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
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 ResearchConceptsRenal 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