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Decrease of rat liver cysteine dioxygenase (cysteine oxidase) activity mediated by glucagon.

Y Hosokawa, K Yamaguchi, N Kohashi

    Journal of Biochemistry
    |August 1, 1978
    PubMed
    Summary
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    Glucagon reduces rat liver cysteine dioxygenase activity by increasing enzyme degradation. Protein synthesis inhibition before glucagon prevents this decrease, suggesting a role for new protein synthesis in the reduction.

    Area of Science:

    • Biochemistry
    • Enzymology
    • Hepatology

    Background:

    • Cysteine dioxygenase (CDO) is a key enzyme in L-cysteine metabolism.
    • Regulation of hepatic CDO activity is crucial for maintaining amino acid homeostasis and cellular redox balance.

    Purpose of the Study:

    • To investigate the mechanism by which glucagon affects hepatic cysteine dioxygenase activity in rats.
    • To determine if the glucagon-mediated decrease in enzyme activity involves changes in protein synthesis or degradation.

    Main Methods:

    • Administration of glucagon, dibutyryl cyclic AMP, theophylline, actinomycin D, and cycloheximide to rats.
    • Measurement of hepatic cysteine dioxygenase activity.
    • Determination of enzyme half-life following glucagon administration.

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    Main Results:

    • Glucagon, dibutyryl cyclic AMP, and theophylline decreased hepatic cysteine dioxygenase activity.
    • Actinomycin D blocked the glucagon effect when administered prior to glucagon, but not after.
    • Cycloheximide induced a rapid decrease in enzyme activity with a half-life of 2.5 hours, while glucagon administration resulted in a half-life of 1 hour.

    Conclusions:

    • The glucagon-mediated decrease in hepatic cysteine dioxygenase activity is likely due to enhanced degradation or inactivation of the enzyme.
    • The results suggest that de novo protein synthesis is not required for the glucagon-induced reduction in enzyme activity.