Nuclear translocation of extracellular superoxide dismutase

Histochemical examination of mouse tissues showed nuclear staining of extracellular superoxide dismutase (EC-SOD), and the nuclear translocation of EC-SOD was also confirmed in cultured cells that had been transfected with its gene, as shown by immunohistochemistry and Western blot analysis. The EC-...

Full description

Saved in:
Bibliographic Details
Published inBiochemical and biophysical research communications Vol. 296; no. 1; pp. 54 - 61
Main Authors Ookawara, Tomomi, Kizaki, Takako, Takayama, Eiji, Imazeki, Nobuo, Matsubara, Osamu, Ikeda, Yoshitaka, Suzuki, Keiichiro, Li Ji, Li, Tadakuma, Takushi, Taniguchi, Naoyuki, Ohno, Hideki
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 09.08.2002
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary:Histochemical examination of mouse tissues showed nuclear staining of extracellular superoxide dismutase (EC-SOD), and the nuclear translocation of EC-SOD was also confirmed in cultured cells that had been transfected with its gene, as shown by immunohistochemistry and Western blot analysis. The EC-SOD which was secreted into the medium was incorporated into 3T3-L1 cells and a significant fraction of the material taken up was localized in the nucleus. Site-directed mutagenesis indicated that the heparin-binding domain of EC-SOD functions as the nuclear localization signal. These results suggest that the mechanism of the nuclear transport of EC-SOD involves a series of N-terminal signal peptide- and C-terminal heparin-binding domain-dependent processes of secretion, re-uptake and the subsequent nuclear translocation. The findings herein provide support for the view that the role of EC-SOD is to protect the genome DNA from damage by reactive oxygen species and/or the transcriptional regulation of redox-sensitive gene expression.
ISSN:0006-291X
1090-2104
DOI:10.1016/S0006-291X(02)00804-5