2016
N-glycosylation critically regulates function of oxalate transporter SLC26A6
Thomson RB, Thomson CL, Aronson PS. N-glycosylation critically regulates function of oxalate transporter SLC26A6. American Journal Of Physiology - Cell Physiology 2016, 311: c866-c873. PMID: 27681177, PMCID: PMC5206297, DOI: 10.1152/ajpcell.00171.2016.Peer-Reviewed Original ResearchConceptsPlasma membraneIntegral membrane proteinsCell surface deliverySLC26A6 functionTissue-specific differencesGlycosylation mutantsMembrane proteinsN-glycosylationSurface deliveryBiotinylation studiesOxalate transporterOxalate homeostasisSecond extracellular loopExtracellular loopIntact cellsEnzymatic deglycosylation studiesTransport activityEnzymatic deglycosylationFunctional studiesDeglycosylation studiesGlycosylationPutative second extracellular loopTransport functionFunctional significanceEssential role
2007
Characterization of Na+/H+ exchanger NHE8 in cultured renal epithelial cells
Zhang J, Bobulescu IA, Goyal S, Aronson PS, Baum MG, Moe OW. Characterization of Na+/H+ exchanger NHE8 in cultured renal epithelial cells. American Journal Of Physiology. Renal Physiology 2007, 293: f761-f766. PMID: 17581925, PMCID: PMC2861566, DOI: 10.1152/ajprenal.00117.2007.Peer-Reviewed Original ResearchConceptsNRK cellsBasolateral NHE activityNHE8 proteinApical membraneNHE1 protein levelsPrimary amino acid sequenceAmino acid sequenceProtein levelsProtein expressionNHE8 protein expressionBasolateral membraneCultured renal epithelial cellsRenal epithelial cellsMammalian cellsNHE activityFunctional characterizationPlasma membraneAcid sequenceRenal cell linesNHE1 protein expressionNative environmentImmunoelectron microscopyExchange activityCell linesNHE8
2006
The life-extending gene Indy encodes an exchanger for Krebs-cycle intermediates
Knauf F, Mohebbi N, Teichert C, Herold D, Rogina B, Helfand S, Gollasch M, Luft FC, Aronson PS. The life-extending gene Indy encodes an exchanger for Krebs-cycle intermediates. Biochemical Journal 2006, 397: 25-29. PMID: 16608441, PMCID: PMC1479758, DOI: 10.1042/bj20060409.Peer-Reviewed Original ResearchConceptsExternal citrateKrebs cycle intermediatesXenopus oocytesSodium dicarboxylate cotransporterMammalian genesDrosophila melanogasterIndy mutantsLifespan extensionLongevity genesPlasma membraneSubstrate effluxExternal mediumSpecific transport mechanismsFunctional studiesSuccinate uptakeAddition of succinateEnergy metabolismIndyTransportable substratesGenesOocytesEffluxMelanogasterMutantsSuccinate
2002
Functional characterization and immunolocalization of the transporter encoded by the life-extending gene Indy
Knauf F, Rogina B, Jiang Z, Aronson PS, Helfand SL. Functional characterization and immunolocalization of the transporter encoded by the life-extending gene Indy. Proceedings Of The National Academy Of Sciences Of The United States Of America 2002, 99: 14315-14319. PMID: 12391301, PMCID: PMC137881, DOI: 10.1073/pnas.222531899.Peer-Reviewed Original ResearchConceptsPlasma membraneLife-extending mutationsNew longevity genesIntermediary metabolismAdult fat bodyIndy expressionCitric acid cycleLife-extending effectsMetabolite transportersVariety of speciesLongevity genesFunctional characterizationLife spanMidgut cellsFat bodyAcid cycleFunctional studiesXenopus oocytesTransport functionIndyBasolateral regionSodium-independent mechanismProminent expressionAverage life spanTransporters
1998
Membrane Topology of NHE3 EPITOPES WITHIN THE CARBOXYL-TERMINAL HYDROPHILIC DOMAIN ARE EXOPLASMIC*
Biemesderfer D, DeGray B, Aronson P. Membrane Topology of NHE3 EPITOPES WITHIN THE CARBOXYL-TERMINAL HYDROPHILIC DOMAIN ARE EXOPLASMIC*. Journal Of Biological Chemistry 1998, 273: 12391-12396. PMID: 9575193, DOI: 10.1074/jbc.273.20.12391.Peer-Reviewed Original ResearchConceptsExchanger Isoform NHE3Membrane vesiclesAbsence of detergentPlasma membraneBorder membrane vesiclesCarboxyl-terminal hydrophilic domainBrush border membrane vesiclesCarboxyl-terminal domainMembrane topologyCytoskeletal effectorsCarboxyl terminusHigh-resolution immunocytochemistryExoplasmic surfaceCytoplasmic surfaceImmunoprecipitation studiesTransporter activityAmino acidsUltrathin cryosectionsImmunoblot analysisMembrane orientationHydrophilic domainsVesiclesMonoclonal antibodiesIntact microvilliGold technique
