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Progesterone "receptor" in rat ovary.

J R Schreiber, J W Hsueh

|October 1, 1979

Summary

Researchers identified a progesterone receptor in rat ovaries. This soluble, thermolabile protein binds the progestin R5020 with high affinity, indicating its role in ovarian function.

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Area of Science:

Reproductive biology
Endocrinology
Molecular endocrinology

Background:

Progesterone plays a crucial role in reproductive processes.
Identifying and characterizing progesterone receptors is essential for understanding hormonal regulation.
Ovarian function is intricately linked to steroid hormone signaling.

Purpose of the Study:

To identify and characterize a progesterone receptor in the ovaries of immature female rats.
To investigate the binding properties and specificity of the identified receptor.

Main Methods:

Incubation of ovarian cytosol with radiolabeled R5020.
Fractionation using Sephadex G-200 column chromatography.
Assessment of binding characteristics including heat lability, trypsin sensitivity, and steroid competition assays.
Scatchard analysis to determine binding affinity and site number.

Main Results:

A soluble, thermolabile protein in ovarian cytosol exhibited characteristics of a progesterone receptor.
The receptor demonstrated saturable binding of the synthetic progestin R5020 with a dissociation constant (Kd) of approximately 4 nM.
Binding was inhibited by progesterone and other steroids, with R5020 showing the highest affinity.
Glycerol stabilized the receptor-ligand complex, while heat and trypsinization abolished binding.

Conclusions:

A protein with the properties of a progesterone receptor was successfully identified in the cytoplasmic fraction of rat ovaries.
This finding contributes to the understanding of progesterone action in the ovary.
The characterized receptor exhibits high affinity for R5020 and specific binding preferences for various steroids.

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