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Antioxidant protection against organic and inorganic oxygen radicals by normal human plasma: the important primary role for iron-binding and iron-oxidising proteins
Abstract
Normal human plasma contains numerous high- and low-molecular-mass redox-active molecules that are able to react rapidly with organic and inorganic oxygen radicals. The ability of such plasma molecules to substantially inhibit, or delay, free-radical mediated oxidation of added substrates has led to their classification as important biological antioxidants. Using phospholipids to detect organic oxygen radicals and deoxyribose to detect inorganic oxygen radicals, we here show that the primary antioxidants of normal human plasma reside mainly in two plasma proteins representing no more than 4% of the total proteins present. The iron-binding properties of transferrin and the iron-oxidising properties of caeruloplasmin, at a reaction dilution of 1:50, offer considerable protection against organic and inorganic oxygen radicals generated by iron and ascorbate. Plasma thiol-group-containing molecules, at concentrations well below those that would be required to compete with the detector molecule (based on known second-order rate constants for reaction with hydroxyl radicals) inhibited damage to deoxyribose, but stimulated damage to phospholipids.
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“Fpn and Heph colocalize on the basolateral membrane of absorptive enterocytes of the duodenum and intestines (121).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [121]
Citations
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Halliwell, B. B., Aeschbach, R., Löliger, J., & Aruoma, O. I. (1995) · Food and Chemical Toxicology · doi:10.1016/0278-6915(95)00024-v · Cited by 993
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Self-citation
Metadata
- Authors
- Gutteridge, J. M. C., & Quinlan, G. J.
- Affiliations
- Royal Brompton Hospital (GB)
- Corresponding author
- Gutteridge, John M.C.
- ORCID
- Quinlan, Gregory J.
- Venue
- Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Publisher
- Elsevier BV
- Published
- 1992-10
- Volume
- 1159
- Issue
- 3
- Pages
- 248-254
- ISSN
- 0167-4838 (ISSN-L)
- OpenAlex
- W2026312693
- Cited by
- 148
- References
- 46
- Citations by year
- 2024: 1 · 2023: 3 · 2021: 3 · 2020: 1 · 2017: 1 · 2015: 1 · 2014: 4 · 2013: 5 · 2012: 4
- FWCI
- 5.92
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology (publishedVersion)
- PubMed (publishedVersion)
- PubMed
- Funders
- British Lung Foundation
- Topics
- Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
- Physical Sciences › Chemistry › Organic Chemistry › Free Radicals and Antioxidants
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- plasma antioxidants, oxygen free radicals, hydroxyl radicals, superoxide, transferrin, ceruloplasmin, iron-binding proteins, phospholipid oxidation, deoxyribose oxidation, vitamin C, sulfhydryl groups, human plasma
- MeSH terms
- Antioxidants, Blood Proteins, Carrier Proteins, Humans, Hydroxides, Iron, Plasma, Free Radical Scavengers, Hydroxyl Radical, Iron-Binding Proteins, Transferrin-Binding Proteins, In Vitro Techniques
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