| First Author | Ookawara T | Year | 2002 |
| Journal | Biochem Biophys Res Commun | Volume | 296 |
| Issue | 1 | Pages | 54-61 |
| PubMed ID | 12147226 | Mgi Jnum | J:78880 |
| Mgi Id | MGI:2386423 | Doi | 10.1016/s0006-291x(02)00804-5 |
| Citation | Ookawara T, et al. (2002) Nuclear translocation of extracellular superoxide dismutase. Biochem Biophys Res Commun 296(1):54-61 |
| abstractText | 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. |
