2005
HSP70 binding modulates detachment of Na-K-ATPase following energy deprivation in renal epithelial cells
Riordan M, Sreedharan R, Wang S, Thulin G, Mann A, Stankewich M, Van Why S, Kashgarian M, Siegel NJ. HSP70 binding modulates detachment of Na-K-ATPase following energy deprivation in renal epithelial cells. American Journal Of Physiology. Renal Physiology 2005, 288: f1236-f1242. PMID: 15701813, DOI: 10.1152/ajprenal.00438.2004.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsEnergy MetabolismEpithelial CellsHSP70 Heat-Shock ProteinsHumansKidneyLLC-PK1 CellsSodium-Potassium-Exchanging ATPaseSwineTransfectionConceptsRenal epithelial cellsATP depletionMolecular chaperone Hsp70Binding of Hsp70Na-K-ATPaseFundamental cellular mechanismsRenal epithelial polarityCultured renal epithelial cellsEpithelial cellsHeat shock protein 70Protein clathrinEpithelial polarityMolecular chaperonesOverexpression of HSP70Chaperone Hsp70Shock protein 70Energy deprivationLLC-PK1 cellsStress proteinsMolecular mechanismsHSP bindingHSP70Cell lysatesCellular mechanismsATP turnover
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
1998
ATP releases HSP-72 from protein aggregates after renal ischemia
Aufricht C, Lu E, Thulin G, Kashgarian M, Siegel N, Van Why S. ATP releases HSP-72 from protein aggregates after renal ischemia. American Journal Of Physiology 1998, 274: f268-f274. PMID: 9486221, DOI: 10.1152/ajprenal.1998.274.2.f268.Peer-Reviewed Original ResearchMeSH KeywordsActinsAdenosine TriphosphateAnimalsCell MembraneCytoskeletonHeat-Shock ProteinsHSP72 Heat-Shock ProteinsHydrolysisIschemiaKidneyMaleProteinsRatsRats, Sprague-DawleyReperfusionSodium-Potassium-Exchanging ATPase
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
1996
The α3 Isoform Protein of the Na+,K+-ATPase Is Associated With the Sites of Cardiac and Neuromuscular Impulse Transmission
Zahler R, Sun W, Ardito T, Zhang Z, Kocsis J, Kashgarian M. The α3 Isoform Protein of the Na+,K+-ATPase Is Associated With the Sites of Cardiac and Neuromuscular Impulse Transmission. Circulation Research 1996, 78: 870-879. PMID: 8620608, DOI: 10.1161/01.res.78.5.870.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsHeart Conduction SystemImmunohistochemistryIsoenzymesMaleMyocardiumNeuromuscular JunctionRatsRats, Sprague-DawleyRats, WistarSodium-Potassium-Exchanging ATPaseSynaptic TransmissionConceptsNeuromuscular junctionConduction systemImpulse transmissionIsoform-specific antibodiesSkeletal muscle expressesSkeletal musclePresynaptic motor terminalsCardiac conduction systemHeart conduction systemAlpha subunitAxonal processesRat heartCardiac myocytesIsoform mRNAsMuscleClassic morphologyJunctional complexesImmunoreactive proteinPump isoformsAntibodiesIsoform proteinsHeartPump proteinImmunohistochemistryIsoformsNa-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
1995
Functional expression and segmental localization of rat colonic K-adenosine triphosphatase.
Lee J, Rajendran V, Mann A, Kashgarian M, Binder H. Functional expression and segmental localization of rat colonic K-adenosine triphosphatase. Journal Of Clinical Investigation 1995, 96: 2002-2008. PMID: 7560093, PMCID: PMC185838, DOI: 10.1172/jci118247.Peer-Reviewed Original ResearchAdenosine TriphosphatasesAnimalsBase SequenceCation Transport ProteinsColonDNA, ComplementaryMolecular Sequence DataOuabainRabbitsRatsSodium-Potassium-Exchanging ATPase
1994
Expression and molecular regulation of Na(+)-K(+)-ATPase after renal ischemia
Van Why S, Mann A, Ardito T, Siegel N, Kashgarian M. Expression and molecular regulation of Na(+)-K(+)-ATPase after renal ischemia. American Journal Of Physiology 1994, 267: f75-f85. PMID: 8048568, DOI: 10.1152/ajprenal.1994.267.1.f75.Peer-Reviewed Original Research
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 ResearchMeSH KeywordsAnimalsBiological TransportCell MembraneImmunoblottingKidney MedullaKidney Tubules, CollectingRabbitsReference ValuesSodium ChannelsSodium-Potassium-Exchanging ATPaseUreteral ObstructionConceptsObstructed kidneysIMCD cellsUntreated control kidneysOuabain-insensitive QO2Ouabain-sensitive QO2Urinary obstructionObstructive nephropathyControl kidneysControl animalsControl groupKidneyMonoclonal antibodiesMarked reductionDuct cellsAlpha 1Cellular mechanismsSignificant differencesChannel proteinsReabsorptionAntibodiesOxygen consumption studiesTransport defectRabbitsCellsImmunoblotTransport defects of rabbit medullary thick ascending limb cells in obstructive nephropathy.