1997
Sodium/Hydrogen Exchanger Gene Defect in Slow-Wave Epilepsy Mutant Mice
Cox G, Lutz C, Yang C, Biemesderfer D, Bronson R, Fu A, Aronson P, Noebels J, Frankel W. Sodium/Hydrogen Exchanger Gene Defect in Slow-Wave Epilepsy Mutant Mice. Cell 1997, 91: 139-148. PMID: 9335342, DOI: 10.1016/s0092-8674(01)80016-7.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAtaxiaBrain ChemistryCell LineCerebellumCerebral CortexChromosome MappingCrosses, GeneticElectroencephalographyEpilepsyFibroblastsGenes, RecessiveIon TransportMiceMice, Inbred C57BLMice, Neurologic MutantsOrgan SpecificityPhenotypePoint MutationRNASodiumSodium-Hydrogen ExchangersConceptsSodium/hydrogen exchangerSpontaneous mouse mutantDisease-causing mutationsPlasma membraneChromosome 4Null allelesMouse mutantsCell survivalHydrogen exchangerNHE genesMutantsGene defectsMutant miceNHE1Growth factorTonic-clonic seizuresSelective neuronal deathNeuronal deathDelicate balanceNeurological syndromeEpilepsy phenotypeGenesNew toolCell volumeMutations
1992
cDNA cloning and localization of a band 3-related protein from ileum
Chow A, Dobbins JW, Aronson PS, Igarashi P. cDNA cloning and localization of a band 3-related protein from ileum. American Journal Of Physiology 1992, 263: g345-g352. PMID: 1415547, DOI: 10.1152/ajpgi.1992.263.3.g345.Peer-Reviewed Original ResearchConceptsRabbit ileal enterocytesDeduced amino acid sequenceBand 3Anion exchanger familyAmino acid sequenceAE gene familyBrush border membraneGene familyNonerythroid tissuesHCO3- exchangerErythroid band 3CDNA cloningPlasma membraneAcid sequenceExchanger familyRelated proteinsMembrane vesiclesIleal enterocytesMolecular identityCytoplasmic fragmentsProteinBasolateral membrane vesiclesBasolateral membraneMembraneEnterocytes
1991
High affinity binding of amiloride analogs at an internal site in renal microvillus membrane vesicles
Desir GV, Cragoe EJ, Aronson PS. High affinity binding of amiloride analogs at an internal site in renal microvillus membrane vesicles. Journal Of Biological Chemistry 1991, 266: 2267-2271. PMID: 1846621, DOI: 10.1016/s0021-9258(18)52238-9.Peer-Reviewed Original ResearchConceptsMembrane vesiclesMicrovillus membrane vesiclesRenal microvillus membrane vesiclesSimilar rank order potencyBinding sitesInternal sitesHigh-affinity inhibitorsMembrane localizationInternal binding siteAmiloride analoguesPlasma membraneRank order potencyHigh-affinity bindingAffinity inhibitorsHigh affinity-binding siteVesiclesBasolateral membrane vesiclesOrder potency
1985
The plasma membrane sodium-hydrogen exchanger and its role in physiological and pathophysiological processes.
Mahnensmith RL, Aronson PS. The plasma membrane sodium-hydrogen exchanger and its role in physiological and pathophysiological processes. Circulation Research 1985, 56: 773-788. PMID: 2988813, DOI: 10.1161/01.res.56.6.773.Commentaries, Editorials and LettersMeSH KeywordsAcid-Base EquilibriumAnimalsBiological Transport, ActiveBlood PlateletsCalciumCarrier ProteinsCations, MonovalentCell MembraneEpitheliumHormonesHumansHydrogenHydrogen-Ion ConcentrationHypertensionLeukocytesMembrane ProteinsNeoplasmsSodiumSodium-Hydrogen ExchangersSodium-Potassium-Exchanging ATPaseWater-Electrolyte BalanceConceptsSodium-hydrogen exchangerCellular acid-base homeostasisAllosteric regulationPlasma membraneRegulation of intracellularStimulus-response couplingIntracellular protonsPathophysiological processesPhysiological roleTransport systemTransmembrane exchangeCell growthAcid-base homeostasisRegulationSodium-hydrogen exchangeKinetic propertiesSuch diverse conditionsMetabolic responsePathophysiological roleDiverse conditionsCellsCell volumeRoleHomeostasisIntracellular