2021
MAL2 mediates the formation of stable HER2 signaling complexes within lipid raft-rich membrane protrusions in breast cancer cells
Jeong J, Shin JH, Li W, Hong JY, Lim J, Hwang JY, Chung JJ, Yan Q, Liu Y, Choi J, Wysolmerski J. MAL2 mediates the formation of stable HER2 signaling complexes within lipid raft-rich membrane protrusions in breast cancer cells. Cell Reports 2021, 37: 110160. PMID: 34965434, PMCID: PMC8762588, DOI: 10.1016/j.celrep.2021.110160.Peer-Reviewed Original ResearchMeSH KeywordsAntineoplastic Agents, ImmunologicalBreast NeoplasmsCell ProliferationCytoskeletal ProteinsDrug Resistance, NeoplasmEndocytosisFemaleHumansMembrane MicrodomainsMyelin and Lymphocyte-Associated Proteolipid ProteinsPhosphoproteinsPlasma Membrane Calcium-Transporting ATPasesReceptor, ErbB-2Sodium-Hydrogen ExchangersTrastuzumabTumor Cells, CulturedConceptsLipid raft formationBreast cancer cellsLipid raftsLipid raft resident proteinsCancer cellsRaft formationRaft-resident proteinsProximity ligation assayProtein complexesMembrane protrusionsProtein interactionsPlasma membraneLigation assayMAL2Membrane stabilityStructural organizationPotential therapeutic targetPhysical interactionMembrane retentionProteinRaftsTherapeutic targetCellsIntracellular calcium concentrationLow intracellular calcium concentration
2019
NHERF1 Is Required for Localization of PMCA2 and Suppression of Early Involution in the Female Lactating Mammary Gland
Jeong J, Kim W, Hens J, Dann P, Schedin P, Friedman PA, Wysolmerski JJ. NHERF1 Is Required for Localization of PMCA2 and Suppression of Early Involution in the Female Lactating Mammary Gland. Endocrinology 2019, 160: 1797-1810. PMID: 31087002, PMCID: PMC6619491, DOI: 10.1210/en.2019-00230.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell PolarityFemaleLactationMammary Glands, AnimalMiceMice, Inbred C57BLMice, KnockoutPhosphoproteinsPlasma Membrane Calcium-Transporting ATPasesSodium-Hydrogen ExchangersConceptsPlasma membrane calcium ATPase 2Mammary epithelial cellsSpecialized plasma membrane domainsMammary epithelial cell deathLuminal epithelial cellsCell deathPremature mammary gland involutionBreast cancer cellsApical-basal polarityEpithelial cellsPlasma membrane domainsApical membraneSecretory luminal epithelial cellsExchanger regulatory factor 1Cell death pathwaysNHERF1 expressionMammary gland involutionCancer cellsRegulatory factor 1Sodium-hydrogen exchanger regulatory factor-1Lactating Mammary GlandNormal mammary epithelial cellsMembrane localizationEpithelial cell deathMembrane domains
2018
Regulation of renal Na transporters in response to dietary K
Yang L, Xu S, Guo X, Uchida S, Weinstein AM, Wang T, Palmer LG. Regulation of renal Na transporters in response to dietary K. American Journal Of Physiology. Renal Physiology 2018, 315: f1032-f1041. PMID: 29923764, PMCID: PMC6230734, DOI: 10.1152/ajprenal.00117.2018.Peer-Reviewed Original ResearchExtracellular anti-angiogenic proteins augment an endosomal protein trafficking pathway to reach mitochondria and execute apoptosis in HUVECs
