2018
Acid Stimulation of the Citrate Transporter NaDC-1 Requires Pyk2 and ERK1/2 Signaling Pathways
Zacchia M, Tian X, Zona E, Alpern RJ, Preisig PA. Acid Stimulation of the Citrate Transporter NaDC-1 Requires Pyk2 and ERK1/2 Signaling Pathways. Journal Of The American Society Of Nephrology 2018, 29: 1720-1730. PMID: 29678998, PMCID: PMC6054333, DOI: 10.1681/asn.2017121268.Peer-Reviewed Original ResearchMeSH KeywordsAcidsAmmonium ChlorideAnimalsCells, CulturedCitric AcidCSK Tyrosine-Protein KinaseDicarboxylic Acid TransportersEndothelin-1Epithelial CellsFocal Adhesion Kinase 2Kidney Tubules, ProximalMAP Kinase Signaling SystemMiceMice, KnockoutMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3OpossumsOrganic Anion Transporters, Sodium-DependentPhosphorylationProto-Oncogene Proteins c-rafReceptor, Endothelin BRibosomal Protein S6 Kinases, 90-kDasrc-Family KinasesTransfectionConceptsET-1/ETEndothelin-1Proximal tubulesCultured opossum kidney cellsAcid stimulationInhibition of Pyk2ET-1 stimulationRenal proximal tubulesNaDC-1Opossum kidney cellsCl loadingC-SrcPhosphorylation of Raf1Urine citratePyk2 knockdownEnd pointAcid loadApical NaERK1/2 pathwayStimulationMiceKidney cellsKidneyPyk2ERK1/2
2011
Chloride Channel (Clc)-5 Is Necessary for Exocytic Trafficking of Na+/H+ Exchanger 3 (NHE3)*
Lin Z, Jin S, Duan X, Wang T, Martini S, Hulamm P, Cha B, Hubbard A, Donowitz M, Guggino SE. Chloride Channel (Clc)-5 Is Necessary for Exocytic Trafficking of Na+/H+ Exchanger 3 (NHE3)*. Journal Of Biological Chemistry 2011, 286: 22833-22845. PMID: 21561868, PMCID: PMC3123051, DOI: 10.1074/jbc.m111.224998.Peer-Reviewed Original ResearchConceptsKO miceTrafficking of NHE3Proximal tubulesOpossum kidney cellsNHE3 activityDent's diseaseClC-5Surface expressionNHE3 surface expressionKidney cellsRenal proximal tubulesTotal protein levelsChloride/proton exchangerRates of basalReduced surface expressionKnockdown cellsParathyroid hormoneWT miceDegree of inhibitionCLCN5 geneSurface NHE3MiceTubule perfusionReduced expressionTwo-photon microscopy
2010
Acute Down-regulation of Sodium-dependent Phosphate Transporter NPT2a Involves Predominantly the cAMP/PKA Pathway as Revealed by Signaling-selective Parathyroid Hormone Analogs
Nagai S, Okazaki M, Segawa H, Bergwitz C, Dean T, Potts JT, Mahon MJ, Gardella TJ, Jüppner H. Acute Down-regulation of Sodium-dependent Phosphate Transporter NPT2a Involves Predominantly the cAMP/PKA Pathway as Revealed by Signaling-selective Parathyroid Hormone Analogs. Journal Of Biological Chemistry 2010, 286: 1618-1626. PMID: 21047792, PMCID: PMC3020770, DOI: 10.1074/jbc.m110.198416.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCattleChlorocebus aethiopsCOS CellsCyclic AMPCyclic AMP-Dependent Protein KinasesDown-RegulationHumansIn Vitro TechniquesKidney Tubules, ProximalMaleMiceMice, Inbred C57BLOpossumsOsteoblastsParathyroid HormonePhosphorusPseudohypoparathyroidismRatsSignal TransductionSodiumSodium-Phosphate Cotransporter Proteins, Type IIaConceptsAcute down-regulationNpt2a expressionParathyroid hormoneRenal proximal tubule cellsParathyroid hormone (PTH)/PTH-related peptideCAMP/PKALong-acting PTH analogPTH analogsWild-type miceRenal proximal tubulesIntracellular calcium responsesParathyroid hormone analogProximal tubule cellsOpossum kidney cellsM-PTH(1Prolonged cAMP responsesParathyroid hormone analoguesCAMP/PKA signaling pathwayPTH-dependent regulationRenal brush border membraneClonal cell linesInducing IP(3Pseudohypoparathyroid patientsMembrane expressionCalcium response
2007
NHE3 phosphorylation at serines 552 and 605 does not directly affect NHE3 activity
Kocinsky HS, Dynia DW, Wang T, Aronson PS. NHE3 phosphorylation at serines 552 and 605 does not directly affect NHE3 activity. American Journal Of Physiology. Renal Physiology 2007, 293: f212-f218. PMID: 17409282, DOI: 10.1152/ajprenal.00042.2007.Peer-Reviewed Original ResearchMeSH Keywords1-Methyl-3-isobutylxanthineAnimalsCells, CulturedColforsinCyclic AMP-Dependent Protein KinasesElectrophoresis, Polyacrylamide GelKidneyKidney Tubules, ProximalMaleMicrovilliParathyroid HormonePhosphodiesterase InhibitorsPhosphorylationRatsRats, Sprague-DawleySerineSodiumSodium RadioisotopesSodium-Hydrogen Exchanger 3Sodium-Hydrogen ExchangersStimulation, ChemicalConceptsSerine 552NHE3 phosphorylationNHE3 activityMicrovillar membrane vesiclesPhosphorylation of NHE3Direct phosphorylationPhosphospecific antibodiesSprague-Dawley ratsExchanger type 3PKA activationMembrane vesiclesSite-specific changesPhosphorylationTransport activityOpossum kidney cellsParathyroid hormoneIntravenous infusionRat modelExchange activityKidney cellsOKP cellsNHE3 inhibitionPKACell modelExact role
