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Induction of cytochrome P-450 isozymes by mirex and chlordecone

M Lewandowski1, P Levi, E Hodgson

  • 1BASF Corporation, Agricultural Research Center, Research Triangle Park, North Carolina 27709.

Insights

Mirex and chlordecone insecticides significantly increase cytochrome P-450 content in mouse liver microsomes. These compounds, similar to phenobarbital, induce specific P-450 isozymes, affecting monooxygenase activities.

Area of Science:

  • Toxicology
  • Biochemistry
  • Pharmacology

Background:

  • Cytochrome P-450 monooxygenase system plays a crucial role in xenobiotic metabolism.
  • Insecticides like mirex and chlordecone can interfere with this system.
  • Understanding their effects is vital for assessing toxicological risks.

Purpose of the Study:

  • To investigate the impact of mirex and chlordecone on the cytochrome P-450 monooxygenase system in C57BL/6N mouse liver microsomes.
  • To compare the effects of these insecticides with known P-450 inducers, phenobarbital and 3-methylcholanthrene.

Main Methods:

  • Mice were administered intraperitoneal injections of mirex and chlordecone at low (6 mg/kg) and high (30 mg/kg) doses for 2 days.
  • Hepatic microsomal P-450 content and specific monooxygenase activities (e.g., benzphetamine N-demethylase) were measured.
  • Immunoquantitation was used to determine the induction of specific P-450 isozymes (P-450 IIB1 and P-450 IA1).

Main Results:

  • Both mirex and chlordecone significantly increased hepatic microsomal P-450 content compared to controls.
  • These insecticides induced monooxygenase activities similarly to phenobarbital.
  • Mirex and chlordecone dose-dependently induced P-450 IIB1; mirex also induced a minor amount of P-450 IA1.

Conclusions:

  • Mirex and chlordecone are inducers of the cytochrome P-450 monooxygenase system in mouse liver.
  • Their induction profile resembles that of phenobarbital, primarily affecting P-450 IIB1.
  • While a minor induction of P-450 IA1 was observed with mirex, it did not significantly contribute to the measured monooxygenase activities.

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