2014
Kir1.1 (ROMK) and Kv7.1 (KCNQ1/KvLQT1) are essential for normal gastric acid secretion: importance of functional Kir1.1
Vucic E, Alfadda T, MacGregor GG, Dong K, Wang T, Geibel JP. Kir1.1 (ROMK) and Kv7.1 (KCNQ1/KvLQT1) are essential for normal gastric acid secretion: importance of functional Kir1.1. Pflügers Archiv - European Journal Of Physiology 2014, 467: 1457-1468. PMID: 25127675, DOI: 10.1007/s00424-014-1593-0.Peer-Reviewed Original ResearchConceptsGastric parietal cellsPotassium channelsParietal cellsΒ-subunitKir1.1 channelsWild-type miceSecretagogue-stimulated gastric acid secretionApical poleGastric glandsLeak pathwayPotential therapeutic targetKir1.1Proton secretionRegulatory characteristicsKv7.1Therapeutic targetATPaseCell numberParietal cell numberCellsNormal gastric acid secretionSecretionInhibitorsAcid secretionMice
2013
The 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 membrane
2008
Mouse model of type II Bartter's syndrome. II. Altered expression of renal sodium- and water-transporting proteins
Wagner CA, Loffing-Cueni D, Yan Q, Schulz N, Fakitsas P, Carrel M, Wang T, Verrey F, Geibel JP, Giebisch G, Hebert SC, Loffing J. Mouse model of type II Bartter's syndrome. II. Altered expression of renal sodium- and water-transporting proteins. American Journal Of Physiology. Renal Physiology 2008, 294: f1373-f1380. PMID: 18322017, DOI: 10.1152/ajprenal.00613.2007.Peer-Reviewed Original ResearchMeSH KeywordsAdaptation, PhysiologicalAnimalsBartter SyndromeCarrier ProteinsCation Transport ProteinsDinoprostoneDisease Models, AnimalEpithelial Sodium ChannelsKidney Tubules, DistalKidney Tubules, ProximalLoop of HenleMiceMice, Mutant StrainsPotassium Channels, Inwardly RectifyingReverse Transcriptase Polymerase Chain ReactionSodiumSodium-Hydrogen Exchanger 3Sodium-Hydrogen ExchangersSodium-Phosphate Cotransporter Proteins, Type IIaSodium-Potassium-Chloride SymportersSolute Carrier Family 12, Member 1Up-RegulationWaterConceptsThick ascending limbBartter's syndromeBartter-like phenotypeType II Bartter's syndromeWild-type miceAntenatal Bartter syndromeWild-type littermatesROMK null micePlasma aldosteroneMaternal polyhydramniosRenal sodiumVolume depletionRenal tubulopathyMouse modelSemiquantitative immunoblottingProximal tubulesAscending limbKidney homogenatesSyndromeHenle's loopNull miceDCT cellsWater transport proteinsCompensatory mechanismsMice
2005
The B1-subunit of the H+ ATPase is required for maximal urinary acidification
Finberg KE, Wagner CA, Bailey MA, Păunescu T, Breton S, Brown D, Giebisch G, Geibel JP, Lifton RP. The B1-subunit of the H+ ATPase is required for maximal urinary acidification. Proceedings Of The National Academy Of Sciences Of The United States Of America 2005, 102: 13616-13621. PMID: 16174750, PMCID: PMC1224669, DOI: 10.1073/pnas.0506769102.Peer-Reviewed Original ResearchConceptsMaximal urinary acidificationNormal urinary acidificationMetabolic acidosisUrinary acidificationDistal renal tubular acidosisAcid challengeRenal tubular acidosisAcute intracellular acidificationB1 subunitLumen-negative potentialFurosemide infusionTubular acidosisAlkaline urineDistal nephronGreater severityAcidosisMiceLoss of B1Intracellular acidificationApical expressionUrineDuctFurther decreaseIsoformsPlasma membrane
2003
A rapid enzymatic method for the isolation of defined kidney tubule fragments from mouse
Wagner CA, Lükewille U, Valles P, Breton S, Brown D, Giebisch GH, Geibel JP. A rapid enzymatic method for the isolation of defined kidney tubule fragments from mouse. Pflügers Archiv - European Journal Of Physiology 2003, 446: 623-632. PMID: 12748863, DOI: 10.1007/s00424-003-1082-3.Peer-Reviewed Original ResearchConceptsProximal tubulesTubule fragmentsMouse kidneyKidney tubule fragmentsCollagenase digestion techniqueMouse proximal tubulesUnits/minTrypan blue exclusionKidney functionInner stripeOuter medullaIntercalated cellsIndependent intracellularBlue exclusionTrypan blueTubulesKidneyMicePH-sensitive dyeLight microscopyDuctAnimalsFurther characterizationATPase activityFunctional characteristics
1993
Endothelin increases [Ca2+]i in M-1 mouse cortical collecting duct cells by a dual mechanism
Korbmacher C, Boulpaep E, Giebisch G, Geibel J. Endothelin increases [Ca2+]i in M-1 mouse cortical collecting duct cells by a dual mechanism. American Journal Of Physiology 1993, 265: c349-c357. PMID: 8368264, DOI: 10.1152/ajpcell.1993.265.2.c349.Peer-Reviewed Original ResearchConceptsEndothelin-1Intracellular storesDuct cellsNifedipine-sensitive Ca2Intracellular calcium concentrationParticipation of Ca2Endothelin increaseFura-2Extracellular calciumExtracellular Ca2Arginine vasopressinIntracellular Ca2Calcium concentrationInitial Ca2Fluorescent imaging systemInitial exposurePlateau phaseMiceEntry mechanismDual mechanismCa2Second Ca2CellsNifedipineVasopressin