ArticleHistochemistry and cell biology2013
Mammalian SOD2 is exclusively located in mitochondria and not present in peroxisomes.
Article in Histochemistry and cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 88 citations in OpenAlex.
- Peroxisomal catalase and plasmalogen biosynthesis protect from oxidative stress in Barth syndrome cardiomyopathy.Basic research in cardiology · 2026Article
- Postbiotics From Ligilactobacillus salivarius Enhance Mitochondrial Robustness Via TLR2 Signaling in Intestinal Macrophages.Probiotics and antimicrobial proteins · 2026Article
- The regulation of mitochondrial ferritin on mitochondrial redox balance is essential to cell fate decision.Redox biology · 2026Review
- Assessing the Association Between Genetic Variants in ACE, SOD1, and PER3 and their Role in Breast Cancer Risk among Jordanian Women.Journal of Cancer · 2026Article
- Investigating the Therapeutic Potential of miRNA-137-3p/383-5p/PGC-1α Signalling Nexus Against Cardiac Hypertrophy.Journal of cardiovascular translational research · 2025Article
- The Role of Reactive Oxygen Species (ROS) in Periodontitis: A Potential Therapeutic Target.Immunity, inflammation and disease · 2025Review
- Manganese Superoxide Dismutase: Structure, Function, and Implications in Human Disease.Antioxidants (Basel, Switzerland) · 2025Review
- Facts, Dogmas, and Unknowns About Mitochondrial Reactive Oxygen Species in Cancer.Antioxidants (Basel, Switzerland) · 2024Review
- MnSOD Mimetics in Therapy: Exploring Their Role in Combating Oxidative Stress-Related Diseases.Antioxidants (Basel, Switzerland) · 2024Review
- Mitochondrial SIRT3 as a protective factor against cyclosporine A-induced nephrotoxicity.Scientific reports · 2024Article
- Palm-based tocotrienol-rich fraction (TRF) supplementation modulates cardiac sod1 expression, fxr target gene expression, and tauro-conjugated bile acid levels in aleptinemic mice fed a high-fat diet.Genes & nutrition · 2024Article
- Association of a single nucleotide polymorphism in SOD2 with susceptibility for the development of diabetic nephropathy in patients with type 2 diabetes: A Saudi population study.Endocrinology, diabetes & metabolism · 2023Article
- Sex and age differences in AMPK phosphorylation, mitochondrial homeostasis, and inflammation in hearts from inflammatory cardiomyopathy patients.Aging cell · 2023Article
- Rewiring of mitochondrial metabolism in therapy-resistant cancers: permanent and plastic adaptations.Frontiers in cell and developmental biology · 2023Review
- The complex role of inflammation and gliotransmitters in Parkinson's disease.Neurobiology of disease · 2023Review
- S-Glutathionylation and S-Nitrosylation in Mitochondria: Focus on Homeostasis and Neurodegenerative Diseases.International journal of molecular sciences · 2022Review
- The Potential of the Mediterranean Diet to Improve Mitochondrial Function in Experimental Models of Obesity and Metabolic Syndrome.Nutrients · 2022Review
- Article
- Insights Into the Peroxisomal Protein Inventory of Zebrafish.Frontiers in physiology · 2022Article
- CD34+ derived macrophage and dendritic cells display differential responses to paraquat.Toxicology in vitro : an international journal published in association with BIBRA · 2021Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Superoxide dismutases (SODs) are metalloenzymes that belong to the essential antioxidant enzyme systems of virtually all oxygen-respiring organisms. SODs catalyze the dismutation of highly reactive superoxide radicals into hydrogen peroxide and molecular oxygen. For the subcellular localization of the manganese superoxide dismutase (SOD2) in eukaryotic cells, a dual mitochondrial localization and peroxisomal localization were proposed in the literature. However, our own observation from immunofluorescence preparations of human and mouse tissues suggested that SOD2 serves as an excellent marker protein for mitochondria but never co-localized with peroxisomes. To clarify whether our observations were correct, we have carefully reinvestigated the subcellular localization of SOD2 using sensitive double-immunofluorescence methods on frozen and paraffin sections as well as in cell culture preparations. In addition, ultrastructural analyses were performed with post-embedding immunoelectron microscopy on LR White sections as well as labeling of ultrathin cryosections with various immunogold techniques. In all morphological experiments, the SOD2 localization was compared to one of the catalase, a typical marker protein for peroxisomes, solely localized in these organelles. Moreover, biochemical subcellular fractions of mouse liver was used to isolate enriched organelles and highly purified peroxisomal fractions for Western blot analyses of the exact subcellular distributions of SOD2 and catalase. All results with the various methodologies, tissues, and cell types used revealed that catalase and SOD2 were always confined to distinct and separate subcellular compartments. SOD2 was unequivocally in mitochondria, but never present in peroxisomes. Furthermore, our results are supported by accumulating database information on organelle proteomes that also indicate that SOD2 is a pure mitochondrial protein.
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