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Endocrinology Vol. 138, No. 3 863-870
Copyright © 1997 by The Endocrine Society

Articles

Comparison of the Ligand Binding Specificity and Transcript Tissue Distribution of Estrogen Receptors {alpha} and ß

George G. J. M. Kuiper1, Bo Carlsson, Kaj Grandien, Eva Enmark, Johan Häggblad, Stefan Nilsson and Jan-Åke Gustafsson2

Center for Biotechnology and Department of Medical Nutrition, Karolinska Institute (G.G.J.M.K., K.G., E.E., J.-Å.G.); and KaroBio AB (B.C., J.H., S.N.) Huddinge, Sweden

Address all correspondence and requests for reprints to: George Kuiper, Center for Biotechnology, Karolinska Institute, NOVUM, S-14186 Huddinge, Sweden. E-mail: george.kuiper{at}cbt.ki.se

The rat estrogen receptor (ER) exists as two subtypes, ER{alpha} and ERß, which differ in the C-terminal ligand binding domain and in the N-terminal transactivation domain. In this study we investigated the messenger RNA expression of both ER subtypes in rat tissues by RT-PCR and compared the ligand binding specificity of the ER subtypes.

Saturation ligand binding analysis of in vitro synthesized human ER{alpha} and rat ERß protein revealed a single binding component for 16{alpha}-iodo-17ß-estradiol with high affinity [dissociation constant (Kd) = 0.1 nM for ER{alpha} protein and 0.4 nM for ERß protein]. Most estrogenic substances or estrogenic antagonists compete with 16{alpha}-[125I]iodo-17ß-estradiol for binding to both ER subtypes in a very similar preference and degree; that is, diethylstilbestrol > hexestrol > dienestrol > 4-OH-tamoxifen > 17ß-estradiol > coumestrol, ICI-164384 > estrone, 17{alpha}-estradiol > nafoxidine, moxestrol > clomifene > estriol, 4-OH-estradiol > tamoxifen, 2-OH-estradiol, 5-androstene-3ß,17ß-diol, genistein for the ER{alpha} protein and dienestrol > 4-OH-tamoxifen > diethylstilbestrol > hexestrol > coumestrol, ICI-164384 > 17ß-estradiol > estrone, genistein > estriol > nafoxidine, 5-androstene-3ß,17ß-diol > 17{alpha}-estradiol, clomifene, 2-OH-estradiol > 4-OH-estradiol, tamoxifen, moxestrol for the ERß protein. The rat tissue distribution and/or the relative level of ER{alpha} and ERß expression seems to be quite different, i.e. moderate to high expression in uterus, testis, pituitary, ovary, kidney, epididymis, and adrenal for ER{alpha} and prostate, ovary, lung, bladder, brain, uterus, and testis for ERß. The described differences between the ER subtypes in relative ligand binding affinity and tissue distribution could contribute to the selective action of ER agonists and antagonists in different tissues.




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