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Related Experiment Videos

Nuclear triiodothyronine-binding protein: partial characterization and binding to chromatin.

L J Degroot, S Refetoff, J Strausser

    Proceedings of the National Academy of Sciences of the United States of America
    |October 1, 1974
    PubMed
    Summary

    Researchers identified a stable triiodothyronine-nuclear protein complex in rat liver nuclei. This complex binds thyroid hormone in vivo and interacts with chromatin, offering insights into thyroid hormone regulation.

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    Area of Science:

    • Molecular Endocrinology
    • Nuclear Receptor Research
    • Thyroid Hormone Metabolism

    Background:

    • Thyroid hormones, like triiodothyronine (T3), play crucial roles in cellular metabolism and development.
    • Understanding the intracellular transport and binding of thyroid hormones is key to elucidating their mechanism of action.
    • Nuclear proteins are suspected to be involved in sequestering and regulating the availability of thyroid hormones within the cell.

    Purpose of the Study:

    • To characterize the nature of triiodothyronine binding to nuclear components in vivo.
    • To investigate the stability and properties of the triiodothyronine-nuclear protein complex.
    • To examine the interaction of this complex with liver chromatin.

    Main Methods:

    • Preparation of rat liver nuclei via sucrose sedimentation.

    Related Experiment Videos

  • Extraction of nuclear proteins using 0.4 M KCl.
  • Analysis of the triiodothyronine-nuclear extract complex using dialysis, anion exchange chromatography, agarose-gel electrophoresis, and enzymatic/chemical treatments (Pronase, urea, p-chloromercuribenzoic acid, RNase, DNase).
  • In vitro binding assays of the complex to crude liver chromatin at varying KCl concentrations.

    • Main Results:

    • A [(125)I]triiodothyronine-nuclear protein complex was isolated from rat liver nuclei.
    • This complex demonstrated stability against dialysis and anion exchange, indicating strong binding.
    • The complex was sensitive to proteases and denaturants but resistant to RNase and DNase, suggesting a proteinaceous nature.
    • Thermal inactivation at 37°C altered binding affinity without affecting electrophoretic mobility.
    • The complex bound to liver chromatin in vitro at low salt concentrations and was extractable at >0.2 M KCl.

    Conclusions:

    • A specific, stable triiodothyronine-nuclear protein complex exists in vivo.
    • This complex exhibits characteristics suggesting its role in thyroid hormone nuclear transport or binding.
    • The complex interacts with chromatin, potentially influencing gene regulation by thyroid hormones.