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Valpromide inhibits human epoxide hydrolase.

G M Pacifici, M Franchi, C Bencini

    British Journal of Clinical Pharmacology
    |September 1, 1986
    PubMed
    Summary

    The antipileptic drug valpromide (VPM) inhibits epoxide hydrolase activity across various human organs. This drug significantly reduces enzyme function, impacting epoxide metabolism in adults and fetuses.

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    Area of Science:

    • Pharmacology
    • Biochemistry
    • Toxicology

    Background:

    • Epoxide hydrolase enzymes are crucial for metabolizing epoxides, reactive intermediates implicated in toxicity and carcinogenesis.
    • Valpromide (VPM) is an established antiepileptic drug with potential interactions with metabolic enzymes.
    • Understanding VPM's effect on epoxide hydrolase is vital for assessing its safety and potential drug interactions.

    Purpose of the Study:

    • To investigate the inhibitory effects of valpromide (VPM) on epoxide hydrolase activity.
    • To determine if VPM's inhibition varies across different human organs and substrates.
    • To elucidate the mechanism of VPM's inhibition on adult liver epoxide hydrolase.

    Main Methods:

    • Epoxide hydrolase activity was measured using styrene oxide and benzo(a)pyrene-4,5-oxide as substrates.
    • Enzyme activity was assessed in human adult and fetal liver, kidneys, lungs, intestine, and placenta.
    • Inhibition kinetics were analyzed, including competitive inhibition studies.

    Main Results:

    • Valpromide (VPM) demonstrated inhibitory effects on epoxide hydrolase from all investigated human organs.
    • The degree of VPM inhibition was consistent regardless of the substrate used (styrene oxide or benzo(a)pyrene-4,5-oxide).
    • A 50% reduction in epoxide hydrolase activity was observed at VPM concentrations comparable to substrate levels, indicating significant inhibition. VPM competitively inhibited adult liver epoxide hydrolase.

    Conclusions:

    • Valpromide (VPM) is a potent inhibitor of human epoxide hydrolase in various tissues.
    • The findings suggest a potential for VPM to alter the metabolism of endogenous and exogenous epoxides.
    • Further research is warranted to explore the clinical implications of VPM-induced epoxide hydrolase inhibition.

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