2000
DOI: 10.1074/jbc.m006777200
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Differential Effects of Xenoestrogens on Coactivator Recruitment by Estrogen Receptor (ER) α and ERβ

Abstract: It has been proposed that tissue-specific estrogenic and/or antiestrogenic actions of certain xenoestrogens may be associated with alterations in the tertiary structure of estrogen receptor (ER) ␣ and/or ER␤ following ligand binding; changes which are sensed by cellular factors (coactivators) required for normal gene expression. However, it is still unclear whether xenoestrogens affect the normal behavior of ER␣ and/or ER␤ subsequent to receptor binding. In view of the wide range of structural forms now recogn… Show more

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Cited by 321 publications
(190 citation statements)
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“…Consistent with this data, genistein-bound ERα recruits the steroid receptor coactivator (SRC)-3 nuclear receptor (NR) box I of the p160 transcriptional coactivator family with less than half of the efficacy of E2-bound ERα, and SRC-3 NR box II is not recruited at all (Routledge et al, 2000;Bramlett et al, 2001). On the other hand, the crystal structure of ERβ with genistein indicates that H12 is positioned on the surface of the LBD and the binding of SRC-3 NR box I showed a 3-fold amount in the presence of genistein greater than E2-bound receptor (Routledge et al, 2000;Bramlett et al, 2001). Thus, selective coactivator recruitment may be an underlying mechanism for tissue/cell (anti) estrogenicity of genistein.…”
Section: Fl Fl Fl Fl Fla a A A Av V V V Vonoid Estr Onoid Estr Onoid supporting
confidence: 60%
“…Consistent with this data, genistein-bound ERα recruits the steroid receptor coactivator (SRC)-3 nuclear receptor (NR) box I of the p160 transcriptional coactivator family with less than half of the efficacy of E2-bound ERα, and SRC-3 NR box II is not recruited at all (Routledge et al, 2000;Bramlett et al, 2001). On the other hand, the crystal structure of ERβ with genistein indicates that H12 is positioned on the surface of the LBD and the binding of SRC-3 NR box I showed a 3-fold amount in the presence of genistein greater than E2-bound receptor (Routledge et al, 2000;Bramlett et al, 2001). Thus, selective coactivator recruitment may be an underlying mechanism for tissue/cell (anti) estrogenicity of genistein.…”
Section: Fl Fl Fl Fl Fla a A A Av V V V Vonoid Estr Onoid Estr Onoid supporting
confidence: 60%
“…Barkhem et al (1998) have used cell lines stabily transfected with either ERa or ERb to test the affinity and potency of widely used anti-oestrogens including tamoxifen, raloxifine and ICI 164,384 and concluded that the ligand binding cavity of ERb is more different to that of ERa than can be anticipated from the primary sequence. Recently novel non-steroidal ligands that show subtype specific binding affinity and transcriptional potency have been identified (Sun et al, 1999) and ligand-dependent differences in the ability of ERa and ERb to recruit co-activators following exposure to xenoestrogens described (Routledge et al, 2000). ERdriven gene activation can be determined by the formation of homo-or hetero-dimers, the cell type, and whether the ligand-activated receptors bind to a promotor containing ERE or an AP-1 site (Watanabe et al, 1997;Jones et al, 1999).…”
Section: Discussionmentioning
confidence: 99%
“…Perhaps the binding of these compounds triggers the recruitment of other coactivators to counteract the Tip60-mediated inhibition (7). For example, GEN can recruit SRC1 isoforms to ER␤1 (64,65). Moreover, all estrogenic chemicals except apigenin significantly inhibited the enhancement by Tip60 at the AP-1 site.…”
Section: Discussionmentioning
confidence: 99%