Chen M, Qiu T, Wu J, Yang Y, Wright GD, Wu M, Ge R. Extracellular anti-angiogenic proteins augment an endosomal protein trafficking pathway to reach mitochondria and execute apoptosis in HUVECs. Cell Death & Differentiation 2018, 25: 1905-1920. PMID: 29523874, PMCID: PMC6219483, DOI: 10.1038/s41418-018-0092-9.Peer-Reviewed Original ResearchMeSH KeywordsAngiostatinsApoptosisCell MembraneEndocytosisEndoplasmic Reticulum Chaperone BiPEndosomesFibronectinsFluorescence Recovery After PhotobleachingHeat-Shock ProteinsHuman Umbilical Vein Endothelial CellsHumansMicroscopy, FluorescenceMitochondriaNeovascularization, PhysiologicPhosphoproteinsProtein TransportRecombinant ProteinsRNA InterferenceRNA, Small InterferingSodium-Hydrogen ExchangersSynaptosomal-Associated Protein 25ThrombospondinsConceptsLate endosomesEndosomal proteinExtracellular proteinsT-SNARE proteinsCytosolic scaffold proteinsTotal internal reflection fluorescent microscopyPro-apoptotic functionFluorescent microscopyRegulatory factor 1Recycling endosomesRNAi knockdownCargo degradationScaffold proteinSuper-resolution fluorescent microscopyMitochondrial traffickingCell fractionationPlasma membraneIsthminProximity ligationMitochondriaProtein 25ProteinBiochemical analysisAnti-angiogenic proteinFactor 1
2017
Gender difference in kidney electrolyte transport. I. Role of AT1a receptor in thiazide-sensitive Na+-Cl− cotransporter activity and expression in male and female mice
Li J, Hatano R, Xu S, Wan L, Yang L, Weinstein AM, Palmer L, Wang T. Gender difference in kidney electrolyte transport. I. Role of AT1a receptor in thiazide-sensitive Na+-Cl− cotransporter activity and expression in male and female mice. American Journal Of Physiology. Renal Physiology 2017, 313: f505-f513. PMID: 28566500, PMCID: PMC5582908, DOI: 10.1152/ajprenal.00087.2017.Peer-Reviewed Original ResearchMeSH KeywordsAngiotensin IIAnimalsDiuresisFemaleHydrochlorothiazideKidneyMaleMice, KnockoutNatriuresisPhenotypeProtein Serine-Threonine KinasesReceptor, Angiotensin, Type 1Receptors, DrugSex CharacteristicsSodium Chloride SymportersSodium-Hydrogen Exchanger 3Sodium-Hydrogen ExchangersSolute Carrier Family 12, Member 3ConceptsUrine volumeKO miceCotransporter activityRenal clearance experimentsReceptor knockout miceGlomerular filtration rateBolus intravenous injectionDelivery of NaClNCC protein expressionGender differencesFiltration rateFemale miceAT1A receptorClearance experimentsKO animalsIntravenous injectionNCC expressionDistal nephronFractional NaKnockout miceMale KOProximal tubulesHCTZMiceNHE3 expressionThe scaffolding protein NHERF1 regulates the stability and activity of the tyrosine kinase HER2
Jeong J, VanHouten JN, Kim W, Dann P, Sullivan C, Choi J, Sneddon WB, Friedman PA, Wysolmerski JJ. The scaffolding protein NHERF1 regulates the stability and activity of the tyrosine kinase HER2. Journal Of Biological Chemistry 2017, 292: 6555-6568. PMID: 28235801, PMCID: PMC5399107, DOI: 10.1074/jbc.m116.770883.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAnimalsApoptosisBreast NeoplasmsCalciumCell Line, TumorCell MembraneCell ProliferationFemaleGene Expression ProfilingGene Expression Regulation, NeoplasticGene Knockdown TechniquesHSP90 Heat-Shock ProteinsHumansMiceMicroscopy, FluorescencePhosphoproteinsPlasma Membrane Calcium-Transporting ATPasesReceptor, ErbB-2RNA, MessengerSignal TransductionSodium-Hydrogen ExchangersConceptsBreast cancerHER2-positive breast cancerHER2-positive statusInvasive breast cancerHuman ductal carcinomaDegradation of HER2Normal mammary epithelial cellsMalignant breast cellsBreast cancer cellsErbB2/HER2Tyrosine kinase HER2Sodium-hydrogen exchanger regulatory factor-1Ductal carcinomaHER2 expressionExchanger regulatory factor 1Mammary epithelial cellsHER2Regulatory factor 1NHERF1 expressionBreast cellsEpithelial cellsCancerCancer cellsFactor 1PMCA2The role of interfacial lipids in stabilizing membrane protein oligomers
