Publications
Detailed Information
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 21 time in
Web of Science
Cited 21 time in Scopus
- Authors
- Issue Date
- 2005-06-01
- Publisher
- Elsevier
- Citation
- Exp Cell Res. 2005 Jul 1;307(1):276-84. Epub 2005 Apr 13.
- Keywords
- Adenoviridae/genetics ; Blotting, Western ; Bronchi/cytology ; Cell Culture Techniques ; Cell Line ; Electrophoretic Mobility Shift Assay ; Enzyme Activation ; Epithelial Cells/cytology ; Gene Expression Regulation/drug effects/*genetics ; HSP70 Heat-Shock Proteins/biosynthesis/metabolism ; Heat-Shock Response/drug effects/*genetics ; Hot Temperature ; Humans ; I-kappa B Proteins/*metabolism ; NF-kappa B/genetics/*metabolism/pharmacology ; Recombinant Proteins/metabolism/pharmacology ; Time Factors ; Transduction, Genetic ; Up-Regulation ; Protein Renaturation
- 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
https://hdl.handle.net/10371/22618
- Files in This Item:
- There are no files associated with this item.
- Appears in Collections:
Item View & Download Count
Items in S-Space are protected by copyright, with all rights reserved, unless otherwise indicated.