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Stabilization of androgen receptor protein is induced by agonist, not by antagonists

Takashi Furutani1, Tomoyuki Watanabe, Kyouko Tanimoto

  • 1Metabolic Diseases Research, Pharmacology Laboratories, Institute for Drug Discovery Research, Yamanouchi Pharmaceutical Co. Ltd., Tsukuba 305-8585, Japan.

Insights

Androgen agonists like DHT stabilize the human androgen receptor (hAR) protein, enhancing its function. Androgen antagonists block this stabilization and function, revealing a key mechanism of action for these drugs.

Area of Science:

  • Molecular Endocrinology
  • Nuclear Receptor Signaling
  • Pharmacology

Background:

  • Nuclear receptor ligand action is primarily determined by receptor expression levels.
  • Receptor expression is regulated by transcriptional and post-transcriptional mechanisms.
  • The impact of ligands on nuclear receptor protein turnover is not well understood.

Purpose of the Study:

  • To investigate the effects of androgen agonists and antagonists on human androgen receptor (hAR) protein turnover.
  • To elucidate the role of ligand-induced stabilization in hAR protein regulation.
  • To understand the mechanism by which androgen antagonists inhibit hAR function.

Main Methods:

  • Utilized stably transformed Chinese hamster ovary (CHO) cells expressing exogenous hAR.
  • Employed Western blot analysis to assess hAR protein levels and stability.
  • Examined the impact of dihydrotestosterone (DHT), hydroxyflutamide, and bicalutamide (BIC) on hAR turnover and transactivation.

Main Results:

  • The potent androgen dihydrotestosterone (DHT) significantly stabilized hAR protein and induced its transactivation function.
  • Androgen antagonists, hydroxyflutamide and bicalutamide (BIC), abrogated DHT-induced hAR stabilization.
  • Antagonists also inhibited the ligand-induced transactivation function of the hAR.

Conclusions:

  • Androgen antagonists exert their effects, at least partly, by preventing agonist-induced stabilization of the hAR protein.
  • Antagonists block both the stabilization and the transactivation function of the hAR in response to ligands.
  • This study provides critical insights into the post-transcriptional regulation of nuclear receptors by their ligands.

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