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NF-kappaB p65 regulates nuclear translocation of Ku70 via degradation of heat shock cognate protein 70 in pancreatic acinar AR42J cells.

Authors
 Joo Weon Lim  ;  Kyung Hwan Kim  ;  Hyeyoung Kim 
Citation
 INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, Vol.40(10) : 2065-2077, 2008 
Journal Title
 INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY 
ISSN
 1357-2725 
Issue Date
2008
MeSH
Animals ; Antigens, Nuclear/metabolism* ; Cell Line ; Cell Nucleus/drug effects ; Cell Nucleus/metabolism* ; Cell Proliferation/drug effects ; Ceruletide/pharmacology ; DNA-Binding Proteins/metabolism* ; Down-Regulation/drug effects ; HSC70 Heat-Shock Proteins/chemistry ; HSC70 Heat-Shock Proteins/metabolism* ; Ku Autoantigen ; Nuclear Localization Signals/metabolism ; Pancreas, Exocrine/cytology* ; Pancreas, Exocrine/metabolism* ; Protein Binding/drug effects ; Protein Processing, Post-Translational*/drug effects ; Protein Structure, Tertiary ; Protein Transport/drug effects ; Rats ; Transcription Factor RelA/metabolism* ; Transfection ; alpha Karyopherins/metabolism
Keywords
NF-κB p65 ; Ku70 ; Heat shock cognate protein 70 ; Pancreatic acinar cells
Abstract
Ku proteins such as Ku70 and Ku80 play key roles in multiple nuclear processes. Nuclear translocation of Ku70 is independent of Ku80 translocation and mediated by nuclear localization signal (NLS) receptors including importin-alpha. In the present study using pancreatic acinar AR42J cells, heat shock cognate protein 70 (Hsc70) was identified as the protein associated with NLS of Ku70. Interaction of Ku70 with importin-alpha and nuclear translocation of Ku70 was suppressed by overexpression of Hsc70, but enhanced by downregulation of Hsc70. The results suggest that the formation of Ku70 complex with Hsc70 prevents NLS of Ku70 from access of importin-alpha and inhibits nuclear translocation of Ku70. Since NF-kappaB p65 activation induced the decrease of Hsc70 level, the interaction of Ku70 with importin-alpha and nuclear translocation of Ku70 increased upon the activation of NF-kappaB p65. NF-kappaB p65 induced cell proliferation through decrease of Hsc70 levels and increase of nuclear translocation of Ku70. In the cells treated with cerulein as a physiological stimulus to activate NF-kappaB p65, nuclear translocation of Ku70 increased through NF-kappaB p65-mediated decrease of Hsc70 level. The results suggest that the involvement of NF-kappaB p65 in nuclear translocation of Ku70 may be mediated by Hsc70 degradation, which may play a key role in cell proliferation of pancreatic acinar AR42J cells.
Full Text
http://www.sciencedirect.com/science/article/pii/S1357272508000721
DOI
10.1016/j.biocel.2008.02.015
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Pharmacology (약리학교실) > 1. Journal Papers
5. Research Institutes (연구소) > Institute of Gastroenterology (소화기병연구소) > 1. Journal Papers
Yonsei Authors
Kim, Kyung Hwan(김경환)
Lim, Joo Weon(임주원)
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/106124
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