Effect of 3,5-di-t-butyl-4-hydroxytoluene (BHT) on glutathione-linked detoxification mechanisms of rat ocular lens.

When rats were orally administered a daily dose of 300 mg kg-1 body weight of 3,5-di-t-butyl-4-hydroxytoluene (BHT) for 4 days, about 90% increase over basal level in total glutathione (GSH) S-transferase activity towards 1-chloro-2,4-dinitrobenzene (CDNB) was observed in ocular lens. GSH S-transferase activity in the ocular lens was also increased towards other substrates such as p-nitrobenzyl chloride and ethacrynic acid. In the rat lens, two isoenzymes of GSH S-transferase (pI 8.0 and 6.1) are present, and both of these isoenzymes are induced by BHT treatment. The quantification of GSH S-transferase protein in the control and the BHT-treated rat lenses indicates that the increase in GSH S-transferase activity in the ocular lens is due to the increased enzyme protein and not due to the activation of the enzyme. A significant increase in glutathione (acid soluble thiol) levels and glutathione reductase activity was also observed in the lenses of rats treated with BHT. Glutathione peroxidase activity and the enzymes of mercapturic acid pathway except GSH S-transferase remained unaltered by the BHT treatment.