2017
Stomach and Bone
Kitay AM, Geibel JP. Stomach and Bone. Advances In Experimental Medicine And Biology 2017, 1033: 97-131. PMID: 29101653, DOI: 10.1007/978-3-319-66653-2_6.Peer-Reviewed Original ResearchConceptsBone metabolismGastric acid secretionCalcium-sensing receptorVitamin DParathyroid glandsAcid secretionGastrointestinal organsTherapeutic implicationsEndocrine modulatorsCalcium homeostasisDiseaseStomachOrgansMetabolismImportant playersIntermediary organDiverse tissuesDysfunctionCaSRPTHCalcitoninKidneySecretionIntestineReceptors
2014
Calcium-sensing receptor 20 years later
Alfadda TI, Saleh AM, Houillier P, Geibel JP. Calcium-sensing receptor 20 years later. American Journal Of Physiology - Cell Physiology 2014, 307: c221-c231. PMID: 24871857, PMCID: PMC4121584, DOI: 10.1152/ajpcell.00139.2014.Peer-Reviewed Original ResearchConceptsCellular ion transport mechanismsG protein-coupled receptor familyProtein-coupled receptor familyEnvironmental cuesExtracellular environmentOrgan physiologyReceptor familySense changesDifferent tissuesCellular levelCalcium-sensing receptorIon transport mechanismsPhysiologyReceptor physiologyAmino acid concentrationsDisease statesReceptorsSystemic physiologyDiversity of locationsReceptor mutationsDifferent organ systemsImportant roleMembersFamilyHomology
2011
The Anion Exchanger Pendrin (SLC26A4) and Renal Acid-base Homeostasis
Wagner CA, Mohebbi N, Capasso G, Geibel JP. The Anion Exchanger Pendrin (SLC26A4) and Renal Acid-base Homeostasis. Cellular Physiology And Biochemistry 2011, 28: 497-504. PMID: 22116363, DOI: 10.1159/000335111.Peer-Reviewed Original ResearchConceptsAcid-base homeostasisAnion exchanger pendrinExchanger pendrinRenal acid-base homeostasisDietary electrolyte intakeSystemic acid-base statusRole of pendrinType BNormal acid-base homeostasisRegulation of pendrinAcid-base statusRenal expressionAngiotensin IIKidney's roleElectrolyte intakePendrin expressionPositive cellsExchanger activityGenetic ablationAdult kidneyPendrinExpressing cellsLuminal poleKidneyHomeostasis
2010
The calcium-sensing receptor.
Geibel JP. The calcium-sensing receptor. Journal Of Nephrology 2010, 23 Suppl 16: s130-5. PMID: 21170870.Peer-Reviewed Original ResearchConceptsCalcium-sensing receptorExtracellular environmentReceptor-targeted drugsThick ascending limbFiltered loadAscending limbNephron segmentsAmino acidsHandling of waterReceptorsImportant roleBasic physiologyImportant memberSalt absorptionRecent studiesDivalent ion concentrationSalinityCalciumIonic absorptionCaSR
2004
Renal Vacuolar H+-ATPase
Wagner CA, Finberg KE, Breton S, Marshansky V, Brown D, Geibel JP. Renal Vacuolar H+-ATPase. Physiological Reviews 2004, 84: 1263-1314. PMID: 15383652, DOI: 10.1152/physrev.00045.2003.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsProximal tubular bicarbonate reabsorptionDistal renal tubular acidosisTubular bicarbonate reabsorptionRenal tubular acidosisFinal urinary acidificationTubular acidosisElectrolyte statusBicarbonate reabsorptionMonogenic defectsProximal tubulesUrinary acidificationKidneyATP-dependent transportVariety of factorsHigher numberPatientsIntracellular organellesAcidosisRegulatory proteinsLocalization patterns
2003
Localization and Regulation of the ATP6V0A4 (a4) Vacuolar H+-ATPase Subunit Defective in an Inherited Form of Distal Renal Tubular Acidosis