Hwang S, Haas M, Harris H, Silva P, Yalla S, Sullivan M, Otuechere G, Kashgarian M, Zeidel M. Transport defects of rabbit medullary thick ascending limb cells in obstructive nephropathy. Journal Of Clinical Investigation 1993, 91: 21-28. PMID: 8380811, PMCID: PMC329990, DOI: 10.1172/jci116173.Peer-Reviewed Original ResearchConceptsMedullary thick ascending limbNa-K-ATPase activityNa-K-ATPaseBasolateral Na-K-ATPaseObstructed kidneysObstructive nephropathyUreteral obstructionLuminal NaRelease of obstructionThick ascending limbMajor sodium transportersUntreated kidneysTransport defectSpecific monoclonal antibodiesSodium transport defectsControl animalsAscending limbOuter medullaKidneyApical NaMarked reductionMonoclonal antibodiesMTAL cellsInhibitory effectObstruction
1992
The cardiac conduction system in the rat expresses the alpha 2 and alpha 3 isoforms of the Na+,K(+)-ATPase.
Zahler R, Brines M, Kashgarian M, Benz E, Gilmore-Hebert M. The cardiac conduction system in the rat expresses the alpha 2 and alpha 3 isoforms of the Na+,K(+)-ATPase. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 99-103. PMID: 1309618, PMCID: PMC48183, DOI: 10.1073/pnas.89.1.99.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsGene ExpressionHeart Conduction SystemIsoenzymesMaleNucleic Acid HybridizationRatsRNA ProbesRNA, MessengerSodium-Potassium-Exchanging ATPaseConceptsAlpha 3 isoformAlpha 2Gene expression approachAlpha 1 isoformIsoform genesSpecific hybridization signalAlpha subunitSpecific expressionMembrane channelsSpecific membrane channelsHybridization signalsIsoformsWorking myocytesCardiac conduction systemExcitable tissuesSodium pumpGenesSubunitsATPaseTissueExpressionStrands
1989
Metabolic alterations in proximal tubule suspensions obtained from ischemic kidneys
Gaudio K, Thulin G, Ardito T, Kashgarian M, Siegel N. Metabolic alterations in proximal tubule suspensions obtained from ischemic kidneys. American Journal Of Physiology 1989, 257: f383-f389. PMID: 2551186, DOI: 10.1152/ajprenal.1989.257.3.f383.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsHistological TechniquesIschemiaKidney Tubules, ProximalNystatinOuabainOxygen ConsumptionRatsRats, Inbred StrainsRenal CirculationSodium-Potassium-Exchanging ATPaseSuspensionsTrypan BlueConceptsProximal tubule suspensionsIschemic injuryTubule suspensionsRenal artery ischemiaVivo ischemic injurySprague-Dawley ratsMin of reflowOxygen consumptionPresence of ouabainBasal O2 consumptionArtery ischemiaIschemic kidneyHistopathological appearanceMetabolic alterationsProximal tubulesControl levelsProtein 1Ankyrin 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
1988
Morphological heterogeneity of the rabbit collecting duct
Ridderstrale Y, Kashgarian M, Koeppen B, Giebisch G, Stetson D, Ardito T, Stanton B. Morphological heterogeneity of the rabbit collecting duct. Kidney International 1988, 34: 655-670. PMID: 2462075, DOI: 10.1038/ki.1988.230.Peer-Reviewed Original ResearchBeneficial effect of thyroxin in the treatment of ischemic acute renal failure
Sutter P, Thulin G, Stromski M, Ardito T, Gaudio K, Kashgarian M, Siegel N. Beneficial effect of thyroxin in the treatment of ischemic acute renal failure. Pediatric Nephrology 1988, 2: 1-7. PMID: 2856365, DOI: 10.1007/bf00870370.Peer-Reviewed Original ResearchMeSH KeywordsAcute Kidney InjuryAdenosine TriphosphateAnimalsIschemiaKidneyMaleRatsRats, Inbred StrainsSodium-Potassium-Exchanging ATPaseThyroxineTime FactorsConceptsAcute renal failureIschemic acute renal failureRenal failureIschemic controlsNormal salineSaline-treated ischemic controlsBeneficial effectsBetter kidney functionDose of T4Min of reflowT4-treated ratsEffect of thyroxinRenal functionKidney functionNS animalsRenal ischemiaInulin clearanceSaline controlsDay 3Day 7IschemiaT4 animalsRenal ATPCellular mechanismsSignificant increase[36] Preparation and use of monoclonal antibodies to Na+,K+-ATPase
Kashgarian M, Biemesderfer D. [36] Preparation and use of monoclonal antibodies to Na+,K+-ATPase. Methods In Enzymology 1988, 156: 392-413. PMID: 2835622, DOI: 10.1016/0076-6879(88)56039-1.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, MonoclonalEnzyme-Linked Immunosorbent AssayFluorescent Antibody TechniqueImmunohistochemistryIndicators and ReagentsKidney TubulesMiceSodium-Potassium-Exchanging ATPaseNa,K-ATPase co-distributes with ankyrin and spectrin in renal tubular epithelial cells.
