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Studies on the mechanism of toxicity of the mycotoxin sporidesmin. 2—evidence for intracellular generation of superoxide radical from sporidesmin

✍ Scribed by R. Munday

Publisher
John Wiley and Sons
Year
1984
Tongue
English
Weight
546 KB
Volume
4
Category
Article
ISSN
0260-437X

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✦ Synopsis

Formation of hydrogen peroxide, the dismutation product of superoxide radical, has been demonstrated in erythrocytes incubated with the mycotoxin sporidesmin. Erythrocytic thiols, both non-protein and protein-bound, were depleted in the presence of sporidesmin, whilst haemoglobin was oxidized to methaemoglobin. Irreversible haemoglobin oxidation also occurred in these cells, shown by the formation of Heinz bodies; purified haemoglobin likewise suffered oxidative damage when incubated with sporidesmin in the presence of glutathione. Sporidesmin has previously been shown to generate superoxide radical in vitro; the erythrocytic changes induced by the mycotoxin, which are characteristically produced by compounds which generate 'active oxygen' species, suggest that it is also capable of generating this radical intracellularly.

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## Abstract The mycotoxin sporidesmin has previously been shown to generate superoxide radical. This reaction involves autoxidation of the reduced form of the mycotoxin, a dithiol. In the present study, a number of mercaptide‐forming metals have been shown to inhibit superoxide formation from spori