Abstract
Oral administration of glutathione has been demonstrated to reduce exercise-induced fatigue and improve liver function, although glutathione can be synthesized in the liver. However, little is known about the underlying mechanism of this effect. To address this, the status of food-derived glutathione in the intestine, blood, and liver was examined. Glutathione-1-13C or N-acetyl-cysteine-1-13C (NAC) was orally administered to rats (50 mg/kg). Food-derived glutathione contents within tissues were estimated by subtracting endogenous glutathione-1-13C from the total glutathione-1-13C. Food-derived glutathione was present in rat intestines and livers (approximately 60 and 300 μmol/kg, respectively, 120 min after ingestion) in electrochemically reduced form, while all food-derived glutathione in the blood plasma was conjugated with proteins and low-molecular-weight thiol compounds. However, no significant amounts of NAC-derived glutathione were detected in the blood plasma. These findings indicate that food-derived glutathione is directly absorbed in its electrochemically reduced form in the intestine, is then transported in the blood in bound forms, and is finally deposited into the liver in reduced form. Therefore, upon entering the bloodstream, food-derived glutathione binds to thiol compounds and releases hydrogen atom; subsequently, it does the reverse upon incorporation into the liver, which might impact the physiological redox condition. With respect to food-derived glutathione and cysteine-containing peptides, this study provides new insights on their modes of transportation and mechanisms of action.
Highlights
Glutathione (γ-L-glutamyl-L-cysteinyl-glycine) is widely distributed in known life forms, from single-cell organisms to higher vertebrates, and is the most prevalent intracellular thiol.[1,2] Glutathione is a cofactor or substrate of glutathione peroxidase and glutathione S-transferase
Glutathione-S-transferase catalyzes the conjugation of glutathione and a wide variety of electrophilic compounds: this is the first step in the mercapturic acid pathway, a crucial component of system detoxification
Our previous study demonstrated that protein-bound glutathione in human plasma increases after ingestion of glutathione.[6] glutathione disulfide was, detected in liver and blood red cell of mice
Summary
Statuses of food-derived glutathione in intestine, blood, and liver of rat Hiroaki Yamada[1], Shinn Ono[2], Sayori Wada[3], Wataru Aoi[3], Eun Young Park[3,4], Yasushi Nakamura[3] and Kenji Sato[1]. The status of food-derived glutathione in the intestine, blood, and liver was examined. Food-derived glutathione was present in rat intestines and livers (approximately 60 and 300 μmol/kg, respectively, 120 min after ingestion) in electrochemically reduced form, while all food-derived glutathione in the blood plasma was conjugated with proteins and low-molecular-weight thiol compounds. No significant amounts of NAC-derived glutathione were detected in the blood plasma. These findings indicate that food-derived glutathione is directly absorbed in its electrochemically reduced form in the intestine, is transported in the blood in bound forms, and is deposited into the liver in reduced form. With respect to food-derived glutathione and cysteine-containing peptides, this study provides new insights on their modes of transportation and mechanisms of action
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