Gupta K, Donlan JAC, Hopper JTS, Uzdavinys P, Landreh M, Struwe WB, Drew D, Baldwin AJ, Stansfeld PJ, Robinson CV. The role of interfacial lipids in stabilizing membrane protein oligomers. Nature 2017, 541: 421-424. PMID: 28077870, PMCID: PMC5501331, DOI: 10.1038/nature20820.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsBinding SitesCardiolipinsCell MembraneEscherichia coliEscherichia coli ProteinsLigandsLipidsMass SpectrometryMembrane ProteinsModels, MolecularMolecular Dynamics SimulationMoritellaProtein MultimerizationProtein StabilityReceptors, G-Protein-CoupledSodium-Hydrogen ExchangersThermodynamicsThermus thermophilusIntegrating mass spectrometry with MD simulations reveals the role of lipids in Na+/H+ antiporters
Landreh M, Marklund EG, Uzdavinys P, Degiacomi MT, Coincon M, Gault J, Gupta K, Liko I, Benesch JL, Drew D, Robinson CV. Integrating mass spectrometry with MD simulations reveals the role of lipids in Na+/H+ antiporters. Nature Communications 2017, 8: 13993. PMID: 28071645, PMCID: PMC5234078, DOI: 10.1038/ncomms13993.Peer-Reviewed Original ResearchConceptsIon mobility mass spectrometryGas phaseMass spectrometryMobility mass spectrometryMolecular dynamics simulationsCatalysis rateMD simulationsLipid-binding propertiesDynamics simulationsConformational stabilityStable dimerLarge-scale conformational changesSecondary active transportersConformational changesSpectrometryAntiporter NhaAKingdoms of lifeAnnular lipidsNative foldProtein segmentsInter-domain contactsRole of lipidsThermus thermophilusMembrane lipidsNHA2
2016
Identification of intestinal ion transport defects in microvillus inclusion disease
Kravtsov DV, Ahsan MK, Kumari V, van Ijzendoorn SC, Reyes-Mugica M, Kumar A, Gujral T, Dudeja PK, Ameen NA. Identification of intestinal ion transport defects in microvillus inclusion disease. AJP Gastrointestinal And Liver Physiology 2016, 311: g142-g155. PMID: 27229121, PMCID: PMC4967175, DOI: 10.1152/ajpgi.00041.2016.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingCaco-2 CellsChloride-Bicarbonate AntiportersCystic Fibrosis Transmembrane Conductance RegulatorEnterocytesGene Expression RegulationHumansIon TransportJejunumMalabsorption SyndromesMembrane Transport ProteinsMicrovilliMucolipidosesMyosin Heavy ChainsMyosin Type VPhenotypePhosphoproteinsRNA InterferenceSignal TransductionSodium-Hydrogen Exchanger 3Sodium-Hydrogen ExchangersSulfate TransportersTranscription FactorsTransfectionYAP-Signaling ProteinsConceptsMicrovillus inclusion diseaseStool lossVillus atrophyInclusion diseaseEnterocyte maturationMicrovillus inclusionsIntestinal fluid transportIntestinal cell modelIon transport defectImmunohistochemical stainingSecretory diarrheaBrush border defectsImmature enterocytesC2BBe cellsT84 cellsElectrophysiological approachesCFTR ion transportBB membraneLoss of MYO5BEnterocytesFunctional CFTRDiarrheaAtrophyFunction mutationsCFTR localization
2015
Na+/H+ exchanger regulatory factor 1 knockout mice have an attenuated hepatic inflammatory response and are protected from cholestatic liver injury
Li M, Mennone A, Soroka CJ, Hagey LR, Ouyang X, Weinman EJ, Boyer JL. Na+/H+ exchanger regulatory factor 1 knockout mice have an attenuated hepatic inflammatory response and are protected from cholestatic liver injury. Hepatology 2015, 62: 1227-1236. PMID: 26108984, PMCID: PMC4589453, DOI: 10.1002/hep.27956.Peer-Reviewed Original ResearchConceptsBile duct ligationLiver injuryInflammatory responseICAM-1BDL miceBDL-induced liver injuryNeutrophil-mediated liver injuryTotal bile acid concentrationTumor necrosis factor alphaIntercellular adhesion molecule-1Hepatic neutrophil accumulationAttenuated liver injuryCholestatic liver injuryHepatic inflammatory responseMouse liverSerum alanine aminotransferaseBile acid concentrationsHepatic inflammatory diseasesICAM-1 expressionNecrosis factor alphaAdhesion molecule-1Wild-type miceICAM-1 proteinNew therapeutic targetsMessenger RNA levelsSpironolactone inhibits the activity of the Na+/H+ exchanger in the aorta of mineralocorticoid-induced hypertensive rats
