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Multiple signaling pathways activate the chicken progesterone receptor

Y Zhang¹, W Bai, V E Allgood

¹Department of Cell Biology, Baylor College of Medicine, Houston, Texas 77030.

Molecular Endocrinology (Baltimore, Md.)

|May 1, 1994

Summary

Ligand-independent activation of the chicken progesterone receptor (cPR) was investigated. Multiple signaling pathways, including phosphatase inhibition and growth factors, were found to activate cPR without hormone binding.

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Area of Science:

Molecular Endocrinology
Cell Signaling
Steroid Receptor Biology

Background:

Previous studies showed ligand-independent activation of chicken progesterone receptor (cPR) using 8-Br-cAMP or okadaic acid.
Subsequent research on other steroid receptors yielded mixed results regarding ligand-independent activation by kinase/phosphatase modulators.

Purpose of the Study:

To determine if ligand-independent activation of cPR is reporter and cell-type specific.
To further characterize the phenomenon of hormone-independent cPR activation.

Main Methods:

Transient transfection of CV1 and HeLa cells with cPR and reporter plasmids (PREtkCAT, GRE2E1bCAT).
Treatment with modulators of kinases and phosphatases, including okadaic acid, vanadate, and epidermal growth factor.

Related Experiment Videos

Analysis of transcriptional activation of cPR.

Main Results:

Ligand-independent activation of cPR was confirmed in both CV1 and HeLa cells using different reporters.
Inhibition of phosphatase 1, but not phosphatase 2A, was required for cPR activation.
Vanadate and epidermal growth factor also induced cPR activation.

Conclusions:

Ligand-independent activation of cPR is not restricted to specific cell types or reporters.
Multiple signaling pathways, involving phosphatase 1 and growth factor signaling, can activate cPR.
These findings highlight the complex regulation of steroid receptor activity beyond hormone binding.