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PMID: 3003078 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Inhibition of erythrocyte superoxide dismutase by diethyldithiocarbamate also results in oxyhemoglobin-catalyzed glutathione depletion and methemoglobin production.

The Journal of biological chemistry ·Vol. 261 ·No. 4 ·1986-02-05 ·Pages 1636-41

Kelner MJ, Alexander NM

Abstract

N,N-Diethyldithiocarbamate (DDC), a copper-chelating agent, not only inhibits superoxide dismutase activity in the red cell, but also depletes glutathione and promotes the production of methemoglobin, sulfhemoglobin, and small amounts of lipid peroxidation products. DDC reacts with oxyhemoglobin to yield disulfiram, hydrogen peroxide, and methemoglobin. Disulfiram and hydrogen peroxide both convert GSH to GSSG, while DDC reduces methemoglobin to oxyhemoglobin. Although disulfiram also reacts with the hemoglobin sulfhydryl groups, this reaction does not play a role in the conversion of GSH to GSSG. Other hemoglobin derivatives, ferrous, and ferric ions do not catalyze the oxidation of GSH by DDC. These results support the conclusion that DDC reacts with the super-oxo-ferriheme complex of oxyhemoglobin to generate hydrogen peroxide and disulfiram and that the cyclic conversion of oxyhemoglobin to methemoglobin and DDC and disulfiram results in the net oxidation of GSH. Thus, damage to DDC-treated erythrocytes exposed to a putative superoxide-generating toxin, such as 1,4-naphthoquinone-2-sulfonate, may actually be due to diminished GSH concentration and hemoglobin oxidation rather than to superoxide radicals. Glucose added to the incubation medium of DDC-treated erythrocytes fully prevented glutathione depletion but not the oxidation of oxyhemoglobin to methemoglobin. Several other copper-chelating agents either failed to inhibit the activity of purified superoxide dismutase or when incubated with erythrocytes produced more extensive GSH depletion and hemoglobin oxidation than DDC. It is concluded that the interpretation of results with erythrocytes exposed to copper-chelating agents must consider their effects on GSH and hemoglobin as well as on superoxide dismutase inhibition. Moreover, one must be mindful of the interference by DDC in the analysis of GSH with 5,5'-dithiobis-(2-nitrobenzoic acid) in the absence of sufficient quantities of metaphosphoric acid to destroy DDC and that contamination of DDC with trace quantities of disulfiram may be a significant problem.

MeSH Terms
Copper/metabolism Disulfiram/biosynthesis Dithionitrobenzoic Acid/metabolism Ditiocarb/pharmacology Erythrocytes/metabolism Glutathione/metabolism Humans Hydrogen Peroxide/biosynthesis Lipid Peroxides/biosynthesis Methemoglobin/biosynthesis Oxidation-Reduction Oxyhemoglobins/metabolism Superoxide Dismutase/antagonists & inhibitors Thiocarbamates/pharmacology
Chemicals
Lipid Peroxides Oxyhemoglobins Thiocarbamates Copper Methemoglobin Ditiocarb Dithionitrobenzoic Acid Hydrogen Peroxide Superoxide Dismutase Glutathione Disulfiram
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Kelner M J
Alexander N M
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1986-02-05
Pages
1636-41
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NIEHS NIH HHS · ES 00142-01 · United States
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