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
2013
Overexpression of Pendrin in Intercalated Cells Produces Chloride-Sensitive Hypertension
Jacques T, Picard N, Miller RL, Riemondy KA, Houillier P, Sohet F, Ramakrishnan SK, Büsst CJ, Jayat M, Cornière N, Hassan H, Aronson PS, Hennings JC, Hübner CA, Nelson RD, Chambrey R, Eladari D. Overexpression of Pendrin in Intercalated Cells Produces Chloride-Sensitive Hypertension. Journal Of The American Society Of Nephrology 2013, 24: 1104-1113. PMID: 23766534, PMCID: PMC3699825, DOI: 10.1681/asn.2012080787.Peer-Reviewed Original ResearchConceptsDistal nephronTransgenic miceSame sodium intakeHigh salt intakeCause of hypertensionHigh-salt dietSodium-driven chloride/bicarbonate exchangerNet NaCl absorptionArterial hypertensionSalt intakeSodium intakeEpithelial sodium channel ENaCPathogenic roleNormal miceHypertensionRenal absorptionExchanger pendrinPrimary abnormalityVascular volumeAppropriate downregulationIntercalated cellsChloride absorptionSodium channel ENaCActivity of transportersPrimary activation
2011
Cholinergic signaling inhibits oxalate transport by human intestinal T84 cells
Hassan HA, Cheng M, Aronson PS. Cholinergic signaling inhibits oxalate transport by human intestinal T84 cells. American Journal Of Physiology - Cell Physiology 2011, 302: c46-c58. PMID: 21956166, PMCID: PMC3328906, DOI: 10.1152/ajpcell.00075.2011.Peer-Reviewed Original ResearchConceptsC-SrcT84 cellsHuman intestinal cell line T84PKC-δ inhibitor rottlerinSrc inhibitor PP2Intestinal cell line T84Human intestinal T84 cellsSurface expressionMuscarinic receptorsRegulation downstreamInhibitor PP2Phosphorylation studiesBiotinylation studiesInhibitor rottlerinKnockdown studiesPharmacological inhibitorsIntestinal T84 cellsIntestinal oxalate secretionPhospholipase CIntestinal ion transportPKC activationSignificant translocationCalcium oxalate urolithiasisPKCAnion exchanger SLC26A6
2010
Role of SLC26A6-mediated Cl⁻-oxalate exchange in renal physiology and pathophysiology.
Aronson PS. Role of SLC26A6-mediated Cl⁻-oxalate exchange in renal physiology and pathophysiology. Journal Of Nephrology 2010, 23 Suppl 16: s158-64. PMID: 21170874.Commentaries, Editorials and LettersMeSH KeywordsAnimalsChloridesHomeostasisHumansKidney Tubules, ProximalMembrane Transport ProteinsMiceOxalatesSulfate TransportersUrolithiasisConceptsNull miceCalcium oxalate urolithiasisProximal tubule cellsStone riskAnimal modelsOxalate urolithiasisProximal tubulesOxalate homeostasisTubule cellsApical membrane ClHyperoxaluriaRenal physiologyOxalate exchangeMiceExchange activitySubsequent studiesAnion transportersPossible mechanismHyperoxalemiaPatientsPathophysiologyUrolithiasisStriking phenotypeReabsorption
2008
Phenotypic and Functional Analysis of Human SLC26A6 Variants in Patients With Familial Hyperoxaluria and Calcium Oxalate Nephrolithiasis
Monico CG, Weinstein A, Jiang Z, Rohlinger AL, Cogal AG, Bjornson BB, Olson JB, Bergstralh EJ, Milliner DS, Aronson PS. Phenotypic and Functional Analysis of Human SLC26A6 Variants in Patients With Familial Hyperoxaluria and Calcium Oxalate Nephrolithiasis. American Journal Of Kidney Diseases 2008, 52: 1096-1103. PMID: 18951670, PMCID: PMC2710965, DOI: 10.1053/j.ajkd.2008.07.041.Peer-Reviewed Original ResearchConceptsPrimary hyperoxaluria type 1Oxalate transportMajor risk factorCalcium oxalate nephrolithiasisUrine oxalate levelsCalcium oxalate urolithiasisRare variantsHyperoxaluria type 1Calcium oxalate stonesAdditional missense variantsUrine oxalateOxalate excretionRisk factorsOxalate nephrolithiasisOxalate urolithiasisHyperoxaluriaAbstractTextAdult subjectsType 1Oxalate stonesPotential modifiersStudy designOxalate levelsGood healthMissense variants
