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Multiple thyroid hormone binding sites on rat liver nuclear envelopes.

J T Venkatraman, Y A Lefebvre

    Biochemical and Biophysical Research Communications
    |October 15, 1985
    PubMed
    Summary
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    Thyroid hormone triiodothyronine (T3) binds to nuclear envelopes in rat liver cells, revealing two distinct binding sites. These findings suggest a potential role for membrane-bound thyroid hormone receptors in hormone transport.

    Area of Science:

    • Endocrinology
    • Cell Biology
    • Molecular Biology

    Background:

    • Thyroid hormones, such as triiodothyronine (T3), play crucial roles in cellular metabolism and development.
    • Nuclear envelopes are key cellular structures involved in regulating gene expression and maintaining nuclear integrity.
    • Understanding thyroid hormone interactions with cellular components is vital for comprehending their physiological effects.

    Purpose of the Study:

    • To investigate the presence and characteristics of thyroid hormone binding sites on isolated nuclear envelopes from male rat liver.
    • To determine the affinity and capacity of these binding sites for T3.
    • To explore the specificity of T3 binding and its potential implications in thyroid hormone transport.

    Main Methods:

    • Isolation of nuclear envelopes from male rat liver, ensuring minimal plasma membrane contamination.

    Related Experiment Videos

  • Incubation of nuclear envelopes with radiolabeled T3 at 20°C for 3 hours.
  • Scatchard analysis to characterize binding sites (affinity and capacity).
  • Competition assays using T4, reverse T3 (rT3), and 3,5-diiodothyronine (T2) to assess binding specificity.
  • Protease sensitivity and salt extractability assays to determine the nature of the binding sites.

    • Main Results:

    • Equilibrium binding of T3 to nuclear envelopes was achieved.
    • Scatchard analysis identified two classes of T3 binding sites: a high-affinity site (KD = 1.8 nM, capacity = 14.5 pmol/mg protein) and a low-affinity site (KD = 152.1 nM, capacity = 346.8 pmol/mg protein).
    • T4, rT3, and T2 effectively competed for T3 binding to the high-affinity site, while only T4 competed for the low-affinity site.
    • The binding sites were sensitive to protease treatment but not extractable by salt.
    • No radioligand degradation was observed during incubation.

    Conclusions:

    • Nuclear envelopes possess distinct high- and low-affinity binding sites for thyroid hormone T3.
    • The characteristics of these binding sites suggest they are proteinaceous.
    • The presence of T3 binding sites on nuclear envelopes, similar to those found on plasma membranes, raises the intriguing possibility of their involvement in thyroid hormone translocation across cellular membranes.