Differential estrogen receptor binding of estrogenic substances: a species comparison

Differential estrogen receptor binding of estrogenic substances: a species comparison The study investigated the ability of 34 natural and synthetic chemicals to compete with ( 3 H)17β-estradiol (E2) for binding to bacterially expressed glutathione- S -transferase (GST)-estrogen receptors (ER) fusion proteins from five different species. Fusion proteins consisted of the ER D, E and F domains of human alpha (GST-hERαdef), mouse alpha (GST-mERαdef), chicken (GST-cERdef), green anole (GST-aERdef) and rainbow trout ERs (GST-rtERdef). All five fusion proteins displayed high affinity for E2 with dissociation constants ( K d ) ranging from 0.3 to 0.9 nM. Although, the fusion proteins exhibited similar binding preferences and binding affinities for many of the chemicals, several differences were observed. For example, α-zearalenol bound with greater affinity to GST-rtERdef than E2, which was in contrast to other GST-ERdef fusion proteins examined. Coumestrol, genistein and naringenin bound with higher affinity to the GST-aERdef, than to the other GST-ERdef fusion proteins. Many of the industrial chemicals examined preferentially bound to GST-rtERdef. Bisphenol A, 4- t -octylphenol and o,p′ DDT bound with approximately a ten-fold greater affinity to GST-rtERdef than to other GST-ERdefs. Methoxychlor, p,p ′-DDT, o,p ′-DDE, p,p ′-DDE, α-endosulfan and dieldrin weakly bound to the ERs from the human, mouse, chicken and green anole. In contrast, these compounds completely displaced ( 3 H)E2 from GST-rtERdef. These results demonstrate that ERs from different species exhibit differential ligand preferences and relative binding affinities for estrogenic compounds and that these differences may be due to the variability in the amino acid sequence within their respective ER ligand binding domains. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Steroid Biochemistry and Molecular Biology Elsevier

Differential estrogen receptor binding of estrogenic substances: a species comparison

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Publisher
Elsevier
Copyright
Copyright © 2000 Elsevier Science Ltd
ISSN
0960-0760
eISSN
1879-1220
DOI
10.1016/S0960-0760(00)00126-6
Publisher site
See Article on Publisher Site

Abstract

The study investigated the ability of 34 natural and synthetic chemicals to compete with ( 3 H)17β-estradiol (E2) for binding to bacterially expressed glutathione- S -transferase (GST)-estrogen receptors (ER) fusion proteins from five different species. Fusion proteins consisted of the ER D, E and F domains of human alpha (GST-hERαdef), mouse alpha (GST-mERαdef), chicken (GST-cERdef), green anole (GST-aERdef) and rainbow trout ERs (GST-rtERdef). All five fusion proteins displayed high affinity for E2 with dissociation constants ( K d ) ranging from 0.3 to 0.9 nM. Although, the fusion proteins exhibited similar binding preferences and binding affinities for many of the chemicals, several differences were observed. For example, α-zearalenol bound with greater affinity to GST-rtERdef than E2, which was in contrast to other GST-ERdef fusion proteins examined. Coumestrol, genistein and naringenin bound with higher affinity to the GST-aERdef, than to the other GST-ERdef fusion proteins. Many of the industrial chemicals examined preferentially bound to GST-rtERdef. Bisphenol A, 4- t -octylphenol and o,p′ DDT bound with approximately a ten-fold greater affinity to GST-rtERdef than to other GST-ERdefs. Methoxychlor, p,p ′-DDT, o,p ′-DDE, p,p ′-DDE, α-endosulfan and dieldrin weakly bound to the ERs from the human, mouse, chicken and green anole. In contrast, these compounds completely displaced ( 3 H)E2 from GST-rtERdef. These results demonstrate that ERs from different species exhibit differential ligand preferences and relative binding affinities for estrogenic compounds and that these differences may be due to the variability in the amino acid sequence within their respective ER ligand binding domains.

Journal

The Journal of Steroid Biochemistry and Molecular BiologyElsevier

Published: Nov 1, 2000

References

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