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
1996
Na-K-ATPase alpha-isoform expression in heart and vascular endothelia: cellular and developmental regulation
Zahler R, Sun W, Ardito T, Kashgarian M. Na-K-ATPase alpha-isoform expression in heart and vascular endothelia: cellular and developmental regulation. American Journal Of Physiology 1996, 270: c361-c371. PMID: 8772464, DOI: 10.1152/ajpcell.1996.270.1.c361.Peer-Reviewed Original ResearchConceptsCardiac conduction systemAlpha 2Alpha 1Alpha 3Vascular endotheliumConduction systemHigh ouabain affinityNa-K-ATPase isoformsDevelopmental regulationAlpha 3 expressionImportant species differencesNeonatal rat myocardiumIsoform patternNeonatal ratsPapillary musclesDistinct physiological rolesSmooth muscleImmunohistochemical analysisConduction tissueVentricular myocardiumOuabain affinityRat myocardiumNormal endotheliumRat heartT-tubule system
1993
Transport defects of rabbit inner medullary collecting duct cells in obstructive nephropathy
Hwang S, Harris H, Otuechere G, Yalla S, Sullivan M, Kashgarian M, Benos D, Kleyman T, Zeidel M. Transport defects of rabbit inner medullary collecting duct cells in obstructive nephropathy. American Journal Of Physiology 1993, 264: f808-f815. PMID: 8388652, DOI: 10.1152/ajprenal.1993.264.5.f808.Peer-Reviewed Original ResearchConceptsObstructed kidneysIMCD cellsUntreated control kidneysOuabain-insensitive QO2Ouabain-sensitive QO2Urinary obstructionObstructive nephropathyControl kidneysControl animalsControl groupKidneyMonoclonal antibodiesMarked reductionDuct cellsAlpha 1Cellular mechanismsSignificant differencesChannel proteinsReabsorptionAntibodiesOxygen consumption studiesTransport defectRabbitsCellsImmunoblot
1989
Ankyrin links fodrin to the alpha subunit of Na,K-ATPase in Madin-Darby canine kidney cells and in intact renal tubule cells.
Morrow J, Cianci C, Ardito T, Mann A, Kashgarian M. Ankyrin links fodrin to the alpha subunit of Na,K-ATPase in Madin-Darby canine kidney cells and in intact renal tubule cells. Journal Of Cell Biology 1989, 108: 455-465. PMID: 2537316, PMCID: PMC2115445, DOI: 10.1083/jcb.108.2.455.Peer-Reviewed Original ResearchConceptsMadin-Darby canine kidney cellsCanine kidney cellsK-ATPaseAlpha subunitMolecular mechanismsMDCK cellsMinor membrane proteinsDistribution of fodrinErythrocyte ankyrinConfluent MDCK cellsBinding of ankyrinKidney cellsHuman erythrocyte ankyrinRenal epithelial cellsCytoplasmic domainNonerythroid cellsMembrane proteinsCortical cytoskeletonBasolateral domainMembrane skeletonPolarized distributionAnkyrinBasolateral marginsCell developmentErythrocyte band 3