Stehberger PA, Schulz N, Finberg KE, Karet FE, Giebisch G, Lifton RP, Geibel JP, Wagner CA. Localization and Regulation of the ATP6V0A4 (a4) Vacuolar H+-ATPase Subunit Defective in an Inherited Form of Distal Renal Tubular Acidosis. Journal Of The American Society Of Nephrology 2003, 14: 3027-3038. PMID: 14638902, DOI: 10.1097/01.asn.0000099375.74789.ab.Peer-Reviewed Original ResearchConceptsDistal renal tubular acidosisRenal tubular acidosisLoop of HenleProximal tubulesTubular acidosisMouse kidneyA4 expressionDistal tubulesDistal convoluted tubuleProtein expression levelsElectrolyte intakeA4 proteinConvoluted tubulesMouse nephron segmentsNephron segmentsApical stainingWestern blottingAcidosisProtein expressionKidneyATPase activityDistal portionHenleExpression levelsTubulesMolecular cloning and characterization of Atp6v1b1, the murine vacuolar H+-ATPase B1-subunit
Finberg KE, Wagner CA, Stehberger PA, Geibel JP, Lifton RP. Molecular cloning and characterization of Atp6v1b1, the murine vacuolar H+-ATPase B1-subunit. Gene 2003, 318: 25-34. PMID: 14585495, DOI: 10.1016/s0378-1119(03)00790-x.Peer-Reviewed Original ResearchMeSH Keywords5' Flanking RegionAmino Acid SequenceAnimalsAntibody SpecificityBase SequenceCloning, MolecularDNADNA, ComplementaryEpididymisGene Expression Regulation, EnzymologicHumansImmune SeraImmunohistochemistryIsoenzymesKidneyMaleMiceMice, Inbred StrainsMolecular Sequence DataPhylogenyProtein SubunitsRNA, MessengerSequence AlignmentSequence Analysis, DNASequence Homology, Amino AcidSequence Homology, Nucleic AcidVacuolar Proton-Translocating ATPasesConceptsDistal renal tubular acidosisRenal tubular acidosisMouse renal cortexProton-translocating ATPasesTubular acidosisRenal cortexSubset of tissuesAnimal modelsATP6V1B1Major organsGenomic organizationGenomic lociMouse kidneyProtein levelsMolecular cloningAcid proteinPlasma membraneMurine orthologIntracellular organellesB1 isoformKidneyNorthern blotting
1999
Thresholds for cellular disruption and activation of the stress response in renal epithelia
van Why S, Kim S, Geibel J, Seebach F, Kashgarian M, Siegel N. Thresholds for cellular disruption and activation of the stress response in renal epithelia. American Journal Of Physiology 1999, 277: f227-f234. PMID: 10444577, DOI: 10.1152/ajprenal.1999.277.2.f227.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCalciumCysteine EndopeptidasesDetergentsDifferential ThresholdDNA-Binding ProteinsEpithelial CellsHeat Shock Transcription FactorsHeat-Shock ProteinsIntracellular MembranesKidneyL-Lactate DehydrogenaseLLC-PK1 CellsMultienzyme ComplexesOctoxynolProteasome Endopeptidase ComplexSodium-Potassium-Exchanging ATPaseSolubilityStress, PhysiologicalSwineTranscription FactorsConceptsATP depletionRenal epitheliumLactate dehydrogenase releaseCellular ATPReduction of ATPRenal ischemiaIntracellular calciumActivation of HSF1Heat shock transcription factorDehydrogenase releaseControl ATPStress responseControl levelsProgressive accumulationProteasome inhibitionAdaptive inductionHSF activationRapid fallActivationEpitheliumIncremental increaseCellular disruptionResponseATPIschemia
1997
Differential activities of H+extrusion systems in MDCK cells due to extracellular osmolality and pH
Feifel E, Krall M, Geibel J, Pfaller W. Differential activities of H+extrusion systems in MDCK cells due to extracellular osmolality and pH. American Journal Of Physiology 1997, 273: f499-f506. PMID: 9362327, DOI: 10.1152/ajprenal.1997.273.4.f499.Peer-Reviewed Original ResearchLife on biomembranes viewed with the atomic force microscope.