Carreño JE, Verdugo FJ, Contreras F, Montellano FA, Veloso S, Schalper KA, Sandoval M, Villanueva S, Marusic E, Irarrazabal CE. Spironolactone inhibits the activity of the Na+/H+ exchanger in the aorta of mineralocorticoid-induced hypertensive rats. Journal Of The Renin-Angiotensin-Aldosterone System 2015, 16: 1225-1231. PMID: 25997821, DOI: 10.1177/1470320315587193.Peer-Reviewed Original ResearchConceptsNHE-1 activityMineralocorticoid receptor activationEthyl isopropyl amilorideVascular contractilityHypertensive ratsReceptor activationMale Sprague-Dawley ratsUninephrectomized male Sprague-Dawley ratsChronic DOCA treatmentDiastolic blood pressureAortic wall thicknessWeeks of treatmentVascular smooth muscle cellsProtein levelsSprague-Dawley ratsSmooth muscle cellsNHE-1 mRNADOCA treatmentBlood pressureDOCA administrationExchanger isoform 1Rat aortaDOCA groupSpironolactoneAortaRegulation of glomerulotubular balance. III. Implication of cytosolic calcium in flow-dependent proximal tubule transport
Du Z, Weinbaum S, Weinstein A, Wang T. Regulation of glomerulotubular balance. III. Implication of cytosolic calcium in flow-dependent proximal tubule transport. American Journal Of Physiology. Renal Physiology 2015, 308: f839-f847. PMID: 25651568, PMCID: PMC4398834, DOI: 10.1152/ajprenal.00601.2014.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBicarbonatesBiological TransportCalciumCalcium-Transporting ATPasesChelating AgentsCytosolEnzyme InhibitorsIn Vitro TechniquesInositol 1,4,5-Trisphosphate ReceptorsKidney Tubules, ProximalKineticsMice, Inbred C57BLPerfusionRenal ReabsorptionSodiumSodium-Hydrogen Exchanger 3Sodium-Hydrogen ExchangersConceptsNa/H exchanger 3Luminal Ca(2Flow-induced increaseCytosolic calciumProximal tubulesCa(2+) chelator BAPTA-AMAntagonist 2-aminoethoxydiphenyl borateCa-ATPase inhibitor thapsigarginProximal tubule transportNa(+) reabsorptionMicroperfused in vitroMouse proximal tubuleChelator BAPTA-AMH-ATPase activityNo effectControl tubulesInhibitor thapsigarginBAPTA-AMIntracellular Ca(2Decreased transportTubule transportBaseline transportStimulates Na(+Modulate Na(+Glomerulotubular balance
2014
Cyclic GMP Kinase II (cGKII) Inhibits NHE3 by Altering Its Trafficking and Phosphorylating NHE3 at Three Required Sites IDENTIFICATION OF A MULTIFUNCTIONAL PHOSPHORYLATION SITE*
Chen T, Kocinsky HS, Cha B, Murtazina R, Yang J, Tse CM, Singh V, Cole R, Aronson PS, de Jonge H, Sarker R, Donowitz M. Cyclic GMP Kinase II (cGKII) Inhibits NHE3 by Altering Its Trafficking and Phosphorylating NHE3 at Three Required Sites IDENTIFICATION OF A MULTIFUNCTIONAL PHOSPHORYLATION SITE*. Journal Of Biological Chemistry 2014, 290: 1952-1965. PMID: 25480791, PMCID: PMC4303652, DOI: 10.1074/jbc.m114.590174.Peer-Reviewed Original ResearchAnimalsBinding SitesCaco-2 CellsCell MembraneCyclic GMP-Dependent Protein Kinase Type IIDexamethasoneHumansIntestinal MucosaMass SpectrometryMiceMicrovilliMutagenesisPhosphorylationProtein Structure, TertiaryProtein TransportSerineSodium-Hydrogen Exchanger 3Sodium-Hydrogen ExchangersSurface PropertiesTransfection
2013
NHE Isoform Switching and KChIP2 Upregulation in Aging Porcine Atria
