2013
Activation of the Ca2+-sensing receptor induces deposition of tight junction components to the epithelial cell plasma membrane
Jouret F, Wu J, Hull M, Rajendran V, Mayr B, Schöfl C, Geibel J, Caplan MJ. Activation of the Ca2+-sensing receptor induces deposition of tight junction components to the epithelial cell plasma membrane. Journal Of Cell Science 2013, 126: 5132-5142. PMID: 24013548, PMCID: PMC3828589, DOI: 10.1242/jcs.127555.Peer-Reviewed Original ResearchConceptsTJ assemblyMDCK cellsStable transfectionFunction mutant formZO-1Tight junction components ZO-1G protein-coupled receptorsHuman CaSRCell-cell contactEpithelial cell plasma membranesMadin-Darby canine kidney cellsCell plasma membraneStimulation of CaSRDivalent ion homeostasisCanine kidney cellsTight junctionsJunction-associated proteinsTight junction componentsEndogenous CaSRProtein kinasePlasma membraneIon homeostasisMutant formsChelator BAPTA-AMCell differentiation
2006
Somatostatin modulates PI3K-Akt, eNOS and NHE activity in the ciliary epithelium
Ghosh S, Choritz L, Geibel J, Coca-Prados M. Somatostatin modulates PI3K-Akt, eNOS and NHE activity in the ciliary epithelium. Molecular And Cellular Endocrinology 2006, 253: 63-75. PMID: 16764985, DOI: 10.1016/j.mce.2006.05.002.Peer-Reviewed Original ResearchConceptsP-Akt Ser473Ciliary epitheliumIntracellular cyclic GMP productionInvolvement of somatostatinDose-dependent attenuationReceptor mRNA expressionCyclic GMP productionSST-like immunoreactivityLack of responseOcular ciliary epitheliumAqueous humorSomatostatinNHE activityExchanger activityMRNA expressionCiliary processesNeuroendocrine cellsPC2 antibodyPI3K-AktMultiple intracellularGMP productionConvertases PC1Increases phosphorylationTissue extractsEpithelium
2002
Calcium-pump inhibitors induce functional surface expression of ΔF508-CFTR protein in cystic fibrosis epithelial cells
Egan ME, Glöckner-Pagel J, Ambrose C, Cahill PA, Pappoe L, Balamuth N, Cho E, Canny S, Wagner CA, Geibel J, Caplan MJ. Calcium-pump inhibitors induce functional surface expression of ΔF508-CFTR protein in cystic fibrosis epithelial cells. Nature Medicine 2002, 8: 485-492. PMID: 11984593, DOI: 10.1038/nm0502-485.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumCalcium pump inhibitorΔF508-CFTR proteinCystic fibrosis epithelial cellsCystic fibrosis transmembrane conductance regulator (CFTR) proteinCystic fibrosis cell lineFunctional surface expressionSurface expressionChaperone activityChaperone proteinsRegulator proteinPlasma membraneCystic fibrosis defectCell surfaceProteinCell linesPotential targetOptimal activityInhibitor thapsigarginEpithelial cellsExpressionCommon mutationsInhibitorsMouse modelReticulum
2001
Effects of the Serine/Threonine Kinase SGK1 on the Epithelial Na+ Channel (ENaC) and CFTR: Implications for Cystic Fibrosis
Wagner C, Ott M, Klingel K, Beck S, Melzig J, Friedrich B, Wild K, Bröer S, Moschen I, Albers A, Waldegger S, Tümmler B, Egan M, Geibel J, Kandolf R, Lang F. Effects of the Serine/Threonine Kinase SGK1 on the Epithelial Na+ Channel (ENaC) and CFTR: Implications for Cystic Fibrosis. Cellular Physiology And Biochemistry 2001, 11: 209-218. PMID: 11509829, DOI: 10.1159/000051935.Peer-Reviewed Original ResearchMeSH Keywords1-Methyl-3-isobutylxanthineAmino Acid SubstitutionAnimalsBronchiCell LineCystic FibrosisCystic Fibrosis Transmembrane Conductance RegulatorEpithelial CellsEpithelial Sodium ChannelsHumansIn Situ HybridizationLungMacrophages, AlveolarMutationOocytesPatch-Clamp TechniquesProtein Serine-Threonine KinasesPulmonary AlveoliRNA, ComplementaryRNA, MessengerSodiumSodium ChannelsXenopus laevisConceptsSerine/threonine kinase SGK1Lung tissueCystic fibrosisCF patientsKinase SGK1CF lung tissueXenopus oocytesLoss of CFTRLung epithelial cell lineCoexpression of CFTREffect of SGK1Pathophysiological factorsEpithelial cell lineRespiratory epitheliumLung phenotypeVariety of stimuliCl(-) secretionSGK1 expressionInhibitor amilorideInhibitory effectEpithelial cellsEnhanced expressionChannel ENaC.CFTR mutationsChannel activityK+-induced HSP-72 expression is mediated via rapid Ca2+ influx in renal epithelial cells
