Superoxide-dependent and -independent mechanisms of iron mobilization from ferritin by xanthine oxidase. Implications for oxygen-free-radical-induced tissue destruction during ischaemia and inflammation
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Xanthine oxidase is able to mobilize iron from ferritin. This mobilization can be blocked by 70% by superoxide dismutase, indicating that part of its action is mediated by superoxide (O2-). Uric acid induced the release of ferritin iron at concentrations normally found in serum. The O2(-)-independent mobilization of ferritin iron by xanthine oxidase cannot be attributed to uric acid, because uricase did not influence the O2(-)-independent part and acetaldehyde, a substrate for xanthine oxidase, also revealed an O2(-)-independent part, although no uric acid was produced. Presumably the amount of uric acid produced by xanthine oxidase and xanthine is insufficient to release a measurable amount of iron from ferritin. The liberation of iron from ferritin by xanthine oxidase has important consequences in ischaemia and inflammation. In these circumstances xanthine oxidase, formed from xanthine dehydrogenase, will stimulate the formation of a non-protein-bound iron pool, and the O2(-)-produced by xanthine oxidase, or granulocytes, will be converted by ‘free’ iron into much more highly toxic oxygen species such as hydroxyl radicals (OH.), exacerbating the tissue damage.
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A mechanism in RA involves elevated superoxide liberating free iron from ferritin in synovial fluid, thereby catalysing further damaging production of hydroxyl radicals.
“a mechanism [1256-1259] in which elevated superoxide liberates free iron from ferritin in synovial fluid (and elsewhere [1260]), thereby catalysing further the damaging production of hydroxyl radicals.”
From Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases (2009) · cites this paper as [1257]
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- Authors
- Biemond, P., Swaak, A. J. G., Beindorff, C. M., & Koster, J. F.
- Affiliations
- Daniel den Hoed Kliniek (NL)
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1986-10-01
- Volume
- 239
- Issue
- 1
- Pages
- 169-173
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1147255
- OpenAlex
- W2132632471
- Cited by
- 179
- References
- 34
- Citations by year
- 2024: 2 · 2022: 2 · 2021: 2 · 2019: 2 · 2018: 1 · 2017: 4 · 2016: 1 · 2015: 3 · 2014: 1 · 2013: 1 · 2012: 2
- FWCI
- 7.07
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- xanthine oxidase, ferritin, iron mobilization, superoxide, superoxide dismutase, uric acid, uricase, acetaldehyde, xanthine dehydrogenase, free iron, hydroxyl radicals, oxygen free radicals, ischemia, inflammation, tissue damage, granulocytes
- MeSH terms
- Ferritins, Free Radicals, Oxygen, Superoxides, Superoxide Dismutase, Urate Oxidase, Uric Acid, Xanthine Oxidase
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