Cited by 2,212Glutathione Transferases and PolymorphismsRedox biology and oxidative stressTrace Elements in Health

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Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression

Zelko, Igor N, Mariani, Thomas J, Folz, Rodney J·2002·Free Radical Biology and Medicine

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Abstract

Superoxide dismutases are an ubiquitous family of enzymes that function to efficiently catalyze the dismutation of superoxide anions. Three unique and highly compartmentalized mammalian superoxide dismutases have been biochemically and molecularly characterized to date. SOD1, or CuZn-SOD (EC 1.15.1.1), was the first enzyme to be characterized and is a copper and zinc-containing homodimer that is found almost exclusively in intracellular cytoplasmic spaces. SOD2, or Mn-SOD (EC 1.15.1.1), exists as a tetramer and is initially synthesized containing a leader peptide, which targets this manganese-containing enzyme exclusively to the mitochondrial spaces. SOD3, or EC-SOD (EC 1.15.1.1), is the most recently characterized SOD, exists as a copper and zinc-containing tetramer, and is synthesized containing a signal peptide that directs this enzyme exclusively to extracellular spaces. What role(s) these SODs play in both normal and disease states is only slowly beginning to be understood. A molecular understanding of each of these genes has proven useful toward the deciphering of their biological roles. For example, a variety of single amino acid mutations in SOD1 have been linked to familial amyotrophic lateral sclerosis. Knocking out the SOD2 gene in mice results in a lethal cardiomyopathy. A single amino acid mutation in human SOD3 is associated with 10 to 30-fold increases in serum SOD3 levels. As more information is obtained, further insights will be gained.

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Self-citation

Authors: Zelko, I. N., Mariani, T. J., & Folz, R. J.
Affiliations: Duke University (US)
Brigham and Women's Hospital (US)
Corresponding author: Folz, Rodney J
ORCID: Zelko, Igor N
Mariani, Thomas J
Folz, Rodney J
Venue: Free Radical Biology and Medicine
Publisher: Elsevier BV
Published: 2002-08
Volume: 33
Issue: 3
Pages: 337-349
ISSN: 0891-5849 (ISSN-L)
DOI: 10.1016/s0891-5849(02)00905-x
OpenAlex: W2104109524
Cited by: 2,212
References: 162
Citations by year: 2026: 77 · 2025: 123 · 2024: 119 · 2023: 109 · 2022: 131 · 2021: 140 · 2020: 117 · 2019: 130 · 2018: 134 · 2017: 133 · 2016: 124 · 2015: 93 · 2014: 103 · 2013: 99 · 2012: 104
FWCI: 12.55
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Free Radical Biology and Medicine (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01hl055166-04)
National Heart, Lung, and Blood Institute (HL55166, P01HL031992, HL 31992)
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: superoxide dismutase, SOD1, manganese superoxide dismutase, SOD3, gene structure, gene evolution, gene expression, SOD1 mutations, amyotrophic lateral sclerosis, superoxide dismutase isoforms
MeSH terms: Animals, Multigene Family, Humans, Superoxide Dismutase, Gene Expression Regulation, Enzymologic, Evolution, Molecular

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Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression

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