Oberleithner H, Geibel J, Guggino W, Henderson R, Hunter M, Schneider S, Schwab A, Wang W. Life on biomembranes viewed with the atomic force microscope. Wiener Klinische Wochenschrift 1997, 109: 419-23. PMID: 9261980.Peer-Reviewed Original ResearchConceptsAtomic force microscopeForce microscopeNear-field microscopePlasma membrane turnoverSoft biological surfacesPore complexRenal epithelial cellsAtomic resolutionNuclear poresXenopus laevis oocytesNuclear envelopeAFM techniquesExperimental biologistsLaevis oocytesMembrane turnoverKidney cellsEpithelial cellsMicroscopePotassium channelsBirthday candlesBiological surfacesCellsBiomembranesMolecular structureRecent dataLocalization of amiloride-sensitive sodium channels in A6 cells by atomic force microscopy
Smith P, Bradford A, Schneider S, Benos D, Geibel J. Localization of amiloride-sensitive sodium channels in A6 cells by atomic force microscopy. American Journal Of Physiology 1997, 272: c1295-c1298. PMID: 9142855, DOI: 10.1152/ajpcell.1997.272.4.c1295.Peer-Reviewed Original ResearchConceptsAtomic force microscopyHigh-resolution imagingRenal epithelial cellsForce microscopyA6 cellsApical microvilliCell surface distributionBovine renal medullaEpithelial cellsA6 renal epithelial cellsAmiloride-sensitive sodium channelsEpithelial ion channelsColloidal gold particlesApical distributionIon channelsChannel complexGold particlesSodium channelsCellsMicrovilliNonimmune immunoglobulin GUnlabeled cellsMicroscopySurface distributionParticles
1995
Visualizing life on biomembranes by atomic force microscopy
Oberleithner H, Brinckmann E, Giebisch G, Geibel J. Visualizing life on biomembranes by atomic force microscopy. Kidney International 1995, 48: 923-929. PMID: 8569101, DOI: 10.1038/ki.1995.373.Peer-Reviewed Original ResearchConceptsAtomic force microscopeNear-field microscopeSoft biological samplesAtomic force microscopyPlasma membrane turnoverForce microscopeForce microscopyPore complexRenal epithelial cellsAtomic resolutionNuclear envelopeAFM techniquesExperimental biologistsMembrane turnoverMolecular structureKidney cellsEpithelial cellsBiological samplesMicroscopeCellsBiomembranesRepresentative examplesRecent dataBiologistsMicroscopy
1994
Living Renal Epithelial Cells Imaged by Atomic Force Microscopy
Oberleithner H, Schwab A, Wang W, Giebisch G, Hume F, Geibel J. Living Renal Epithelial Cells Imaged by Atomic Force Microscopy. Nephron 1994, 66: 8-13. PMID: 8107959, DOI: 10.1159/000187759.Peer-Reviewed Original Research
1993
Imaging the lamellipodium of migrating epithelial cells in vivo by atomic force microscopy
Oberleithner H, Giebisch G, Geibel J. Imaging the lamellipodium of migrating epithelial cells in vivo by atomic force microscopy. Pflügers Archiv - European Journal Of Physiology 1993, 425: 506-510. PMID: 8134267, DOI: 10.1007/bf00374878.Peer-Reviewed Original ResearchConceptsPlasma membraneCell locomotionNew plasma membraneCell surfacePlasma membrane potentialCanine kidney cell linePlasma membrane integrityMadin-Darby canine kidney (MDCK) cell lineDynamic physiological processesKidney cell lineAlkaline stressInvagination processCytoskeletal elementsMDCK-F cellsPhysiological processesMembrane integrityMembrane turnoverCell linesKidney cellsMembrane potentialEpithelial cellsTurnover processCellsMembranePotential roleMechanism of activation of K++ channels by minoxidil-sulfate in Madin-Darby canine kidney cells
Schwab A, Geibel J, Wang W, Oberleithner H, Giebisch G. Mechanism of activation of K++ channels by minoxidil-sulfate in Madin-Darby canine kidney cells. The Journal Of Membrane Biology 1993, 132: 125-136. PMID: 8496944, DOI: 10.1007/bf00239002.Peer-Reviewed Original Research