2003
Molecular 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
2002
Regulation of the expression of the Cl-/anion exchanger pendrin in mouse kidney by acid-base status
Wagner CA, Finberg KE, Stehberger PA, Lifton RP, Giebisch GH, Aronson PS, Geibel JP. Regulation of the expression of the Cl-/anion exchanger pendrin in mouse kidney by acid-base status. Kidney International 2002, 62: 2109-2117. PMID: 12427135, DOI: 10.1046/j.1523-1755.2002.00671.x.Peer-Reviewed Original ResearchConceptsPendrin-positive cellsAcid-base statusPositive cellsBicarbonate secretionMouse kidneyAcid-base transportKnockout mouse modelProtein expression levelsMetabolic alkalosisDeficient dietExchanger pendrinPendrin expressionMouse modelSensorineural deafnessThyroid glandBicarbonate loadPendred syndromeWestern blottingApical membraneInner earPendrin proteinControl levelsKidneyPendrinProtein levels
2001
K+-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