Abstract
Molecular hydrogen (H2) has been shown to have antioxidant and anti-inflammatory activities that may reduce the development and progression of many diseases. In this study, hydrogen-rich water (HRW) was obtained by reacting hybrid magnesium–carbon hydrogen storage materials with water. Then, the effects of intake of HRW on the activities of xenobiotic-metabolizing enzymes, membrane transporters, and oxidative stress in rats were investigated. Rats were given HRW ad libitum for four weeks. The results showed that intake of HRW had no significant effect on the activities of various cytochrome P450 (CYP) enzymes (CYP1A1, 1A2, 2B, 2C, 2D, 2E1, 3A, and 4A), glutathione-S-transferase, and Uridine 5′-diphospho (UDP)-glucuronosyltransferase. Except for a mild lower plasma glucose concentration, intake of HRW had no effect on other plasma biochemical parameters in rats. p-Glycoprotein and multidrug resistance-associated protein (Mrp) 2 protein expressions in liver were elevated after intake of HRW. However, HRW had no significant effects on glutathione, glutathione peroxidase, or lipid peroxidation in liver. The results from this study suggest that consumption of HRW may not affect xenobiotic metabolism or oxidative stress in liver. However, intake of HRW may increase the efflux of xenobiotics or toxic substances from the liver into bile by enhancing p-glycoprotein and Mrp2 protein expressions.
Highlights
Xenobiotics, such as drugs or toxic chemicals, can be metabolized and eliminated by xenobioticmetabolizing enzymes and membrane transporters
The cytochrome P450 (CYP) enzymes are the major phase I enzymes responsible for the metabolism of endogenous molecules and exogenous xenobiotics, resulting in the formation of more water-soluble and less toxic metabolites [1]
hydrogen-rich water (HRW) had no significant effect on Mrp3 protein expression. These results suggest that intake of HRW may increase the efflux of endogenous substances and exogenous xenobiotics from liver into bile by increasing Mrp2 and p-glycoprotein protein expression without affecting the hepatic activity of xenobiotic-metabolizing enzymes in rats
Summary
Xenobiotics, such as drugs or toxic chemicals, can be metabolized and eliminated by xenobioticmetabolizing enzymes and membrane transporters. Some CYP enzymes, such as CYP1A1, 3A, and 2E1, are involved in the bioactivation of chemicals, such as benzo[a]pyrene, aflatoxin B1, and acetaminophen [2,3,4], and produce electrophile intermediates that may covalently bind to proteins, lipids, and DNA. These enzyme reactions may produce more reactive oxygen species (ROS) and increase oxidative damage to tissues [5]. Uridine 5’-diphospho (UDP)-glucuronosyltransferase (UGT) and glutathione S-transferase (GST) are two important phase II detoxifying enzymes that catalyze the conjugation reactions, resulting
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