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-...
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Published in | Biochemical and biophysical research communications Vol. 296; no. 1; pp. 54 - 61 |
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Main Authors | , , , , , , , , , , |
Format | Journal Article |
Language | English |
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United States
Elsevier Inc
09.08.2002
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Abstract | 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. |
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AbstractList | 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. |
Author | Imazeki, Nobuo Ookawara, Tomomi Suzuki, Keiichiro Ikeda, Yoshitaka Li Ji, Li Matsubara, Osamu Kizaki, Takako Ohno, Hideki Takayama, Eiji Taniguchi, Naoyuki Tadakuma, Takushi |
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Keywords | Nuclear localization signal Extracellular superoxide dismutase Heparin binding domain Secretion ROS |
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Snippet | Histochemical examination of mouse tissues showed nuclear staining of extracellular superoxide dismutase (EC-SOD), and the nuclear translocation of EC-SOD was... |
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SubjectTerms | 3T3 Cells Animals Blotting, Western Cell Nucleus - metabolism COS Cells Extracellular superoxide dismutase Heparin - metabolism Heparin binding domain Immunohistochemistry Mice Nuclear localization signal Nuclear Localization Signals Plasmids Protein Transport ROS Secretion Superoxide Dismutase - chemistry Superoxide Dismutase - genetics Superoxide Dismutase - metabolism |
Title | Nuclear translocation of extracellular superoxide dismutase |
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