Metabolism of carbon tetrachloride in hepatic microsomes and reconstituted monooxygenase systems and its relationship to lipid peroxidation

C. R. Wolf; W. G. Harrelson; W. M. Nastainczyk; R. M. Philpot; B. Kalyanaraman; R. P. Mason

Metabolism of carbon tetrachloride in hepatic microsomes and reconstituted monooxygenase systems and its relationship to lipid peroxidation

C. R. Wolf, W. G. Harrelson, W. M. Nastainczyk, R. M. Philpot, B. Kalyanaraman, R. P. Mason

Systems Medicine

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Abstract

The metabolism of carbon tetrachloride has been investigated in liver microsomes and in reconstituted cytochrome P-450-dependent monooxygenase systems. In both cases cytochrome P-450 appears to be the sole site of carbon tetrachloride reduction. In aerobic incubations of microsomal preparations from phenobarbital-treated rats or rabbits, carbon tetrachloride induces large increases in NADPH oxidation and oxygen uptake. This cofactor utilization is not directly related to monooxygenase-mediated metabolism. Under aerobic conditions carbon tetrachloride induces lipid peroxidation, a reaction which is not inhibited by carbon monoxide. Under anaerobic conditions, carbon monoxide is a potent inhibitor of the cytochrome P-450-mediated reduction of carbon tetrachloride. These facts are inconsistent with a role for carbon tetrachloride metabolism in the potentiation of lipid peroxidation.

Original language	English
Pages (from-to)	553-558
Number of pages	6
Journal	Molecular Pharmacology
Volume	18
Issue number	3
Publication status	Published - 1 Dec 1980

ASJC Scopus subject areas

Medicine(all)
Molecular Medicine
Pharmacology

Cite this

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abstract = "The metabolism of carbon tetrachloride has been investigated in liver microsomes and in reconstituted cytochrome P-450-dependent monooxygenase systems. In both cases cytochrome P-450 appears to be the sole site of carbon tetrachloride reduction. In aerobic incubations of microsomal preparations from phenobarbital-treated rats or rabbits, carbon tetrachloride induces large increases in NADPH oxidation and oxygen uptake. This cofactor utilization is not directly related to monooxygenase-mediated metabolism. Under aerobic conditions carbon tetrachloride induces lipid peroxidation, a reaction which is not inhibited by carbon monoxide. Under anaerobic conditions, carbon monoxide is a potent inhibitor of the cytochrome P-450-mediated reduction of carbon tetrachloride. These facts are inconsistent with a role for carbon tetrachloride metabolism in the potentiation of lipid peroxidation.",

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AU - Wolf, C. R.

AU - Harrelson, W. G.

AU - Nastainczyk, W. M.

AU - Philpot, R. M.

AU - Kalyanaraman, B.

AU - Mason, R. P.

PY - 1980/12/1

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N2 - The metabolism of carbon tetrachloride has been investigated in liver microsomes and in reconstituted cytochrome P-450-dependent monooxygenase systems. In both cases cytochrome P-450 appears to be the sole site of carbon tetrachloride reduction. In aerobic incubations of microsomal preparations from phenobarbital-treated rats or rabbits, carbon tetrachloride induces large increases in NADPH oxidation and oxygen uptake. This cofactor utilization is not directly related to monooxygenase-mediated metabolism. Under aerobic conditions carbon tetrachloride induces lipid peroxidation, a reaction which is not inhibited by carbon monoxide. Under anaerobic conditions, carbon monoxide is a potent inhibitor of the cytochrome P-450-mediated reduction of carbon tetrachloride. These facts are inconsistent with a role for carbon tetrachloride metabolism in the potentiation of lipid peroxidation.

AB - The metabolism of carbon tetrachloride has been investigated in liver microsomes and in reconstituted cytochrome P-450-dependent monooxygenase systems. In both cases cytochrome P-450 appears to be the sole site of carbon tetrachloride reduction. In aerobic incubations of microsomal preparations from phenobarbital-treated rats or rabbits, carbon tetrachloride induces large increases in NADPH oxidation and oxygen uptake. This cofactor utilization is not directly related to monooxygenase-mediated metabolism. Under aerobic conditions carbon tetrachloride induces lipid peroxidation, a reaction which is not inhibited by carbon monoxide. Under anaerobic conditions, carbon monoxide is a potent inhibitor of the cytochrome P-450-mediated reduction of carbon tetrachloride. These facts are inconsistent with a role for carbon tetrachloride metabolism in the potentiation of lipid peroxidation.

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Metabolism of carbon tetrachloride in hepatic microsomes and reconstituted monooxygenase systems and its relationship to lipid peroxidation

Abstract

ASJC Scopus subject areas

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