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Thyronamines are substrates for human liver sulfotransferases.

C A Pietsch1, T S Scanlan, R J Anderson

  • 1Veterans Affairs Medical Center, 4101 Woolworth Avenue, Omaha, Nebraska 68105, and University of California, San Francisco 94143, USA.

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Area of Science:

  • Biochemistry
  • Pharmacology
  • Endocrinology

Background:

  • Sulfotransferases (SULTs) are crucial enzymes for metabolizing endogenous compounds, including neurotransmitters and thyroid hormones.
  • Thyronamines, derived from thyroid hormones, exert rapid, nongenomic physiological effects that may be terminated by sulfation.
  • Understanding thyronamine metabolism is key to elucidating their biological roles and potential therapeutic applications.

Purpose of the Study:

  • To investigate thyronamines (T0AM, T1AM, T2AM, T3AM) as substrates for human liver and cDNA-expressed sulfotransferase (SULT) activities.
  • To characterize the biochemical properties of SULTs involved in thyronamine metabolism.
  • To determine the role of SULT-mediated sulfation in regulating the physiological effects of thyronamines.

Main Methods:

  • Assessed SULT activity using thyronamines in human liver supernatant and with eight cDNA-expressed SULT isoforms (SULT1A1, 1A2, 1A3, 1C2, 1E1, 2A1, 2B1a, 2B1b).
  • Quantified SULT activity using different thyronamine substrates and characterized kinetic properties.
  • Compared SULT activity across various SULT isoforms and thyronamine structures.

Main Results:

  • Human liver SULTs exhibited significant activity with thyronamines, with 3-iodothyronamine (T1AM) showing the highest activity.
  • Expressed SULT1A3 demonstrated the greatest activity with T0AM, T1AM, and T3AM, while SULT1A1 was active with T3AM.
  • T1AM, known for its potent pharmacological activity, correlated with the highest SULT activity in both liver preparations and expressed SULT1A3/SULT1E1.

Conclusions:

  • Sulfation by human liver SULTs is a significant metabolic pathway for thyronamines.
  • Specific SULT isoforms, notably SULT1A3, play a key role in thyronamine metabolism.
  • SULT-mediated sulfation likely contributes to the termination of thyronamine's physiological actions, regulating their effects.