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 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
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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.
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
Author_xml – sequence: 1
  givenname: Tomomi
  surname: Ookawara
  fullname: Ookawara, Tomomi
  organization: Department of Biochemistry, Hyogo College of Medicine, Nishinomiya, Hyogo 663-8501, Japan
– sequence: 2
  givenname: Takako
  surname: Kizaki
  fullname: Kizaki, Takako
  organization: Department of Molecular Preventive Medicine and Sport Science, Kyorin University, School of Medicine, Mitaka, Tokyo 181-8611, Japan
– sequence: 3
  givenname: Eiji
  surname: Takayama
  fullname: Takayama, Eiji
  organization: Departments of Parasitology, National Defense Medical College, Tokorozawa, Saitama 359-8513, Japan
– sequence: 4
  givenname: Nobuo
  surname: Imazeki
  fullname: Imazeki, Nobuo
  organization: Departments of Pathology II, National Defense Medical College, Tokorozawa, Saitama 359-8513, Japan
– sequence: 5
  givenname: Osamu
  surname: Matsubara
  fullname: Matsubara, Osamu
  organization: Departments of Pathology II, National Defense Medical College, Tokorozawa, Saitama 359-8513, Japan
– sequence: 6
  givenname: Yoshitaka
  surname: Ikeda
  fullname: Ikeda, Yoshitaka
  organization: Department of Biochemistry, Osaka University Medical School, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan
– sequence: 7
  givenname: Keiichiro
  surname: Suzuki
  fullname: Suzuki, Keiichiro
  organization: Department of Biochemistry, Hyogo College of Medicine, Nishinomiya, Hyogo 663-8501, Japan
– sequence: 8
  givenname: Li
  surname: Li Ji
  fullname: Li Ji, Li
  organization: Department of Kinesiology, School of Education, University of Wisconsin Madison, Madison, WI 53706-1189, USA
– sequence: 9
  givenname: Takushi
  surname: Tadakuma
  fullname: Tadakuma, Takushi
  organization: Departments of Parasitology, National Defense Medical College, Tokorozawa, Saitama 359-8513, Japan
– sequence: 10
  givenname: Naoyuki
  surname: Taniguchi
  fullname: Taniguchi, Naoyuki
  email: proftani@biochem.med.osaka-u.ac.jp
  organization: Department of Biochemistry, Osaka University Medical School, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan
– sequence: 11
  givenname: Hideki
  surname: Ohno
  fullname: Ohno, Hideki
  organization: Department of Molecular Preventive Medicine and Sport Science, Kyorin University, School of Medicine, Mitaka, Tokyo 181-8611, Japan
BackLink https://www.ncbi.nlm.nih.gov/pubmed/12147226$$D View this record in MEDLINE/PubMed
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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
URI https://dx.doi.org/10.1016/S0006-291X(02)00804-5
https://www.ncbi.nlm.nih.gov/pubmed/12147226
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