2010
The maximal cytoprotective function of the heat shock protein 27 is dependent on heat shock protein 70
Sreedharan R, Riordan M, Thullin G, Van Why S, Siegel NJ, Kashgarian M. The maximal cytoprotective function of the heat shock protein 27 is dependent on heat shock protein 70. Biochimica Et Biophysica Acta 2010, 1813: 129-135. PMID: 20934464, PMCID: PMC3014454, DOI: 10.1016/j.bbamcr.2010.08.012.Peer-Reviewed Original ResearchConceptsHeat shock protein 70Shock protein 70Cell injuryProtein 70Heat shock protein 27Renal cell injuryExpression of HSP27Maximal cytoprotective effectShock protein 27Endogenous hspNuclear binding sitesCytoprotective effectsInjuryRenal cellsLLC-PK1 cellsProtein 27Specific siRNAHSP-70HSP70 inductionRespective controlsHSP27Particular HSP70Cytoprotective functionEnergy depletionATP depletion
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
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
Role of heat stress response in the tolerance of immature renal tubules to anoxia
Gaudio K, Thulin G, Mann A, Kashgarian M, Siegel N. Role of heat stress response in the tolerance of immature renal tubules to anoxia. American Journal Of Physiology 1998, 274: f1029-f1036. PMID: 9841493, DOI: 10.1152/ajprenal.1998.274.6.f1029.Peer-Reviewed Original ResearchMeSH KeywordsAge FactorsAnimalsAnimals, NewbornBlotting, NorthernCarbonyl Cyanide m-Chlorophenyl HydrazoneCell HypoxiaDNA, MitochondrialDNA-Binding ProteinsElectrophoresisHeat Shock Transcription FactorsHeat-Shock ProteinsHot TemperatureHSP72 Heat-Shock ProteinsKidney TubulesMitochondriaNystatinOuabainOxygen ConsumptionRatsRNA, MessengerTranscription FactorsATP 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 ResearchHeat-shock protein 25 induction and redistribution during actin reorganization after renal ischemia
Aufricht C, Ardito T, Thulin G, Kashgarian M, Siegel N, Van Why S. Heat-shock protein 25 induction and redistribution during actin reorganization after renal ischemia. American Journal Of Physiology 1998, 274: f215-f222. PMID: 9458842, DOI: 10.1152/ajprenal.1998.274.1.f215.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsAorta, AbdominalCytoskeletonHeat-Shock ProteinsIschemiaKidneyKidney Tubules, ProximalMaleRatsRats, Sprague-DawleyRenal ArteryConceptsHSP-25Renal ischemiaHeat shock protein 25Ischemic renal injuryH reflowRat renal cortexControl proximal tubulesRenal injuryPostischemic recoveryRenal cortexIschemiaProximal tubulesIntracytoplasmic accumulationPeak levelsHeat shock proteinsProtein 25Actin stainingInsoluble cytoskeletal fractionPunctate accumulationsCytoskeletal disruptionSmall heat shock proteinsRegulatory roleInductionIntracellular distributionCytoskeletal fraction
1992
Induction and intracellular localization of HSP-72 after renal ischemia
Van Why S, Hildebrandt F, Ardito T, Mann A, Siegel N, Kashgarian M. Induction and intracellular localization of HSP-72 after renal ischemia. American Journal Of Physiology 1992, 263: f769-f775. PMID: 1443167, DOI: 10.1152/ajprenal.1992.263.5.f769.Peer-Reviewed Original ResearchConceptsHSP 72Renal ischemiaHeat shock proteinsIschemic renal injuryMin of reperfusionProtein elaborationHSP mRNA expressionHSP-70 mRNARenal injuryIschemic injuryTransient ischemiaProximal tubulesIschemiaRat kidneyMRNA expressionIntracellular localizationMRNA inductionInjuryTubule morphologyImmunofluorescent localizationShock proteinsVesicular patternCellular recoveryHSP proteinsCellular remodeling