ARS | Publication request: AUROTHIOGLUCOSE INHIBITION OF THIOREDOXIN REDUCTASE AND GLUTATHIONE PEROXIDASE

Submitted to: Experimental Biology
Publication Type: Abstract Only
Publication Acceptance Date: March 31, 2001
Publication Date: N/A

Technical Abstract: Aurothioglucose (ATG) is a potent inhibitor of selenoproteins. The effects of ATG on thioredoxin reductase (TR) and glutathione peroxidase (GSH-Px) activity were studied in 84 male weanling, Fisher 344 rats. Rats were fed a selenium adequate diet (0.1 mg/kg) for eight weeks then injected with ATG in amounts of 0.05, 0.025, 0.01, 0.005 or 0 mg ATG/g bodyweight (BW) and killed at either 2, 48, 168 or 336 h post-injection. GSH-Px activity was most sensitive to ATG inhibition in the kidney and liver, whereas TR inhibition was greatest in kidney, followed by the muscle and liver. Preliminary analysis of western blots indicates that ATG has a minimal effect on TR protein concentrations. These data indicate that ATG inhibits TR and GSH-Px activity in a manner dependent on dose and target tissue, but total protein is not altered.