help button home button Endocrine Society Endocrinology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
This version published online on March 4, 2004
Endocrinology, doi:10.1210/en.2003-0806
A more recent version of this article appeared on June 1, 2004
This Article
Right arrow Author Manuscript (PDF)
Right arrow All Versions of this Article:
145/6/2968    most recent
Author Manuscript (PDF)
Right arrow Purchase Article
Right arrow View Shopping Cart
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Request Copyright Permission
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hawkins, M. B.
Right arrow Articles by Thomas, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hawkins, M. B.
Right arrow Articles by Thomas, P.

Submitted on June 27, 2003
Accepted on February 17, 2004

The unusual binding properties of the third distinct teleost estrogen receptor subtype ER{beta}a are accompanied by highly conserved amino acid changes in the ligand binding domain

M. B. Hawkins* and P. Thomas

North Carolina State University, Zoology Department, Box 7617, Raleigh, NC 27695 USA PH 919-515-5770 FAX 919-515-2698 email: beth_hawkins@ncsu.edu, The University of Texas at Austin Marine Science Institute, Port Aransas, TX 78373 USA

* To whom correspondence should be addressed. E-mail: beth_hawkins{at}ncsu.edu.

Three forms of estrogen receptor: ER{alpha}, ER{beta} (ER{beta}b), and a second ER{beta}, ER{beta}a (formerly ER{gamma}) are present in teleost fish. All ER{beta}as share amino acid changes in the ligand binding domain that may influence ligand specificity and receptor function. We compared binding specificities of the three ERs of the teleost fish, Atlantic croaker Micropogonias undulatus . Bacterially-expressed acER{alpha}, {beta}b, and {beta}a fusion proteins showed specific, high affinity binding to [3H]estradiol with Kds of 0.61 ± 0.013, 0.40 ± 0.006, and 0.38 ± 0.059 nM respectively. Rank orders of binding were: diethylstilbesterol >> ICI182780 > 4OH-tamoxifen > ICI164384 > estradiol >= zearalenone > moxestrol > tamoxifen > estrone >= 17{alpha} estradiol > estriol > 2-hydroxyestrone = genistein >> RU486 for acER{alpha}; ICI182780 > diethylstilbesterol > 4OH-tamoxifen > estradiol > ICI164384 > genistein > moxestrol > tamoxifen > zearalenone = estrone > estriol = 17{alpha} estradiol > 2-hydroxyestrone >> RU486 for acER{beta}b; and estradiol >= diethylstilbesterol > 4OH-tamoxifen > ICI182780 > ICI 164384 > estriol >= genistein > moxestrol > zearalenone > estrone > 17{alpha} estradiol > RU486 >= tamoxifen > 2-hydroxyestrone for acER{beta}a. acER{beta}a showed higher relative binding affinities (RBAs) for estradiol, estriol and RU486 and lower RBAs for synthetic estrogens and antiestrogens than previously characterized ERs. Mutation of the conserved teleost substitutions (acER{beta}aPhe396) to the ER{alpha} or ER{beta}b counterpart shifted DES and tamoxifen affinities toward those of wild-type acER{alpha} and acER{beta}b, supporting the hypothesis that the positions with conserved residue changes in teleost ERs are important to ER structure and function.
Key words: estrogen receptor • fish • estradiol • steroid hormones • steroid hormone receptors • xenoestrogens • synthetic estrogens • ligand binding • steroid receptor evolution • gene duplication • anti-estrogens • anti-progestins




This article has been cited by other articles:


Home page
 EndocrinologyHome page
Y. Pang, J. Dong, and P. Thomas
Estrogen Signaling Characteristics of Atlantic Croaker G Protein-Coupled Receptor 30 (GPR30) and Evidence It Is Involved in Maintenance of Oocyte Meiotic Arrest
Endocrinology, July 1, 2008; 149(7): 3410 - 3426.
[Abstract] [Full Text] [PDF]

Home page
 J. Pharmacol. Exp. Ther.Home page
R. M. Pelis, R. C. Hartman, S. H. Wright, T. M. Wunz, and C. E. Groves
Influence of Estrogen and Xenoestrogens on Basolateral Uptake of Tetraethylammonium by Opossum Kidney Cells in Culture
J. Pharmacol. Exp. Ther., November 1, 2007; 323(2): 555 - 561.
[Abstract] [Full Text] [PDF]

Home page
 J Mol EndocrinolHome page
T. Sabo-Attwood, J. L Blum, K. J Kroll, V. Patel, D. Birkholz, N. J Szabo, S. Z Fisher, R. McKenna, M. Campbell-Thompson, and N. D Denslow
Distinct expression and activity profiles of largemouth bass (Micropterus salmoides) estrogen receptors in response to estradiol and nonylphenol
J. Mol. Endocrinol., October 1, 2007; 39(4): 223 - 237.
[Abstract] [Full Text] [PDF]

Home page
 J Mol EndocrinolHome page
A M Tarrant, S R Greytak, G V Callard, and M E Hahn
Estrogen receptor-related receptors in the killifish Fundulus heteroclitus: diversity, expression, and estrogen responsiveness.
J. Mol. Endocrinol., August 1, 2006; 37(1): 105 - 120.
[Abstract] [Full Text] [PDF]

Home page
 Biol. Reprod.Home page
A.L. Filby and C.R. Tyler
Molecular Characterization of Estrogen Receptors 1, 2a, and 2b and Their Tissue and Ontogenic Expression Profiles in Fathead Minnow (Pimephales promelas)
Biol Reprod, October 1, 2005; 73(4): 648 - 662.
[Abstract] [Full Text] [PDF]

Home page
 EndocrinologyHome page
P. Thomas, Y. Pang, E. J. Filardo, and J. Dong
Identity of an Estrogen Membrane Receptor Coupled to a G Protein in Human Breast Cancer Cells
Endocrinology, February 1, 2005; 146(2): 624 - 632.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Endocrinology Endocrine Reviews J. Clin. End. & Metab.
Molecular Endocrinology Recent Prog. Horm. Res. All Endocrine Journals
Copyright © 2004 by The Endocrine Society