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Multiple epoxide hydrolases in human lung.

T M Guenthner, T A Karnezis

    Drug Metabolism and Disposition: the Biological Fate of Chemicals
    |March 1, 1986
    PubMed
    Summary
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    Human lung epoxide hydrolase activity was measured for benzo(a)pyrene 4,5-oxide (BPO) and trans-stilbene oxide. Both cytosolic and microsomal enzymes showed similar catalytic properties, suggesting they may be identical.

    Area of Science:

    • Biochemistry
    • Enzymology
    • Toxicology

    Background:

    • Epoxide hydrolases are crucial enzymes involved in the metabolism of xenobiotics.
    • Benzo(a)pyrene 4,5-oxide (BPO) and trans-stilbene oxide are model substrates for studying epoxide hydrolase activity.
    • Human lung tissue is a relevant site for investigating xenobiotic metabolism due to potential environmental exposures.

    Purpose of the Study:

    • To investigate and compare the catalytic properties of benzo(a)pyrene 4,5-oxide (BPO) hydrolase activity in human lung cytosolic and microsomal fractions.
    • To determine if the cytosolic and microsomal BPO hydrolases in the human lung are distinct enzymes or different forms of the same enzyme.

    Main Methods:

    • Human lung samples from 12 patients were used to measure BPO hydrolase and trans-stilbene oxide hydrolase activities.

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  • Enzyme activity was assessed in both cytosolic and microsomal cell fractions.
  • Catalytic properties, including Km values and inhibition kinetics, were determined using various enzyme inhibitors.

    • Main Results:

    • Significant BPO hydrolase and trans-stilbene oxide hydrolase activities were detected in both cytosolic and microsomal fractions.
    • Similar Michaelis constant (Km) values were observed for both microsomal (22 microM) and cytosolic (37 microM) BPO hydrolases.
    • Both enzyme forms exhibited identical responses to enzyme inhibitors in vitro, with consistent IC50 and Kii values.

    Conclusions:

    • The human lung cytosolic and microsomal BPO hydrolases display highly similar catalytic properties.
    • These findings suggest that the two forms of BPO hydrolase in the human lung may be identical enzymes.
    • Further research is warranted to confirm the identity and structural characteristics of these epoxide hydrolases.