4.4 Article

Diphenyl diselenide in its selenol form has dehydroascorbate reductase and glutathione S-transferase-like activity dependent on the glutathione content

Journal

JOURNAL OF PHARMACY AND PHARMACOLOGY
Volume 62, Issue 9, Pages 1146-1151

Publisher

WILEY-BLACKWELL
DOI: 10.1111/j.2042-7158.2010.01147.x

Keywords

antioxidant; dehydroascorbate reductase-like; diphenyl diselenide; glutathione s-transferase-like; selenium; organoselenium

Funding

  1. FAPERGS
  2. CAPES
  3. CNPq

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Objectives The antioxidant action of diphenyl diselenide ((PhSe)(2)) is attributed to the mechanism by which (PhSe)(2) has pharmacological activity. Although (PhSe)(2) has glutathione peroxidase mimetic activity, the exact mechanism involved in its antioxidant effect has not yet been completely elucidated. In the present study, mechanisms involved in the antioxidant property of (PhSe)(2) (1-50 mu m) were investigated. Methods Dehydroascorbate (DHA) reductase- and glutathione S-transferase (GST)-like activity, 2,2'-diphenyl-1-picrylhydrazyl (DPPH) and 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) radical-scavenging activity and the protection against the oxidation of Fe2+ were evaluated. Key findings (PhSe)(2) at concentrations equal to, or greater than, 5 mu m showed DHA reductase- and GST-like activity. (PhSe)(2) was not a scavenger of DPPH or ABTS radicals and did not protect against the oxidation of Fe2+. Conclusions These results clearly indicated that DHA reductase- and GST-like activity are the mechanisms involved in the antioxidant effect of (PhSe)(2).

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