Copper,zinc superoxide dismutase is primarily a cytosolic protein in human cells.
Open accessAbstract
The intracellular localization of human copper,zinc superoxide dismutase (Cu,Zn-SOD; superoxide:superoxide oxidoreductase, EC 1.15.1.1) was evaluated by using EM immunocytochemistry and both isolated human cell lines and human tissues. Eight monoclonal antibodies raised against either native or recombinant human Cu,Zn-SOD and two polyclonal antibodies raised against either native or recombinant human Cu,Zn-SOD were used. Fixation with 2% paraformaldehyde/0.2% glutaraldehyde was found necessary to preserve normal distribution of the protein. Monoclonal antibodies were less effective than polyclonal antibodies in recognizing the antigen after adequate fixation of tissue. Cu,Zn-SOD was found widely distributed in the cell cytosol and in the cell nucleus, consistent with it being a soluble cytosolic protein. Mitochondria and secretory compartments did not label for this protein. In human cells, peroxisomes showed a labeling density slightly less than that of cytoplasm.
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Cu,Zn-SOD is known to be increased as a response to certain therapies or in some diseases, therefore determination of activities of different SODs is necessary.
“Cu, Zn-SOD is known to be increased as a response to certain therapies or in some diseases therefore determination of activities of different SODs is necessary (Crapo et al. 1992).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Crapo et al. 1992
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- Authors
- Crapo, J. D., Oury, T., Rabouille, C., Slot, J. W., & Chang, L. Y.
- Affiliations
- Duke Medical Center (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1992-11
- Volume
- 89
- Issue
- 21
- Pages
- 10405-10409
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC50347
- OpenAlex
- W2042662902
- Cited by
- 503
- References
- 12
- Citations by year
- 2026: 8 · 2025: 8 · 2024: 12 · 2023: 12 · 2022: 21 · 2021: 15 · 2020: 21 · 2019: 12 · 2018: 14 · 2017: 13 · 2016: 28 · 2015: 17 · 2014: 19 · 2013: 17 · 2012: 20
- FWCI
- 2.12
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01hl042609-08)
- National Heart, Lung, and Blood Institute (R01 HL42609, P01HL031992, P01-HL 31992)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- copper-zinc superoxide dismutase, subcellular localization, cytosol, nuclear localization, peroxisomes, mitochondria, monoclonal antibodies, polyclonal antibodies, paraformaldehyde fixation, human cell lines, human tissue
- MeSH terms
- Aged, Animals, Antibodies, Carcinoma, Cytosol, Fibroblasts, Carcinoma, Hepatocellular, Humans, Isoenzymes, Liver Neoplasms, Lung, Lung Neoplasms, Male, Recombinant Proteins, Superoxide Dismutase, Tumor Cells, Cultured, Microscopy, Immunoelectron, Rats
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