| 8032311 |
Fujita M, Sano M, Yoshino K, Tomita I: Effects of aldehyde dehydrogenase and glutathione on the degradation of (E)-4-hydroxy-2-nonenal and N-hexanal in rat liver. Biochem Mol Biol Int. 1994 Mar;32(3):429-34.
The relative contribution of the aldehyde dehydrogenase (EC 1.2.1.3, ALDH) and glutathione (GSH) conjugate system to the degradation of (E)-4-hydroxy-2-nonenal (4HN), a toxic breakdown product arising from lipid peroxidation, was investigated in rat liver. Significant increases in the contents of 4HN and hexanal (HA) and a decrease of ALDH but not alcohol dehydrogenase (EC 1.1.1.2, ADH) activity were recognized in rat liver following administration of carbon tetrachloride (3 ml/kg, p.o.). Hepatic ALDH activity was correlated with HA production (r = -0.82, P < 0.01) but not with 4HN. When lipid peroxidation was induced by t-butyl hydroperoxide, the ratio of HA to 4HN production in the liver of rats pretreated with the ALDH inhibitor, cyanamide (100 mg/kg, i.p.) was higher than that in controls, whereas the ratio was lower in the liver of rats pretreated with the glutathione-depleting agent, phorone (250 mg/kg, i.p.). These results suggest that 4HN in rat liver is metabolized by the GSH-conjugate system in preference to degradation by ALDH. |
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