2007
SLC26A7 Can function as a chloride-loading mechanism in parietal cells
Kosiek O, Busque SM, Föller M, Shcheynikov N, Kirchhoff P, Bleich M, Muallem S, Geibel JP. SLC26A7 Can function as a chloride-loading mechanism in parietal cells. Pflügers Archiv - European Journal Of Physiology 2007, 454: 989-998. PMID: 17404755, DOI: 10.1007/s00424-007-0254-y.Peer-Reviewed Original ResearchMeSH Keywords4,4'-Diisothiocyanostilbene-2,2'-Disulfonic AcidAnimalsAntiportersChloride-Bicarbonate AntiportersChloridesFluorescent Antibody TechniqueGastric AcidGastric MucosaImage Processing, Computer-AssistedIn Vitro TechniquesMaleOocytesParietal Cells, GastricPatch-Clamp TechniquesRatsRats, Sprague-DawleySodiumSodium-Potassium-Chloride SymportersSolute Carrier Family 12, Member 2Sulfate TransportersXenopusConceptsParietal cellsXenopus laevis oocyte expression systemRat parietal cellsExpression of SLC26A7Rat gastric glandsAcid secretionOocyte expression systemNKCC inhibitorWestern blotHistamine stimulationPharmacological inhibitorsAcidic pHiGastric glandsDIDS concentrationExchanger AE2Subsequent readditionTransporter activityDisulfonic acidInhibitorsCellsSLC26A7InfluxImmunohistochemistrySecretagoguesUptake system
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 activity
2000
Calcium, ATP and nuclear pore channel gating
Bustamante J, Michelette E, Geibel J, Dean D, Hanover J, McDonnell T. Calcium, ATP and nuclear pore channel gating. Pflügers Archiv - European Journal Of Physiology 2000, 439: 433-444. PMID: 10678739, PMCID: PMC4400178, DOI: 10.1007/s004249900189.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsAntibodies, MonoclonalBiological TransportCalciumCalcium ChannelsChelating AgentsCytosolDextransEgtazic AcidEndoplasmic ReticulumEnzyme InhibitorsFluorescein-5-isothiocyanateFluorescent DyesGene Expression Regulation, NeoplasticInositol 1,4,5-TrisphosphateIon Channel GatingMaleNuclear EnvelopeOocytesPatch-Clamp TechniquesProstatic NeoplasmsThapsigarginTumor Cells, CulturedXenopus laevisConceptsNPC channelGene activityChannel gatingMacromolecular transportCytosolic Ca2Fluorescence microscopy observationsTranscription factorsNE membranesProstate cancer cellsCytosolic ATPIntracellular messengerCellular rhythmsRole of Ca2ATPCancer cellsPatch-clamp studiesPresent patch-clamp studyRNAIon channel behaviorRegulationCardiomyocyte nucleiGatingExpressionCa2Thapsigargin
1997
Life 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 data