2007
Specificity and Regulation of Renal Sulfate Transporters
Markovich D, Aronson PS. Specificity and Regulation of Renal Sulfate Transporters. Annual Review Of Physiology 2007, 69: 361-375. PMID: 17002596, DOI: 10.1146/annurev.physiol.69.040705.141319.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsMeSH KeywordsAnimalsCation Transport ProteinsHumansMembrane Transport ProteinsSodium Sulfate CotransporterSulfate TransportersSymportersConceptsProximal tubulesSulfate reabsorptionProximal tubular cellsRenal expressionApical membraneKnockout mouse studiesTubular cellsNet reabsorptionNaCl reabsorptionMouse studiesMajor roleReabsorptionSulfate homeostasisCFEXKidneyFamily membersPhysiological roleCurrent dataNormal cellular functionBasolateral membraneTubulesSLC26 family members
2004
WNK4 regulates apical and basolateral Cl– flux in extrarenal epithelia
Kahle KT, Gimenez I, Hassan H, Wilson FH, Wong RD, Forbush B, Aronson PS, Lifton RP. WNK4 regulates apical and basolateral Cl– flux in extrarenal epithelia. Proceedings Of The National Academy Of Sciences Of The United States Of America 2004, 101: 2064-2069. PMID: 14769928, PMCID: PMC357052, DOI: 10.1073/pnas.0308434100.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, WesternCarrier ProteinsCell PolarityChloridesEpitheliumHumansImmunohistochemistryIon TransportKidneyMembrane ProteinsMembrane Transport ProteinsMiceOocytesProtein Serine-Threonine KinasesRNA, MessengerSodium-Potassium-Chloride SymportersSolute Carrier Family 12, Member 2Sulfate TransportersXenopus laevisConceptsCl fluxBlood-brain barrierUnrelated ion channelsActivity of mediatorsWNK4 mRNABile ductPancreatic ductExtrarenal expressionExtrarenal tissuesCl(-) handlingPseudohypoaldosteronism type IIChannel ROMKNaCl reabsorptionSerine-threonine kinase WNK4Specialized endotheliumExchanger SLC26A6NaCl cotransporterWNK4 effectsColonic cryptsEpitheliumVariable inhibitionSweat ductsTight junctionsKidneyElectrolyte flux
2002
Regulation of the expression of the Cl-/anion exchanger pendrin in mouse kidney by acid-base status
Wagner CA, Finberg KE, Stehberger PA, Lifton RP, Giebisch GH, Aronson PS, Geibel JP. Regulation of the expression of the Cl-/anion exchanger pendrin in mouse kidney by acid-base status. Kidney International 2002, 62: 2109-2117. PMID: 12427135, DOI: 10.1046/j.1523-1755.2002.00671.x.Peer-Reviewed Original ResearchConceptsPendrin-positive cellsAcid-base statusPositive cellsBicarbonate secretionMouse kidneyAcid-base transportKnockout mouse modelProtein expression levelsMetabolic alkalosisDeficient dietExchanger pendrinPendrin expressionMouse modelSensorineural deafnessThyroid glandBicarbonate loadPendred syndromeWestern blottingApical membraneInner earPendrin proteinControl levelsKidneyPendrinProtein levelsFormate-stimulated NaCl absorption in the proximal tubule is independent of the pendrin protein
Karniski LP, Wang T, Everett LA, Green ED, Giebisch G, Aronson PS. Formate-stimulated NaCl absorption in the proximal tubule is independent of the pendrin protein. American Journal Of Physiology. Renal Physiology 2002, 283: f952-f956. PMID: 12372770, DOI: 10.1152/ajprenal.00182.2002.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiological TransportCarrier ProteinsFemaleFormatesHemostaticsKidney Tubules, ProximalMaleMembrane Transport ProteinsMiceMice, KnockoutMicrovilliSodium ChlorideSulfate TransportersConceptsProximal tubulesChloride/formate exchangeNaCl reabsorptionChloride reabsorptionElectroneutral NaCl reabsorptionNaCl absorptionRole of pendrinFormate exchangePds-knockout mouseRecycling of formatePendrin proteinReabsorptionMicePendrinBrush border membrane vesiclesTubulesPresent studyChloride transportApical membrane