Kashgarian M, Morrow J, Foellmer H, Mann A, Cianci C, Ardito T. Na,K-ATPase co-distributes with ankyrin and spectrin in renal tubular epithelial cells. Progress In Clinical And Biological Research 1988, 268B: 245-50. PMID: 2851802.Peer-Reviewed Original ResearchAnimalsAnkyrinsBlood ProteinsCell LineEpitheliumKidneyKidney TubulesMembrane ProteinsRatsSodium-Potassium-Exchanging ATPaseSpectrin
1985
Monoclonal antibody to Na,K-ATPase: Immunocytochemical localization along nephron segments
Kashgarian M, Biemesderfer D, Caplan M, Forbush B. Monoclonal antibody to Na,K-ATPase: Immunocytochemical localization along nephron segments. Kidney International 1985, 28: 899-913. PMID: 3003443, DOI: 10.1038/ki.1985.216.Peer-Reviewed Original ResearchConceptsMonoclonal antibodiesNephron segmentsEvidence of labellingRenal tubular epithelial cellsTubular epithelial cellsK-ATPaseThick ascending limbOnly principal cellsDifferent nephron segmentsDog antigensBasal-lateral membranesSignificant antibodiesAscending limbMesangial regionHenle's loopOccasional cellsRenal medullaOuter renal medullaAbundant antibodyAntibodiesApical labelingTubule segmentsPrincipal cellsEpithelial cellsImmunocytochemical localization
1984
Role of aldosterone in the mechanism of potassium adaptation in the initial collecting tubule
Hirsch D, Kashgarian M, Boulpaep E, Hayslett J. Role of aldosterone in the mechanism of potassium adaptation in the initial collecting tubule. Kidney International 1984, 26: 798-807. PMID: 6099857, DOI: 10.1038/ki.1984.221.Peer-Reviewed Original ResearchMeSH KeywordsAdrenal GlandsAldosteroneAnimalsEpitheliumKidney TubulesKidney Tubules, CollectingKidney Tubules, DistalMaleMembrane PotentialsPotassiumRatsRats, Inbred StrainsSodium-Potassium-Exchanging ATPaseWater-Electrolyte BalanceConceptsInitial collecting tubuleCollecting tubuleDistal convolutionAldosterone levelsPotassium adaptationChronic potassium loadingMineralocorticoid-sensitive tissuesRole of aldosteronePlasma aldosterone levelsAction of aldosteroneIntact adrenal glandsPotassium loadingPhysiological plasma levelsChronic hyperaldosteronismTransepithelial potential differenceChronic administrationEpithelial changesAdrenal glandPlasma levelsDietary potassium loadingBasal valuesAldosteroneTubule cellsNephron segmentsTarget tissues
1980
Changes in membrane surfaces of collecting duct cells in potassium adaptation
Rastegar A, Biemesderfer D, Kashgarian M, Hayslett J, Kashgarian M. Changes in membrane surfaces of collecting duct cells in potassium adaptation. Kidney International 1980, 18: 293-301. PMID: 6257963, DOI: 10.1038/ki.1980.139.Peer-Reviewed Original ResearchMeSH KeywordsAdaptation, PhysiologicalAnimalsCell MembraneKidney MedullaKidney TubulesKidney Tubules, CollectingMaleNephronsPotassiumRatsSodium-Potassium-Exchanging ATPase