Publikace detail

Glutathione Reductase Is Inhibited by Acetaminophen-glutathione Conjugate in vitro

Autoři: Roušar Tomáš | Pařík Patrik | Kučera Otto | Bartoš Martin | Červinková Zuzana

Rok: 2010

Druh publikace: článek v odborném periodiku

Název zdroje: Physiological Research

Název nakladatele: Fyziologický ústav AV ČR

Místo vydání: Praha

Strana od-do: 1-6

Tituly:

Jazyk	Název	Abstrakt	Klíčová slova
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

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