Extracellular superoxide dismutase and other superoxide dismutase isoenzymes in tissues from nine mammalian species
Open accessAbstract
The contents of extracellular superoxide dismutase, CuZn superoxide dismutase and Mn superoxide dismutase were determined in tissues from nine mammalian species. The pattern of CuZn superoxide dismutase distribution was similar in all species, with high activity in metabolically active organs such as liver and kidney and low activity in, for example, skeletal muscle. Mn superoxide dismutase activity was high in organs with high respiration, such as liver, kidney, and myocardium. Overall the Mn superoxide dismutase activity in organs was almost as high as the CuZn superoxide dismutase activity. The content of extracellular superoxide dismutase was, almost without exception, lower than the content of the other isoenzymes. The pattern of tissue distribution was distinctly different from those of CuZn superoxide dismutase and Mn superoxide dismutase. The tissue distribution of extracellular superoxide dismutase differed among species, but in general there was much in lungs and kidneys and little in skeletal muscle. In man, pig, sheep, cow, rabbit and mouse the overall tissue extracellular superoxide dismutase activities were similar to each other, whereas dog, cat and rat tissues contained distinctly less. There was no general correlation between the tissue extracellular superoxide dismutase activity of any of the various species and the variable plasma activity. The ratio between the plasma and the overall tissue activities was high, for some species over unity, providing further evidence for the notion that one role of extracellular superoxide dismutase is as a plasma protein.
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There is one more, called SOD3 or EC-SOD, located outside the cell (in the extracellular matrix), and has copper and zinc and is the only extracellular protein that can remove O2•.
“Finally, there is one more, called SOD3 or EC-SOD [73], located outside the cell (in the extracellular matrix), and has copper and zinc and is the only extracellular protein that can remove O2•.”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [73]
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Self-citation
- Authors
- Marklund, S. L.
- Affiliations
- University Hospital of Umeå (SE)
- Corresponding author
- Marklund, S L
- ORCID
- Marklund, S L
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1984-09-15
- Volume
- 222
- Issue
- 3
- Pages
- 649-655
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1144226
- OpenAlex
- W1802861244
- Cited by
- 518
- References
- 18
- Citations by year
- 2026: 10 · 2025: 9 · 2024: 10 · 2023: 8 · 2022: 20 · 2021: 20 · 2020: 7 · 2019: 18 · 2018: 10 · 2017: 11 · 2016: 6 · 2015: 5 · 2014: 9 · 2013: 8 · 2012: 16
- FWCI
- 2.73
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Cancerfonden
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Keywords
- extracellular superoxide dismutase, Cu/Zn superoxide dismutase, Mn superoxide dismutase, tissue distribution, cross-species comparison, mammalian tissues, respiratory system, liver, kidney, myocardium, skeletal muscle
- MeSH terms
- Animals, Cats, Cattle, Chromatography, Gel, Dogs, Extracellular Space, Humans, Isoenzymes, Rabbits, Sheep, Species Specificity, Superoxide Dismutase, Swine, Tissue Distribution, Mice, Rats
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