Biochemical and Biophysical Research Communications, Vol.291, No.3, 550-553, 2002
Ebselen has dehydroascorbate reductase and thioltransferase-like activities
Ebselen (2-phenyl-1,2-benzisoselenazol-3(2H)-one), a seleno-organic compound, has been reported to mimic glutathione peroxidase (GPX). Since bovine erythrocyte GPX showed dehydroascorbic acid (DHA) reductase and thioltransferase (TTase) activities, ebselen was also examined for DHA reductase and TTase-like activities. Evidence is reported that, in the presence of GSH, ebselen catalyzed the in vitro reduction of DHA to L-ascorbic acid in a dose-dependent manner. Using S-sulfocysteine and GSH as co-substrates, ebselen catalyzed the in vitro formation of glutathione disulfide in a dose-dependent manner, thereby acting as a TTase mimic. 1-Chloro-2,4-dinitrobezene (CDNB), a co-substrate with GSH for glutathione S-transferase, was used to measure rates of adduct formation with ebselen pretreated with GSH and compared with GSH alone. The reaction rate was proportional to ebselen, and ebselen was about 250 times more reactive than GSH on an equimolar basis. The DHA reductase and TTase-like activities, in addition to the powerful nucleophilic reactivity of ebselen selenol, may contribute to ebselen's significant anti-inflammatory and anti-oxidative properties in vivo. (C) 2002 Elsevier Science (USA).