2008
Shear-induced reorganization of renal proximal tubule cell actin cytoskeleton and apical junctional complexes
Duan Y, Gotoh N, Yan Q, Du Z, Weinstein A, Wang T, Weinbaum S. Shear-induced reorganization of renal proximal tubule cell actin cytoskeleton and apical junctional complexes. Proceedings Of The National Academy Of Sciences Of The United States Of America 2008, 105: 11418-11423. PMID: 18685100, PMCID: PMC2516248, DOI: 10.1073/pnas.0804954105.Peer-Reviewed Original ResearchConceptsProximal tubule cellsAdherens junctionsTight junctionsEndothelial cellsEpithelial cellsMouse proximal tubule cellsCell actin cytoskeletonDistribution of filamentous actinActin cytoskeletal reorganizationStress fiber disruptionActin-disrupting drugsApical junctional complexRenal epithelial cellsPeripheral actin bandsCuboidal epithelial cellsVascular endothelial cellsActin cytoskeletonFilamentous actinCytoskeletal reorganizationCytoskeletal responsesF-actinTubule cellsRenal epitheliumCytochalasin D.Water reabsorption
2007
Transgenic RNAi Depletion of Claudin-16 and the Renal Handling of Magnesium*
Hou J, Shan Q, Wang T, Gomes A, Yan Q, Paul D, Bleich M, Goodenough D. Transgenic RNAi Depletion of Claudin-16 and the Renal Handling of Magnesium*. Journal Of Biological Chemistry 2007, 282: 17114-17122. PMID: 17442678, DOI: 10.1074/jbc.m700632200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceClaudinsDNA PrimersKidneyLentivirusMagnesiumMembrane ProteinsMiceMice, KnockoutMicroscopy, ConfocalRNA InterferenceConceptsClaudin-16Tight junction proteinsTight junction proteins claudin-16Junction proteinsRenal handlingTight junctionsRenal handling of magnesiumRenal wasting of magnesiumParacellular ion reabsorptionHandling of magnesiumKnock-downFamilial hypomagnesemiaRenal functionElectrolyte disordersCation channelsTarget of drug developmentAscending limbMouse modelFHHNCParacellular cation channelsControl of ion homeostasisRenal controlIn vivo analysisIon reabsorptionNephrocalcinosis
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
2005
Role of PDZK1 in membrane expression of renal brush border ion exchangers
Thomson RB, Wang T, Thomson BR, Tarrats L, Girardi A, Mentone S, Soleimani M, Kocher O, Aronson PS. Role of PDZK1 in membrane expression of renal brush border ion exchangers. Proceedings Of The National Academy Of Sciences Of The United States Of America 2005, 102: 13331-13336. PMID: 16141316, PMCID: PMC1201624, DOI: 10.1073/pnas.0506578102.Peer-Reviewed Original ResearchConceptsProximal tubulesExpression of NHE3Functional activityRole of PDZK1Protein PDZK1Reabsorption of NaBrush border expressionMammalian kidneyCFEXBrush border localizationMutant miceGST fusion proteinProtein expressionKidneyBrush border membrane proteinsExchanger NHE3Membrane expressionNHE3Brush borderBrush border membrane vesiclesPDZK1 interactionTubulesNormal expressionMembrane proteinsPDZK1
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