Glutathione (GSH) is a well-known antioxidative cellular component which is ubiquitous in nature. Several enzymes involved in GSH metabolism and recycling have been found to play important roles in detoxification of xenobiotics and free radicals.
In this study, total GSH content, activity of GSH peroxidase and GSH reductase were measured in liver and kidney of cisplatin treated rats.
Total GSH content (mM/g protein) of liver was higher in cisplatin treated rats (1.51±0.28) than of nontreated control (0.95±0.28), and in kidney, it was also higher in cisplatin treated rats (0.87±0.20) than that of control (0.68±0.14).
The activity of GSH peroxidase (μM/mg protein/min) was lower in liver of cisplatin treated rats (348.0±18.54) than that of control (415.5±53.15), in kidney it was increase din cisplatin treated rats (380.5±51.86) compared to control
(327.3±20.36).
The activity of GSH reductase (μM/mg protein/min) was higher in liver of cisplatin treated rats (3.09μ0.88) than that of control (2.28μ0.61), in kidney it was also higher in cisplatin treated rats (8.50±2.62) than that of control
(3.30±1.10).
In summary, detoxification of ciplatin was revealed lesser effect in kidney as show increasion of GSH peroxidase and reductase and detoxification of cisplatin was expressed effectively in liver by increasing of GSH content and decreasing GSH
peroxidase.
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