Effects of Arbutin on Potassium Bromate-Induced Erythrocyte Toxicity in Rats: Biochemical Evaluation of Some Metabolic Enzyme Activities In Vivo and In Vitro.

Abstract

In the present study, the inhibitory effect of potassium bromate on the pentose phosphate pathway and intracellular antioxidant systems enzymes (glucose 6-phosphate dehydrogenase (G6PD), 6-phosphogluconate dehydrogenase (6PGD), glutathione reductase (GR), glutathione S-transferase (GST), and thioredoxin reductase (TrxR)) and the role of arbutin in ameliorating this inhibition were investigated. In the in vivo phase of the study, Wistar Albino rats (28 male adults) were randomly divided into four groups. Control (n = 7): isotonic serum (0.5 mL, i.p), potassium bromate group (n = 7): potassium bromate (100 mg/kg), arbutin group (n = 7): arbutin (i.p.) (50 mg/kg/day), potassium bromate + arbutin, and Group (n = 7): potassium bromate (100 mg/kg) + arbutin (50 mg/kg/day) (i.p). The results of in vivo study showed that the activities of G6PD, 6PGD, GR, and TrxR enzymes were strongly inhibited in potassium bromate groups (p < 0.05). It was determined that GST enzyme activity decreased in the potassium bromate group, but this decrease was not statistically significant compared to the control group (p ⩾ 0.05). A statistically significant increase was found in G6PD, 6PGD, GST, and TrxR enzyme activities in the arbutin group compared to the control group (p < 0.05). The increase in GR enzyme activity was not statistically significant (p ⩾ 0.05). The potassium bromate + arbutin group's enzyme activity increased in comparison to the potassium bromate group and was discovered to be closer to the control group. It was found that potassium bromate inhibited the 6PGD enzyme obtained from rat erythrocyte tissues with IC50 = 346 μM value and Ki = 434.4 μM ± 6.1 value, and the inhibition was noncompetitive.