Title : Inhibition by cycloheximide of degradation of cytochrome P-450 in primary cultures of adult rat liver parenchymal cells and in vivo.

Pub. Date : 1979 Jun 15

PMID : 486136






5 Functional Relationships(s)
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1 Inhibition by cycloheximide of degradation of cytochrome P-450 in primary cultures of adult rat liver parenchymal cells and in vivo. Cycloheximide cytochrome P450, family 2, subfamily g, polypeptide 1 Rattus norvegicus
2 The decline in cytochrome P-450 and the subsequent increase in haem oxygenase activity was prevented by incubation of hepatocytes in medium containing an inhibitor of protein synthesis such as cycloheximide, puromycin, actinomycin D, or azaserine. Cycloheximide cytochrome P450, family 2, subfamily g, polypeptide 1 Rattus norvegicus
3 These results suggest that the conditions of cell culture stimulate selective degradation of cytochrome P-450 by a process that is inhibited by cycloheximide and hence may require protein synthesis. Cycloheximide cytochrome P450, family 2, subfamily g, polypeptide 1 Rattus norvegicus
4 Administration of cycloheximide to either bromobenzene-treated rats or to untreated rats decreased the degradation of the haem moiety of cytochrome P-450. Cycloheximide cytochrome P450, family 2, subfamily g, polypeptide 1 Rattus norvegicus
5 These findings confirm that the catabolism of hepatic cytochrome P-450 haem is controlled by similar cycloheximide-sensitive processes in the basal steady state in vivo, as stimulated by bromobenzene in vivo, or in hepatocytes under the conditions of cell culture. Cycloheximide cytochrome P450, family 2, subfamily g, polypeptide 1 Rattus norvegicus