polycystin-1 C terminus. Journal Of Clinical Investigation 2004, 114: 1433-1443. PMID: 15545994, PMCID: PMC525739, DOI: 10.1172/jci21753.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell LineCell NucleusChlorocebus aethiopsCHO CellsCOS CellsCricetinaeCricetulusDogsEmbryo, MammalianEpithelial CellsKidney TubulesMembrane ProteinsMiceMice, TransgenicPolycystic Kidney, Autosomal DominantProteinsSequence DeletionSignal TransductionStress, MechanicalTranscription Factor AP-1TRPP Cation ChannelsConceptsC-terminal tailAutosomal dominant polycystic kidney diseaseCell-matrix interactionsCiliary signalingSecond genePolycystin-2Polycystin-1C-terminusNovel pathwayProteolytic cleavageNuclear translocationMechanical stimuliGenesDominant polycystic kidney diseasePolycystic kidney diseasePrecise mechanismCleavageTerminusSignalingTranslocationNucleusPathway
1999
Nongastric H+,K+-ATPase: cell biologic and functional properties.
Grishin AV, Reinhard J, Dunbar LA, Courtois-Coutry N, Wang T, Giebisch G, Caplan MJ. Nongastric H+,K+-ATPase: cell biologic and functional properties. Seminars In Nephrology 1999, 19: 421-30. PMID: 10511382.Peer-Reviewed Original ResearchConceptsATPase isoformsP-type ATPasesEndocytic regulationEndocytosis signalATPase familyCell machineryCytoplasmic tailK resorptionATPasesIon pumpsATPase isoform expressionApical surfaceIsoformsCell biologicIsoform expressionPhysiological studiesTubule epithelial cellsATPaseEpithelial cellsTransgenic miceCation transportK transportFunctional propertiesRenal K transportEndocytosis
1998
A tyrosine-based signal regulates H-K-ATPase-mediated potassium reabsorption in the kidney
Wang T, Courtois-Coutry N, Giebisch G, Caplan M. A tyrosine-based signal regulates H-K-ATPase-mediated potassium reabsorption in the kidney. American Journal Of Physiology 1998, 275: f818-f826. PMID: 9815140, DOI: 10.1152/ajprenal.1998.275.5.f818.Peer-Reviewed Original ResearchConceptsGlomerular filtration rateTransgenic miceGastric acid outputPlasma K concentrationK pumpK-ATPaseRenal collecting tubulesK clearanceBlood pressurePotassium reabsorptionAcid outputUrine volumeK excretionFiltration rateGastric acidK reabsorptionPump functionCollecting tubuleMicePlasma NaTyrosine-based sequenceTyrosine-based signalsKidneyExcretionCytoplasmic tailTubule Function in Transgenic Mice
Wang T, Giebisch G. Tubule Function in Transgenic Mice. Nephron 1998, 6: 447-453. PMID: 9730661, DOI: 10.1159/000020554.Peer-Reviewed Original ResearchConceptsNa-HK-ATPaseK-ATPase expressionRenal tubule transportRenal electrolyte transportStrains of miceRenal transport functionsTransport functionColonic isoformH,K-ATPaseIsoforms NHE2Isoforms NHE1Tubule transportTubule functionTubule segmentsMouse modelTransgenic miceTransgenic knockoutTransport lesionKnockout modelsMiceKidney tubulesElectrolyte transportNull mutationTubules