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Related Experiment Videos

Glutathione metabolizing enzyme activities in human thyroid.

G Del Boccio, R Casaccia, A Aceto

    General Pharmacology
    |January 1, 1987
    PubMed
    Summary

    Human thyroid tissue primarily contains selenium-dependent glutathione peroxidase. Glutathione transferase activity showed significant interindividual variation, with a single isoenzyme identified in thyroid cytosols.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Thyroid Research

    Background:

    • Glutathione-related enzymes play crucial roles in cellular defense mechanisms.
    • Understanding the specific isoforms and activities of these enzymes in human thyroid tissue is important for comprehending thyroid physiology and pathology.

    Purpose of the Study:

    • To analyze the activities of key glutathione-processing enzymes in human thyroid tissue.
    • To identify the specific type of glutathione peroxidase present in the thyroid.
    • To characterize glutathione transferase activity and isoenzymes in thyroid cytosols.

    Main Methods:

    • Enzyme activity assays for glutathione peroxidase (using H2O2 and cumene hydroperoxide), glutathione transferase (using 1-chloro-2,4-dinitrobenzene), glutathione reductase, and gamma-glutamyl transpeptidase.

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  • Gel filtration chromatography to assess glutathione peroxidase independence from selenium.
  • Isoelectric focusing of partially purified thyroid cytosols to characterize glutathione transferase isoenzymes.

    • Main Results:

    • Human thyroid tissue exclusively possesses selenium-dependent glutathione peroxidase, with no detectable selenium-independent activity.
    • Significant interindividual variation (up to 28-fold) in glutathione transferase activity was observed.
    • A single glutathione transferase isoenzyme, with activity centered at pH 4.6, was identified in thyroid cytosols.
    • Adequate levels of glutathione reductase and gamma-glutamyl transpeptidase activities were consistently found.

    Conclusions:

    • The human thyroid primarily relies on selenium-dependent glutathione peroxidase for its antioxidant defense.
    • Glutathione transferase activity in the thyroid exhibits considerable variability and is characterized by a specific acidic isoenzyme.
    • The consistent presence of glutathione reductase and gamma-glutamyl transpeptidase suggests their integral roles in thyroidal glutathione metabolism.