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Related Experiment Videos

Characterization of thyroid hormone sulfotransferases

T J Visser1, E Kaptein, H Glatt

  • 1Department of Internal Medicine III, Erasmus University Medical School, Rotterdam, The Netherlands. visser@inw3.azr.nl

Chemico-Biological Interactions
|May 5, 1998
PubMed
Summary

Thyroid hormone metabolism involves sulfation, facilitating degradation. This study identifies key sulfotransferase isoenzymes in rat and human liver, including rSULT1C1 and hSULT1A1, crucial for thyroid hormone sulfation.

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Area of Science:

  • Biochemistry
  • Endocrinology
  • Molecular Biology

Background:

  • Sulfation is a key thyroid hormone metabolism pathway.
  • Type I deiodinase (D1) facilitates thyroid hormone degradation via sulfation.
  • Understanding sulfotransferase isoenzymes is crucial for thyroid hormone regulation.

Purpose of the Study:

  • Characterize iodothyronine sulfotransferase activities in rat and human liver.
  • Identify specific sulfotransferase isoenzymes involved in thyroid hormone metabolism.
  • Investigate sex-based differences in sulfotransferase activity in rats.

Main Methods:

  • Assessed sulfotransferase activity using rat and human liver cytosol.
  • Utilized recombinant rat SULT1C1 (rSULT1C1) and human SULT1A1 (hSULT1A1) isoenzymes.

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  • Employed phenol derivatives as inhibitors to characterize enzyme activity.

    • Main Results:

    • Sulfation efficiency followed the order: 3,3'-diiodothyronine (3,3'-T2) > T3 ≈ rT3 > T4.
    • 3,3'-T2 sulfotransferase activity was higher in male than female rat liver.
    • rSULT1C1 was identified as a key enzyme in male rat liver sulfation; hSULT1A1 in human liver.

    Conclusions:

    • rSULT1C1 is a significant thyroid hormone sulfotransferase in male rat liver.
    • Another isoenzyme, possibly rSULT1B1, is important for female rat liver sulfation.
    • hSULT1A1 plays a crucial role in human liver thyroid hormone sulfation.