Kant R, Hu Z, Malhotra JK, Krogh-Madsen T, Christini DJ, Heerdt PM, Abbott GW. NHE Isoform Switching and KChIP2 Upregulation in Aging Porcine Atria. PLOS ONE 2013, 8: e82951. PMID: 24376615, PMCID: PMC3871617, DOI: 10.1371/journal.pone.0082951.Peer-Reviewed Original ResearchConceptsAtrial fibrillationMyocyte action potential durationHuman cardiac physiologyCessation of stimulationAction potential durationLarge animal modelSodium-hydrogen exchangerReperfusion arrhythmiasNHE1-specific inhibitorMyocardial responsivenessPharmacological responsivenessPharmacologic efficacyYoung adult pigsAtrial tissuePotential durationTherapeutic targetAnimal modelsCardiac pathologyKChIP2 expressionReal-time qPCRPotential molecular basisTherapeutic agentsCardiac physiologyFemale swineYoung adultsCharacterization of CFTR High Expresser cells in the intestine
Jakab RL, Collaco AM, Ameen NA. Characterization of CFTR High Expresser cells in the intestine. AJP Gastrointestinal And Liver Physiology 2013, 305: g453-g465. PMID: 23868408, PMCID: PMC3761243, DOI: 10.1152/ajpgi.00094.2013.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcholineAlkaline PhosphataseAnimalsCyclic AMPCystic Fibrosis Transmembrane Conductance RegulatorIntestinal MucosaIntestine, SmallMaleMicrovilliProtein TransportQa-SNARE ProteinsRatsRats, Sprague-DawleySodium-Hydrogen Exchanger 3Sodium-Hydrogen ExchangersSodium-Potassium-Exchanging ATPaseSolute Carrier Family 12, Member 2ConceptsCHE cellsNeighboring enterocytesVacuolar ATPase proton pumpCystic fibrosis transmembrane conductance regulator (CFTR) Cl(-) channelDouble-label immunofluorescence microscopyEightfold higher levelsBrush border membraneRegulatory factors NHERF1Crypt-villus axisCFTR abundanceSyntaxin 3Myosin-1aApical domainEffect of NSAIDs on Na+/H+ exchanger activity in rat colonic crypts
Roginiel AC, Kohut DL, Kaur S, Saleh AM, Weber T, Geibel P, Singh H, Geibel JP. Effect of NSAIDs on Na+/H+ exchanger activity in rat colonic crypts. American Journal Of Physiology - Cell Physiology 2013, 305: c512-c518. PMID: 23739181, DOI: 10.1152/ajpcell.00303.2012.Peer-Reviewed Original ResearchConceptsRat colonic cryptsExchanger activityNonsteroidal anti-inflammatory drugsUpper GI injuryColonic cryptsLower GI bleedingUse of NSAIDsChronic inflammatory stateLower GI tractUse of suppositoriesEffects of NSAIDsAnti-inflammatory drugsGI injuryNSAIDs aspirinGI bleedingPain reliefRheumatoid diseaseEpithelial erosionsInflammatory stateMyocardial infarctionChronic conditionsMucosal barrierUlcer formationColonic tissueGastrointestinal tractThe calcium sensing receptor modulates fluid reabsorption and acid secretion in the proximal tubule
Capasso G, Geibel PJ, Damiano S, Jaeger P, Richards WG, Geibel JP. The calcium sensing receptor modulates fluid reabsorption and acid secretion in the proximal tubule. Kidney International 2013, 84: 277-284. PMID: 23615500, DOI: 10.1038/ki.2013.137.Peer-Reviewed Original ResearchMeSH KeywordsAcid-Base EquilibriumAnimalsCalcimimetic AgentsCalciumHydrogen-Ion ConcentrationIn Vitro TechniquesKidney Tubules, ProximalMaleMiceMice, KnockoutNuclear ProteinsPerfusionPuncturesRatsRats, Sprague-DawleyReceptors, Calcium-SensingReceptors, G-Protein-CoupledSodium-Hydrogen ExchangersTranscription FactorsConceptsProximal tubulesLuminal calcium concentrationFluid reabsorptionAcid secretionKnockout miceCalcium ion concentrationCalcium concentrationRole of CaSRActivation of CaSRCalcium sensing receptorCalcium-sensing receptorMouse proximal tubulesProton secretionSodium-hydrogen exchangerCalcimimetic agentBicarbonate absorptionSensing receptorCaSRFluid absorptionSecretionReabsorptionMiceCalcimimeticsTubulesLuminal membraneProximal tubule specific knockout of the Na+/H+ exchanger NHE3: effects on bicarbonate absorption and ammonium excretion
