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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

Cited 20 time in Web of Science Cited 20 time in Scopus
Authors
Lee, K. H.; Lee, C. T.; Kim, Y. W.; Han, S. K.; Shim, Y. S.; Yoo, C. G.
Issue Date
2005-06-01
Publisher
Elsevier
Citation
Exp Cell Res. 2005 Jul 1;307(1):276-84. Epub 2005 Apr 13.
Keywords
Adenoviridae/geneticsBlotting, WesternBronchi/cytologyCell Culture TechniquesCell LineElectrophoretic Mobility Shift AssayEnzyme ActivationEpithelial Cells/cytologyGene Expression Regulation/drug effects/*geneticsHSP70 Heat-Shock Proteins/biosynthesis/metabolismHeat-Shock Response/drug effects/*geneticsHot TemperatureHumansI-kappa B Proteins/*metabolismNF-kappa B/genetics/*metabolism/pharmacology*Protein RenaturationRecombinant Proteins/metabolism/pharmacologyTime FactorsTransduction, GeneticUp-Regulation
Abstract
Heat 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.
ISSN
0014-4827 (Print)
Language
English
URI
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15922746

http://hdl.handle.net/10371/22618
DOI
https://doi.org/10.1016/j.yexcr.2005.03.014
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College of Medicine/School of Medicine (의과대학/대학원)Immunology (면역학전공)Journal Papers (저널논문_면역학전공)
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