Effects of acute CS2 intoxication on liver protein and drug metabolism |
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Authors: | J. Järvisalo H. Savolainen H. Vainio |
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Affiliation: | Institute of Occupational Health, Department of Industrial Hygiene and Toxicology, Haartmaninkatu 1, SF-00290 Helsinki 29 Finland |
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Abstract: | Rats pretreated with phenobarbitone and their controls were exposed to 0.15% atmospheric CS2 for 2 h. Liver protein metabolism and microsomal drug metabolizing enzyme activities were analyzed 1, 4 and 46 h later. In the pretreated rats the [14C]leucine uptake was at first inhibited, then liver RNA tended to increase. This increase was followed by a decline in the [14C]leucine uptake, while RNA content diminished to the control level. In the control rats (not pretreated with phenobarbital) the effects of CS2 on liver protein metabolism were less; only at 4 h after the exposure was liver RNA increased and [14C]leucine uptake slightly stimulated. In the pretreated rats CS2 had decreased microsomal P-450 by about 50% at 1 and 4 h, and the activity of 7-O-dealkylase of ethoxycoumarin had decreased even more. The measurable UDPglucuronosyltransferase of the liver microsomes of the pretreated rats had increased by 26% at 1 h and by 80% at 4 h after the CS2 exposure. The in vivo activation of microsomal UDPglucuronosyltransferase may result from a stimulated lipid peroxidation of reticuloendothelial membranes by CS2 metabolites in vivo, as suggested by the diene conjugation spectra. In control rats CS2 depressed only the ethoxycoumarin deethylase activity. All the microsomal changes caused by CS2 exposure were restored within 46 h.It is suggested that the different action of CS2 on the liver protein metabolism of rats pretreated with phenobarbitone and controls results from the different stage of protein turnover in the two groups, i.e. in the barbituratetreated animals there is a phase of increased protein synthesis and accordingly the protein turnover is more sensitive to the action of CS2. |
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