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This version published online on November 11, 2004
Endocrinology, doi:10.1210/en.2004-1064
A more recent version of this article appeared on February 1, 2005
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Submitted on August 16, 2004
Accepted on November 4, 2004

Identity of an Estrogen Membrane Receptor Coupled to a G-protein in Human Breast Cancer Cells

P. Thomas*, Y. Pang, E. J. Filardo, and J. Dong

Marine Science Institute, University of Texas at Austin, 750 Channelview Drive, Port Aransas, TX 78373, USA; Department of Medicine, Brown University School of Medicine, Providence, 593 Eddy Street, RI 02903, USA

* To whom correspondence should be addressed. E-mail: thomas{at}utmsi.utexas.edu.

Although nonclassical estrogen actions initiated at the cell surface have been described in many tissues, the identities of the membrane estrogen receptors (mERs) mediating these actions remain unclear. Here we show that GPR30, an orphan receptor unrelated to nuclear estrogen receptors (nERs), has all the binding and signaling characteristics of a mER. A high affinity (Kd: 2.7 nM), limited capacity, displaceable, single binding site specific for estrogens was detected in plasma membranes of SKBR3 breast cancer cells that express GPR30, but lack nERs. Progesterone-induced increases and siRNA-induced decreases in GPR30 expression in SKBR3 cells were accompanied by parallel changes in specific estradiol-17{beta} (E2) binding. Plasma membranes of HEK293 cells transfected with GPR30, but not those of untransfected cells, and human placental tissues that express GPR30, also displayed high affinity, specific estrogen binding typical of mERs. E2 treatment of transfected cell membranes caused activation of a stimulatory G protein (Gs) that is directly coupled to the receptor, indicating GPR30 is a G protein-coupled receptor (GPCR), and also increased adenylyl cyclase actvity. The finding that the antiestrogens tamoxifen and ICI 182,780, and an environmental estrogen, o,p'-DDE, have high binding affinities to the receptor and mimic the actions of E2 has important implications for both the development and treatment of estrogen-dependent breast cancer. GPR30 is structurally unrelated to the recently -discovered family of GPCR-like membrane progestin receptors. The identification of a second distinct class of GPCR-like steroid membrane receptors suggests a widespread role for GPCRs in nonclassical steroid hormone actions.
Key words: membrane estrogen receptor • breast cancer cells • GPCR • GPR30 • G-protein coupled receptor




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