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Related Experiment Videos

Pyrethroid insecticides: esterase cleavage in relation to selective toxicity.

C O Abernathy, J E Casida

    Science (New York, N.Y.)
    |March 23, 1973
    PubMed
    Summary
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    Mouse liver enzymes rapidly break down certain pyrethroid insecticide chemicals, especially the (+)-trans isomers. This breakdown likely explains the low toxicity of these compounds in mammals.

    Area of Science:

    • Biochemistry
    • Toxicology
    • Enzymology

    Background:

    • Pyrethroid insecticides are widely used for pest control.
    • Understanding the metabolic pathways of pyrethroids is crucial for assessing their safety and efficacy.
    • Mammalian toxicity of pyrethroids varies, suggesting specific metabolic detoxification mechanisms.

    Purpose of the Study:

    • To investigate the role of mouse hepatic microsomal esterases in the metabolism of primary alcohol chrysanthemates.
    • To determine the substrate specificity of these esterases towards different pyrethroid isomers.
    • To elucidate the contribution of esterase activity to the low mammalian toxicity of specific pyrethroid insecticides.

    Main Methods:

    • In vitro cleavage assays using mouse hepatic microsomes and primary alcohol chrysanthemates.

    Related Experiment Videos

  • Comparison of hydrolysis rates for (+)-trans and (+)-cis isomers.
  • In vivo substrate-specificity and inhibition studies.

    • Main Results:

    • Mouse hepatic microsomal esterases efficiently cleave the ester group of primary alcohol chrysanthemates.
    • Hydrolysis occurred more rapidly for the (+)-trans isomers compared to the (+)-cis isomers.
    • Inhibition studies confirmed the involvement of specific esterases in pyrethroid metabolism.

    Conclusions:

    • Mouse hepatic microsomal esterases are key enzymes in the detoxification of primary alcohol chrysanthemates.
    • The differential hydrolysis rates for (+)-trans and (+)-cis isomers contribute to isomer-specific toxicity.
    • These findings support the hypothesis that pyrethroid-hydrolyzing esterases are responsible for the low mammalian toxicity of insecticides like bioresmethrin.