Li H, Du Z, Barone S, Rubera I, McDonough A, Tauc M, Zahedi K, Wang T, Soleimani M. Proximal tubule specific knockout of the Na+/H+ exchanger NHE3: effects on bicarbonate absorption and ammonium excretion. Journal Of Molecular Medicine 2013, 91: 951-963. PMID: 23508938, PMCID: PMC3730089, DOI: 10.1007/s00109-013-1015-3.Peer-Reviewed Original ResearchConceptsNa+/H+ exchanger NHE3Proximal convoluted tubulesKO miceMetabolic acidosisBicarbonate reabsorptionDays of acid loadingIsolated proximal convoluted tubulesConvoluted tubulesIn vitro microperfusion studyCompared to WT miceNHE3 knockout miceProximal tubule NHE3Acid loadNH4Cl acid loadMild metabolic acidosisWT miceNHE3Microperfusion studiesKnockout miceBicarbonate absorptionMutant miceVolume reabsorptionFloxed miceNH4Cl loadingTransgenic miceEzrin Is Required for the Functional Regulation of the Epithelial Sodium Proton Exchanger, NHE3
Hayashi H, Tamura A, Krishnan D, Tsukita S, Suzuki Y, Kocinsky HS, Aronson PS, Orlowski J, Grinstein S, Alexander RT. Ezrin Is Required for the Functional Regulation of the Epithelial Sodium Proton Exchanger, NHE3. PLOS ONE 2013, 8: e55623. PMID: 23405179, PMCID: PMC3566197, DOI: 10.1371/journal.pone.0055623.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonAnimalsColonCyclic AMPCytoskeletal ProteinsDogsEpithelial CellsFluorescence Recovery After PhotobleachingHumansMadin Darby Canine Kidney CellsMaleMembrane ProteinsMiceMice, KnockoutMicrofilament ProteinsMicrovilliOctoxynolPhosphorylationProtein TransportRNA, Small InterferingSodiumSodium-Hydrogen Exchanger 3Sodium-Hydrogen ExchangersConceptsApical actin cytoskeletonNHE3 activitySodium hydrogen exchanger isoform 3CAMP-dependent inhibitionEzrin knockdown miceERM proteinsActin cytoskeletonSodium-proton exchangerApical cytoskeletonApical localizationFunctional regulationWild-type animalsEpithelial cell culture modelEzrinProton exchangersFluorescent recoveryEpithelial phenotypeCytoskeletonMolecular determinantsCell culture modelExchanger isoform 3Functional studiesNon-targeting siRNAApical membraneIsoform 3
2012
Regulation of glomerulotubular balance. II. Impact of angiotensin II on flow-dependent transport
Du Z, Wan L, Yan Q, Weinbaum S, Weinstein A, Wang T. Regulation of glomerulotubular balance. II. Impact of angiotensin II on flow-dependent transport. American Journal Of Physiology. Renal Physiology 2012, 303: f1507-f1516. PMID: 22952281, PMCID: PMC3532483, DOI: 10.1152/ajprenal.00277.2012.Peer-Reviewed Original ResearchMeSH KeywordsAngiotensin IIAngiotensin II Type 1 Receptor BlockersAnimalsBicarbonatesBiological TransportEnzyme InhibitorsFemaleHemostasisIn Vitro TechniquesKidney GlomerulusKidney TubulesLosartanMacrolidesMiceMice, KnockoutModels, AnimalProton-Translocating ATPasesReceptor, Angiotensin, Type 1SodiumSodium-Hydrogen Exchanger 3Sodium-Hydrogen ExchangersConceptsNa(+)-H(+) exchanger 3Mouse tubulesImpact of angiotensin IIH-ATPaseMicroperfused in vitroAT(2) receptorsAT(1A) receptorFlow-mediated changesH-ATPase activityParacellular Cl(-Receptor availabilityAngiotensin IIAT(1ARegulate Na(+Increased Na(+Local angiotensinBasolateral transportJ(HCO3Mouse kidneyNet fluidInhibitor bafilomycinProtein levelsMiceReceptorsTubules
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