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- W2022187003 abstract "In order to determine whether non-specific defects of protein synthesis account for reduced levels of cytochrome P-450 in cirrhotic liver, total microsomal protein synthesis and response to microsomal enzyme-inducing agents have been examined in rats. Cirrhosis was produced by administration of carbon tetrachloride (CCl4) and phenobarbitone for 10 weeks. Ten days after stopping these agents, cytochrome P-450 levels were 30% lower in cirrhotic liver than in controls (p<0·0001). However, total microsomal protein synthesis, determined in vivo by administration of [3H]-leucine, was similar in cirrhotic (1347 ± 420 dpm/mg protein) and control (1317 ± 303 dpm/mg protein) liver. Three separate types of microsomal enzyme-inducing agents, phenobarbitone, β-naphthoflavone, and pregnenolone 16α-carbonitrile, were administered to cirrhotic and normal rats. In both groups of animals increases of total cytochrome P-450 and selective changes of cytochrome P-450 isoenzymes (assessed by mixed function oxidase activity towards four substrates) were qualitatively and quantitatively similar. It is concluded that (1) hepalocytes of cirrhotic rat liver synthesize microsomal protein at a normal rate but less of it is cytochrome P-450, and (2) the entire process of enzyme induction is intact. Thus, it appears likely that altered regulation of basal levels of cytochrome P-450 rather than an altered response of the liver is responsible for the lowered cytochrome P-450 content of cirrhotic rat liver." @default.
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- W2022187003 title "MICROSOMAL PROTEIN SYNTHESIS AND INDUCTION OF CYTOCHROME P-450 IN CIRRHOTIC RAT LIVER" @default.
- W2022187003 doi "https://doi.org/10.1038/icb.1984.29" @default.
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