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Rat cytosolic epoxide hydrolase.

F Oesch, L Schladt, R Hartmann

    Advances in Experimental Medicine and Biology
    |January 1, 1986
    PubMed
    Summary
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    Rat liver epoxide hydrolase activity varies significantly between individuals and tissues. Peroxisome proliferators, but not common enzyme inducers, drastically increase cytosolic epoxide hydrolase activity.

    Area of Science:

    • Biochemistry
    • Pharmacology
    • Toxicology

    Background:

    • Epoxide hydrolases (EH) are crucial enzymes in xenobiotic metabolism.
    • Microsomal (mEH) and cytosolic (cEH) epoxide hydrolase isoforms exhibit distinct substrate specificities and tissue distribution.
    • Understanding EH activity and regulation is vital for assessing chemical safety and individual susceptibility.

    Purpose of the Study:

    • To characterize the substrate specificity and interindividual variability of rat liver microsomal and cytosolic epoxide hydrolase.
    • To investigate the tissue distribution of EH activity in rats.
    • To examine the effects of common enzyme inducers and peroxisome proliferators on rat liver EH activity.

    Main Methods:

    • Enzyme kinetic assays using specific substrates (styrene oxide for mEH, trans-stilbene oxide for cEH).

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  • Measurement of specific EH activity in liver microsomes and cytosol from Sprague-Dawley and Fischer F-344 rats.
  • Analysis of EH activity in various rat tissues (kidney, heart, brain, lung, testis, spleen).
  • Treatment with xenobiotic metabolizing enzyme inducers and peroxisome proliferating drugs (clofibrate, tiadenol, acetylsalicylic acid) followed by activity measurements.

    • Main Results:

    • Significant interindividual variability in Sprague-Dawley rat liver cEH activity (2-77 pmol/min x mg protein), with lower variability in Fischer F-344 rats.
    • mEH showed much lower interindividual variation compared to cEH.
    • cEH activity was highest in kidney and heart, followed by liver, with lower levels in brain, lung, testis, and spleen.
    • mEH activity was predominantly localized in the liver.
    • Common enzyme inducers did not significantly alter liver cEH activity.
    • Peroxisome proliferators (clofibrate, tiadenol, acetylsalicylic acid) markedly increased liver cEH activity (5-13 fold), paralleling increased peroxisomal beta-oxidation.

    Conclusions:

    • Rat liver cEH exhibits substantial interindividual variability, particularly in outbred strains, suggesting genetic or environmental influences.
    • Tissue distribution of EH activity differs significantly between mEH and cEH isoforms.
    • Liver cEH activity is potently induced by peroxisome proliferating agents, indicating a link between peroxisome proliferation and EH regulation.
    • These findings highlight the complex regulation of epoxide hydrolases and their potential role in mediating the toxicity of peroxisome-inducing agents.