GPR30: a novel therapeutic target in estrogen-related disease

Trends Pharmacol Sci. 2008 Mar;29(3):116-23. doi: 10.1016/j.tips.2008.01.001. Epub 2008 Feb 11.

Abstract

Estrogen is a crucial hormone in human physiology that regulates a multitude of biological processes. It is also an important target in many diseases such as cancer and skeletal, neurological and immunological conditions. The actions of estrogen have traditionally been ascribed to one of two closely related classical nuclear hormone receptors, ERalpha and ERbeta, which are best characterized for regulating gene expression. Recent studies have revealed the contribution of a novel estrogen receptor GPR30, which belongs to the family of seven-transmembrane G-protein-coupled receptors, to many of the rapid biological responses to estrogen. Many drugs, such as tamoxifen and fulvestrant, which seem to selectively inhibit the activities of the classical estrogen receptors, are in widespread clinical use. However, recent results indicate that these same drugs activate multiple cellular-signaling pathways via GPR30. Unraveling the pharmacological profiles and specificities of ERalpha, ERbeta and GPR30 will be vital for understanding not only the physiological roles of each receptor but also for the development of the next generation of receptor-specific drugs.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Disease* / etiology
  • Estradiol Congeners / adverse effects
  • Estradiol Congeners / pharmacology
  • Estradiol Congeners / therapeutic use
  • Humans
  • Ligands
  • Phytoestrogens / adverse effects
  • Phytoestrogens / pharmacology
  • Phytoestrogens / therapeutic use
  • Receptors, Estrogen / genetics
  • Receptors, Estrogen / metabolism*
  • Receptors, G-Protein-Coupled / genetics
  • Receptors, G-Protein-Coupled / metabolism*

Substances

  • Estradiol Congeners
  • GPER1 protein, human
  • Ligands
  • Phytoestrogens
  • Receptors, Estrogen
  • Receptors, G-Protein-Coupled