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Related Experiment Videos

Does glutathione regulate thyroxine deiodinase activity in cells?

K Sato, J Robbins

    Hormone and Metabolic Research. Supplement Series
    |January 1, 1984
    PubMed
    Summary
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    Glutathione (GSH) regulates thyroid hormone deiodination not by its total concentration, but by the ratio of its oxidized form (GSSG) to total GSH. This finding impacts understanding of thyroid hormone metabolism and related disorders.

    Area of Science:

    • Biochemistry
    • Endocrinology
    • Cell Biology

    Background:

    • Thyroid hormone deiodination is crucial for regulating T3 levels.
    • Iodothyronine monodeiodinase enzymes require reduced sulfhydryl groups for activity.
    • Hepatic nonprotein sulfhydryls, including glutathione (GSH), are implicated in this process.

    Purpose of the Study:

    • To investigate the regulatory role of glutathione (GSH) in thyroid hormone deiodination.
    • To determine if total GSH concentration or its redox state influences monodeiodinase activity.

    Main Methods:

    • Cultured rat hepatocytes were used to manipulate GSH levels and redox state.
    • Hepatocytes were cultured in cysteine and methionine-deficient medium to decrease GSH.
    • Glutathione disulfide (GSSG) to total GSH ratio was altered using diamide, butylhydroperoxide, or vinblastine.

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  • Fetal mouse liver explants were also studied to assess deiodinase activity and GSH levels.

    • Main Results:

    • Decreasing total GSH by 90% in hepatocytes did not affect 5'- or 5-deiodinase activity.
    • Increasing the GSSG:total GSH ratio in hepatocytes led to decreased 5'-deiodination.
    • In fetal mouse liver explants, decreased 5'-deiodination correlated with a normal GSSG ratio and reduced Vmax.

    Conclusions:

    • Monodeiodinase activity in hepatocytes is not regulated by the total concentration of GSH.
    • Thyroid hormone deiodination is inversely correlated with the GSSG to total GSH ratio, indicating redox state is a key regulatory factor.