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Chick oviduct progesterone receptor: structure, immunology, function.

J M Renoir, J Mester

    Molecular and Cellular Endocrinology
    |August 1, 1984
    PubMed
    Summary
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    The chick oviduct progesterone receptor exists in two forms: activated (4S) and non-activated (8S). The non-activated form contains hormone-binding proteins complexed with a 90 kDa protein, which dissociates upon activation.

    Area of Science:

    • Molecular Endocrinology
    • Steroid Hormone Receptors
    • Chick Oviduct Biology

    Background:

    • The progesterone receptor (PR) mediates the effects of progesterone, a key steroid hormone regulating reproductive functions.
    • Understanding the structural dynamics of PR is crucial for deciphering steroid hormone signaling pathways.
    • Chick oviduct is a well-established model system for studying steroid hormone receptor regulation.

    Purpose of the Study:

    • To biochemically and immunologically characterize the purified chick oviduct progesterone receptor.
    • To elucidate the subunit composition and activation mechanism of the progesterone receptor.
    • To investigate the role of associated proteins in receptor structure and function.

    Main Methods:

    • Biochemical analysis of purified chick oviduct progesterone receptor.

    Related Experiment Videos

  • Immunological approaches using anti-progesterone receptor antibodies.
  • Analysis of receptor subunits and their molecular weights (Mr).
  • Histological studies to determine receptor localization.

    • Main Results:

    • The activated progesterone receptor (4S) comprises two progestin-binding polypeptides: A (79 kDa) and B (110 kDa).
    • The non-activated receptor (8S) is a complex of hormone-binding polypeptides (A or B) with a 90 kDa non-hormone-binding protein (two molecules per complex).
    • The 90 kDa protein is also associated with non-activated forms of other chick steroid hormone receptors.
    • Molybdate stabilizes the non-activated 8S receptor form.
    • Activation involves subunit dissociation without primary structure changes and facilitates nuclear binding.
    • Ligand presence accelerates activation but is not essential in vitro.
    • Non-activated receptors may also be nuclear, despite activated forms binding nuclei.

    Conclusions:

    • The chick oviduct progesterone receptor exists as distinct activated (4S) and non-activated (8S) forms with different subunit compositions.
    • A 90 kDa protein plays a significant role in maintaining the non-activated state of steroid hormone receptors.
    • Receptor activation is a process of subunit dissociation, leading to nuclear translocation and function.
    • The localization of non-activated receptors in the nucleus suggests complex regulatory mechanisms.