The antioxidant properties of serum albumin
Abstract
Free radicals are a normal component of cellular oxygen metabolism in mammals. However, free radical‐associated damage is an important factor in many pathological processes. Glycation and oxidative damage cause protein modifications, frequently observed in numerous diseases. Albumin represents a very abundant and important circulating antioxidant. This review brings together recent insights on albumin antioxidant properties. First, it focuses on the different activities of albumin concerning protein antioxidation. In particular, we describe the role of albumin in ligand binding and free radical‐trapping activities. In addition, physiological and pathological situations that modify the antioxidant properties of albumin are reported.
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In the interstitium, albumin acts as the main extracellular scavenger, antioxidative agent, and supplier of amino acids for cell and matrix synthesis.
“In the interstitium, albumin acts as the main extracellular scavenger, antioxidative agent, and as supplier of amino acids for cell and matrix synthesis.”
From Hypoalbuminemia: Pathogenesis and Clinical Significance (2019) · cites this paper as [79]
In blood, serum albumin binds fatty acids, bilirubin, bile acids, calcium, iron, copper, zinc, and other cations, drugs, and tryptophan.
“In blood, serum albumin binds fatty acids; bilirubin; bile acids; calcium, iron (Fe), copper (Cu), zinc, and other cations; drugs; and tryptophan; for an extensive review, see Roche et al.79”
From Hypoalbuminemia: Pathogenesis and Clinical Significance (2019) · cites this paper as [79]
The breakdown of serum albumin is complicated by the fact that after oxidation, glycation, or binding of pro-oxidative substances, serum albumin loses its antioxidant capacity and is more rapidly degraded than reduced unbound serum albumin.
“The breakdown of serum albumin is complicated by the fact that after oxidation, glycation, or binding of pro‐oxidative substances, serum albumin loses its antioxidant capacity and is more rapidly degraded than reduced unbound serum albumin.79, 80, 81, 82, 83”
From Hypoalbuminemia: Pathogenesis and Clinical Significance (2019) · cites this paper as [79]
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- Authors
- Roche, M., Rondeau, P., Singh, N. R., Tarnus, E., & Bourdon, E.
- Affiliations
- University of Reunion Island (RE)
- Corresponding author
- Bourdon, Emmanuel
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2008-05-12
- Volume
- 582
- Issue
- 13
- Pages
- 1783-1787
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2007790334
- Cited by
- 1,255
- References
- 62
- Citations by year
- 2026: 97 · 2025: 86 · 2024: 109 · 2023: 91 · 2022: 114 · 2021: 90 · 2020: 76 · 2019: 58 · 2018: 83 · 2017: 60 · 2016: 70 · 2015: 54 · 2014: 61 · 2013: 54 · 2012: 48
- FWCI
- 2.65
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Physical Sciences › Chemistry › Organic Chemistry › Free Radicals and Antioxidants
- Keywords
- serum albumin, antioxidant activity, free radicals, oxidative damage, glycation, protein modification, ligand binding, free radical trapping, oxidative stress, pathological conditions
- MeSH terms
- Free Radicals, Humans, Ligands, Oxidation-Reduction, Serum Albumin, Free Radical Scavengers
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