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Cytochrome P-450 and halothane metabolism. Decrease in rat liver microsomal P-450 in vitro.

P A Krieter, R A van Dyke

    Chemico-Biological Interactions
    |June 1, 1983
    PubMed
    Summary
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    Halothane irreversibly decreases cytochrome P-450 in rat liver microsomes under anaerobic conditions. This effect, linked to reactive metabolites, is specific to phenobarbital-induced enzymes and involves heme destruction.

    Area of Science:

    • Biochemistry
    • Pharmacology
    • Toxicology

    Background:

    • Cytochrome P-450 enzymes are crucial for drug metabolism.
    • Halothane is an anesthetic agent with known toxic effects.
    • Enzyme induction can alter drug metabolism and toxicity.

    Purpose of the Study:

    • To investigate the mechanism of halothane-induced cytochrome P-450 inactivation.
    • To determine the role of oxygen concentration in halothane's effect on cytochrome P-450.
    • To elucidate the specific interactions between halothane metabolites and microsomal components.

    Main Methods:

    • In vitro anaerobic and aerobic incubation of rat liver microsomes.
    • Use of microsomes from phenobarbital (PB)-induced, 3-methylcholanthrene (3-MC)-induced, and untreated rats.

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  • Measurement of cytochrome P-450 and heme content.
  • Assessment of halothane metabolite binding to proteins via gel electrophoresis.
  • Evaluation of lipid peroxidation and heme N-alkyl adduct formation.

    • Main Results:

    • Anaerobic incubation with halothane irreversibly decreased cytochrome P-450 and heme in PB-induced rat microsomes.
    • Aerobic incubation showed reversible cytochrome P-450 decrease, correctable by dialysis or ferricyanide.
    • No significant decrease was observed in 3-MC-induced or untreated rat microsomes.
    • Halothane metabolites bound irreversibly to proteins under low oxygen conditions.
    • The mechanism involves reactive metabolite formation, protein binding, and heme destruction, not lipid peroxidation.

    Conclusions:

    • Halothane causes irreversible inactivation of cytochrome P-450, particularly in PB-induced rats, via reactive metabolites.
    • Oxygen availability is critical in determining the reversibility of halothane's effect on cytochrome P-450.
    • The findings suggest a mechanism involving direct damage to both the heme and protein components of cytochrome P-450.