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Heat shock protein 70 negatively regulates the heat-shock-induced suppression of the IkappaB/NF-kappaB cascade by facilitating IkappaB kinase renaturation and blocking its further denaturation

DC Field Value Language
dc.contributor.authorLee, K. H.-
dc.contributor.authorLee, C. T.-
dc.contributor.authorKim, Y. W.-
dc.contributor.authorHan, S. K.-
dc.contributor.authorShim, Y. S.-
dc.contributor.authorYoo, C. G.-
dc.date.accessioned2009-12-24T11:22:24Z-
dc.date.available2009-12-24T11:22:24Z-
dc.date.issued2005-06-01-
dc.identifier.citationExp Cell Res. 2005 Jul 1;307(1):276-84. Epub 2005 Apr 13.en
dc.identifier.issn0014-4827 (Print)-
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15922746-
dc.identifier.urihttp://hdl.handle.net/10371/22618-
dc.description.abstractHeat shock (HS) treatment has been previously shown to suppress the IkappaB/nuclear factor-kappaB (NF-kappaB) cascade by denaturing, and thus inactivating IkappaB kinase (IKK). HS is characterized by the induction of a group of heat shock proteins (HSPs). However, their role in the HS-induced suppression of the IkappaB/NF-kappaB cascade is unclear. Adenovirus-mediated HSP70 overexpression was found not to suppress the TNF-alpha-induced activation of the IkappaB/NF-kappaB pathway, thus suggesting that HSP70 is unlikely to suppress this pathway. When TNF-alpha-induced activation of the IkappaB/NF-kappaB pathway was regained 24 h after HS, HSP70 was found to be highly up-regulated. Moreover, blocking HSP70 induction delayed TNF-alpha-induced IkappaBalpha degradation and the resolubilization of IKK. In addition, HSP70 associated physically with IKK, suggesting that HSP70 is involved in the recovery process via molecular chaperone effect. Adenovirus-mediated HSP70 overexpression prior to HS blocked the IkappaBalpha stabilizing effect of HS by suppressing IKK insolubilization. Moreover, the up-regulation of endogenous HSP70 by preheating, suppressed this subsequent HS-induced IKK insolubilization, and this effect was abrogated by blocking HSP70 induction. These findings indicate that HSP70 accumulates during HS and negatively regulates the HS-induced suppression of the IkappaB/NF-kappaB cascade by facilitating the renaturation of IKK and blocking its further denaturation.en
dc.language.isoenen
dc.publisherElsevieren
dc.subjectAdenoviridae/geneticsen
dc.subjectBlotting, Westernen
dc.subjectBronchi/cytologyen
dc.subjectCell Culture Techniquesen
dc.subjectCell Lineen
dc.subjectElectrophoretic Mobility Shift Assayen
dc.subjectEnzyme Activationen
dc.subjectEpithelial Cells/cytologyen
dc.subjectGene Expression Regulation/drug effects/*geneticsen
dc.subjectHSP70 Heat-Shock Proteins/biosynthesis/metabolismen
dc.subjectHeat-Shock Response/drug effects/*geneticsen
dc.subjectHot Temperatureen
dc.subjectHumansen
dc.subjectI-kappa B Proteins/*metabolismen
dc.subjectNF-kappa B/genetics/*metabolism/pharmacologyen
dc.subject*Protein Renaturationen
dc.subjectRecombinant Proteins/metabolism/pharmacologyen
dc.subjectTime Factorsen
dc.subjectTransduction, Geneticen
dc.subjectUp-Regulationen
dc.titleHeat shock protein 70 negatively regulates the heat-shock-induced suppression of the IkappaB/NF-kappaB cascade by facilitating IkappaB kinase renaturation and blocking its further denaturationen
dc.typeArticleen
dc.contributor.AlternativeAuthor이경희-
dc.contributor.AlternativeAuthor이춘택-
dc.contributor.AlternativeAuthor김영환-
dc.contributor.AlternativeAuthor한성구-
dc.contributor.AlternativeAuthor심영수-
dc.contributor.AlternativeAuthor유철규-
dc.identifier.doi10.1016/j.yexcr.2005.03.014-
Appears in Collections:
College of Medicine/School of Medicine (의과대학/대학원)Immunology (면역학전공)Journal Papers (저널논문_면역학전공)
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