Eickelberg O, Geibel J, Seebach F, Giebisch G, Kashgarian M. K+-induced HSP-72 expression is mediated via rapid Ca2+ influx in renal epithelial cells. American Journal Of Physiology. Renal Physiology 2001, 281: f280-f287. PMID: 11457719, DOI: 10.1152/ajprenal.2001.281.2.f280.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCalcium Channel BlockersCell LineDiltiazemEgtazic AcidEnzyme InhibitorsEpithelial CellsGallic AcidGenes, ReporterHeat-Shock ProteinsHSP72 Heat-Shock ProteinsImmunoblottingKidney Tubules, ProximalMicroscopy, ConfocalPotassiumPromoter Regions, GeneticRecombinant Fusion ProteinsSodiumSwineThapsigarginUrotheliumConceptsHSP 72 expressionPromoter activityHSP 72Protein expressionProtective cellular responseLuciferase reporter geneHSP-25Heat shock protein expressionRenal epithelial cellsTranscriptional inductionShock protein expressionIonic stressReporter geneHSP-90 levelsHSC 73Cellular responsesChannel blocker diltiazemIntracellular lumenWestern blot analysisChelator EGTA-AMPathophysiological stimuliBlot analysisConfocal microscopyProtein levelsExtracellular space
1999
Continuous detection of extracellular ATP on living cells by using atomic force microscopy
Schneider S, Egan M, Jena B, Guggino W, Oberleithner H, Geibel J. Continuous detection of extracellular ATP on living cells by using atomic force microscopy. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 12180-12185. PMID: 10518596, PMCID: PMC18432, DOI: 10.1073/pnas.96.21.12180.Peer-Reviewed Original ResearchConceptsAtomic force microscopyForce microscopyLiving cellsImportant compoundsSurface of cellsATP concentrationSurface microenvironmentScanning tipExtracellular ATPCell linesMicroscopyPhysiological conditionsPowerful techniqueCellsContinuous detectionBiosensorSurfaceCompoundsActive tipATPConcentrationFuture developmentSoftnessDetectionMicroenvironmentThresholds 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
1998
Role of Apical H-K Exchange and Basolateral K Channel in the Regulation of Intracellular pH in Rat Distal Colon Crypt Cells
Ikuma M, Binder H, Geibel J. Role of Apical H-K Exchange and Basolateral K Channel in the Regulation of Intracellular pH in Rat Distal Colon Crypt Cells. The Journal Of Membrane Biology 1998, 166: 205-212. PMID: 9843594, DOI: 10.1007/s002329900462.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntiportersBariumCell PolarityColonEpithelial CellsH(+)-K(+)-Exchanging ATPaseHomeostasisHydrogen-Ion ConcentrationIntestinal MucosaIntracellular FluidIon TransportMaleOuabainPotassiumPotassium ChannelsPotassium-Hydrogen AntiportersRatsRats, Sprague-DawleySodium-Potassium-Exchanging ATPaseSorting of P-type ATPases in polarized epithelial cells.
Dunbar LA, Courtois-Coutry N, Roush DL, Muth TR, Gottardi CJ, Rajendran V, Geibel J, Kashgarian M, Caplan MJ. Sorting of P-type ATPases in polarized epithelial cells. Acta Physiologica Scandinavica. Supplementum 1998, 643: 289-95. PMID: 9789572.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell PolarityEpithelial CellsH(+)-K(+)-Exchanging ATPaseSodium-Potassium-Exchanging ATPaseConceptsApical localizationK-ATPaseMost epithelial cell typesTyrosine-based signalsP-type familyP-type ATPasesEpithelial cellsCritical tyrosine residuesApical plasma membraneFourth transmembrane domainBeta-subunit sequencesApical cell surfaceEpithelial cell typesSorting signalsTransmembrane domainCytoplasmic tailSequence domainsPlasma membraneHomologous membersTyrosine residuesParietal cellsStorage compartmentCell typesCell surfaceBasolateral surface
1997
Sorting of Ion Pumps in Polarized Epithelial Cells.a
DUNBAR L, ROUSH D, COURTOIS‐COUTRY N, MUTH T, GOTTARDI CJ, RAJENDRAN V, GEIBEL J, KASHGARIAN M, CAPLAN M. Sorting of Ion Pumps in Polarized Epithelial Cells.a. Annals Of The New York Academy Of Sciences 1997, 834: 514-523. PMID: 9405853, DOI: 10.1111/j.1749-6632.1997.tb52309.x.Peer-Reviewed Original ResearchAmino Acid SequenceCell MembraneCell PolarityConserved SequenceEpithelial CellsH(+)-K(+)-Exchanging ATPaseHumansMacromolecular SubstancesModels, MolecularMolecular Sequence DataProtein Structure, SecondaryReceptors, TransferrinRecombinant Fusion ProteinsSequence AlignmentSequence Homology, Amino AcidSodium-Potassium-Exchanging ATPase
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 ResearchMeSH KeywordsAnimalsCell LineCell MembraneCell MovementDogsEpithelial CellsEpitheliumImage Processing, Computer-AssistedKidneyMicroscopyConceptsPlasma 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 role