2005
Use of phospho-specific antibodies to determine the phosphorylation of endogenous Na+/H+ exchanger NHE3 at PKA consensus sites
Kocinsky HS, Girardi AC, Biemesderfer D, Nguyen T, Mentone S, Orlowski J, Aronson PS. Use of phospho-specific antibodies to determine the phosphorylation of endogenous Na+/H+ exchanger NHE3 at PKA consensus sites. American Journal Of Physiology. Renal Physiology 2005, 289: f249-f258. PMID: 15687252, DOI: 10.1152/ajprenal.00082.2004.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodiesAntibodies, MonoclonalAntibody SpecificityCell LineChlorocebus aethiopsCOS CellsCyclic AMP-Dependent Protein KinasesDopamineElectrophoresis, Polyacrylamide GelImmunohistochemistryKidneyMaleMiceMice, Inbred BALB CMicroscopy, FluorescenceMicrovilliOpossumsPhosphorylationRatsRats, Sprague-DawleySodiumSodium-Hydrogen Exchanger 3Sodium-Hydrogen ExchangersSubcellular FractionsTransfectionConceptsSerine 552Total NHE3Brush border membranePKA consensus sitesEffects of dopamineProximal tubule cellsWestern blot assaysOpossum kidney cellsBaseline phosphorylationPeptide antibodiesInhibition of NHE3Tubule cellsBlot assaysAntibodiesPhosphorylation of NHE3Phosphospecific antibodiesExchanger NHE3NHE3DopamineEndogenous NHE3Kidney cellsVivoPhospho-specific antibodiesTransfection studiesVitro
1999
Glucocorticoids enhance acid activation of the Na+/H+ exchanger 3 (NHE3)
Ambühl P, Yang X, Peng Y, Preisig P, Moe O, Alpern R. Glucocorticoids enhance acid activation of the Na+/H+ exchanger 3 (NHE3). Journal Of Clinical Investigation 1999, 103: 429-435. PMID: 9927505, PMCID: PMC407891, DOI: 10.1172/jci2913.Peer-Reviewed Original ResearchConceptsNHE3 protein abundanceM hydrocortisoneNHE3 activityAcid incubationNHE3 mRNA abundanceTrafficking of NHE3Absence of hydrocortisoneOpossum kidney cellsExogenous glucocorticoidsExchanger 3 (NHE3) activityHydrocortisoneProtein abundanceGlucocorticoidsProtein synthesisExchanger 3Kidney cellsTwofold increaseMRNA abundanceApical membrane
1994
Angiotensin II stimulation of Na-H antiporter activity is cAMP independent in OKP cells
Cano A, Miller RT, Alpern RJ, Preisig PA. Angiotensin II stimulation of Na-H antiporter activity is cAMP independent in OKP cells. American Journal Of Physiology 1994, 266: c1603-c1608. PMID: 8023891, DOI: 10.1152/ajpcell.1994.266.6.c1603.Peer-Reviewed Original ResearchConceptsPertussis toxin-sensitive G proteinToxin-sensitive G proteinNa-H antiporter activityAngiotensin IINa-H antiporterOKP cellsAngiotensin II concentrationAngiotensin II receptorsAbsence of IBMXAngiotensin II stimulationG proteinsCyclic monophosphateProximal tubule apical membraneOpossum kidney cellsConcentration-dependent mannerCAMP-independent mechanismM losartanAcute treatmentAT1 receptorII stimulationPertussis toxinII receptorsProximal tubulesCAMP productionStimulatory effect
1993
Chronic regulation of the Na/H antiporter.
Alpern RJ, Yamaji Y, Cano A, Horie S, Miller RT, Moe OW, Preisig PA. Chronic regulation of the Na/H antiporter. Translational Research 1993, 122: 137-40. PMID: 8393472.Peer-Reviewed Original ResearchConceptsNa/H antiporter activityNa/H antiporterChronic regulationH antiporterAcute inhibitory effectRabbit proximal tubule cellsAcid-induced increaseProximal tubule cellsOpossum kidney cellsMRNA abundanceProtein kinase AChronic decreaseAntiporter activityChronic studiesChronic activationTubule cellsImmediate early genesIntact animalsKinase AInhibitory effectProtein synthesisNonrenal cellsPrimary culturesC-fosExtracellular fluid
1991
Specific, high-affinity binding sites for angiotensin II on Mycoplasma hyorhinis
Bergwitz C, Madoff S, Abou-Samra A, Ju¨ppner H. Specific, high-affinity binding sites for angiotensin II on Mycoplasma hyorhinis. Biochemical And Biophysical Research Communications 1991, 179: 1391-1399. PMID: 1718269, DOI: 10.1016/0006-291x(91)91727-t.Peer-Reviewed Original ResearchConceptsAngiotensin II receptorsAngiotensin IIII receptorsHigh-affinity binding sitesAngiotensin II bindingOpossum kidney cellsCGP 42112ADuP 753Angiotensin IIIStrains of Mycoplasma hyorhinisAngiotensin IHuman angiotensin IIM. hominisHigh affinityKidney cellsBinding sitesII bindingMycoplasma hyorhinisSpecific bindingReceptorsStrains of M. hominisAntagonist DuP 753Fold decreaseSensitive to bacitracin
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