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Cited by 280

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Antioxidant protection by haemopexin of haem-stimulated lipid peroxidation

Open access
Gutteridge, J M, Smith, A·1988·Biochemical Journal
DOI 10.1042/bj2560861
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Abstract

Haem (ferrous protoporphyrin IX) is a reactive low-molecular-mass form of iron able to participate in oxygen-radical reactions that can lead to the degradation of proteins, lipids, carbohydrates and DNA. Oxygen-radical reactions are likely to occur upon tissue damage. Extracellular fluids rely on antioxidant mechanisms different from those found inside the cell, and circulating proteins limit radical reactions by converting pro-oxidant forms of iron into less-reactive forms. Of the compounds tested, only apohaemopexin and the chain-breaking antioxidant butylated hydroxytoluene inhibited (by more than 90%) haemin-stimulated peroxidation as measured by formation of conjugated dienes, thiobarbituric acid-reactive material from linolenic acid or peroxidation-induced phospholipid fluorescence. Haptoglobin, the haemoglobin-binding serum protein, was ineffective. Conversely, only haptoglobin significantly inhibited haemoglobin-stimulated lipid peroxidation. Iron-salt-induced lipid peroxidation was inhibited only by apotransferrin and the iron-chelator desferrioxamine. All lipid peroxidations were inhibited by the radical scavengers butylated hydroxytoluene and propyl gallate. These findings support the concept that transport and conservation of body iron stores are closely linked to antioxidant protection.

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Metadata

Authors
Gutteridge, J. M., & Smith, A.
Venue
Biochemical Journal
Publisher
Portland Press Ltd.
Published
1988-12-15
Volume
256
Issue
3
Pages
861-865
ISSN
  • 0264-6021 (ISSN-L)
  • 1470-8728
DOI
10.1042/bj2560861
OpenAlex
W1891909707
Cited by
280
References
0
FWCI
2.71
Type
journal article
Language
en
Open access
green

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