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Glutathione Reductase Is Inhibited by Acetaminophen-glutathione Conjugate in vitro
Authors: Roušar Tomáš | Pařík Patrik | Kučera Otto | Bartoš Martin | Červinková Zuzana
Year: 2010
Type of publication: článek v odborném periodiku
Name of source: Physiological Research
Publisher name: Fyziologický ústav AV ČR
Place: Praha
Page from-to: 1-6
Titles:
Language Name Abstract Keywords
cze Glutathionreduktasa je inhibována konjugátem acetaminofenu in vitro Cílem práce bylo vyšetřit případné inhibiční efekt AG na GR. Bylo zjištěno, že glutathionreduktasa je inhibována konjugátem acetaminofenu in vitro a že tento vliv může být velmi důležitý i během APAP toxicity. glutathionreduktasa;glutathion;hepatotoxicita
eng Glutathione Reductase Is Inhibited by Acetaminophen-glutathione Conjugate in vitro The aim of the present work was to investigate a new mechanism likely contributing to the toxic action of acetaminophen especially to explore the possible inhibition of glutathione reductase through an acetaminophen-glutathione conjugate (APAP-SG). APAP-SG conjugate was synthesized by organic synthesis and purified by column chromatography. The inhibitory effect of the conjugate on two types of glutathione reductase (from yeasts and rat hepatocytes) was tested spectrophotometrically. In addition, the enzyme activity (from hepatocytes lysate) was decreased to 79?7 %, 67?2 % and 39?7 %, in 0.37, 1.48 and 3.7 mM concentration of the conjugate, respectively. We ound that glutathione reductase, the essential enzyme of the antioxidant system, was dosedependently inhibited by the product of acetaminophen metabolism - the conjugate of acetaminophen and glutathione. Acetaminophen toxicity; glutathione reductase; glutathione; hepatotoxicity