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Endocrinology Vol. 145, No. 6 2968-2977
Copyright © 2004 by The Endocrine Society

The Unusual Binding Properties of the Third Distinct Teleost Estrogen Receptor Subtype ERßa Are Accompanied by Highly Conserved Amino Acid Changes in the Ligand Binding Domain

M. B. Hawkins and P. Thomas

Zoology Department, North Carolina State University (M.B.H.), Raleigh, North Carolina 27695; and University of Texas at Austin, Marine Science Institute (P.T.), Port Aransas, Texas 78373

Address all correspondence and requests for reprints to: Dr. Mary Beth Hawkins, Department of Zoology, North Carolina State University, Box 7617, Raleigh, North Carolina 27695. E-mail: beth_hawkins{at}ncsu.edu.

Three forms of estrogen receptor: ER{alpha}, ERß (ERßb), and a second ERß, ERßa (formerly ER{gamma}) are present in teleost fish. All ERßas 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 Atlantic croaker (ac) ER{alpha}, -ßb, and -ßa fusion proteins showed specific, high affinity binding to 17ß-[3H]estradiol, with Kd values of 0.61 ± 0.013, 0.40 ± 0.006, and 0.38 ± 0.059 nM, respectively. Rank orders of binding were: diethylstilbestrol >> ICI182780 > 4-hydroxytamoxifen > ICI164384 > estradiol >= zearalenone > moxestrol > tamoxifen > estrone >= 17{alpha}-estradiol > estriol > 2-hydroxyestrone = genistein >> RU486 for acER{alpha}; ICI182780 > diethylstilbestrol > 4-hydroxytamoxifen > estradiol > ICI164384 > genistein > moxestrol > tamoxifen > zearalenone = estrone > estriol = 17{alpha}-estradiol > 2-hydroxyestrone >> RU486 for acERßb; and estradiol >= diethylstilbestrol > 4-hydroxytamoxifen > ICI182780 > ICI 164384 > estriol >= genistein > moxestrol > zearalenone > estrone > 17{alpha}-estradiol > RU486 >= tamoxifen > 2-hydroxyestrone for acERßa. acERßa showed higher relative binding affinities for estradiol, estriol, and RU486 and lower relative binding affinities for synthetic estrogens and antiestrogens than previously characterized ERs. Mutation of the conserved teleost substitutions (acERßaPhe396) to the ER{alpha} or ERßb counterpart shifted diethylstilbestrol and tamoxifen affinities toward those of wild-type acER{alpha} and acERßb, supporting the hypothesis that the positions with conserved residue changes in teleost ERs are important to ER structure and function.




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