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Department of Cell Biology, Baylor College of Medicine, Houston, Texas 77030-3498
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ABSTRACT |
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 TOP ABSTRACT INTRODUCTIONRESULTSDISCUSSIONMATERIALS AND METHODSREFERENCES |
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INTRODUCTION |
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TOPABSTRACTINTRODUCTIONRESULTSDISCUSSIONMATERIALS AND METHODSREFERENCES |
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In addition to hormone, the ER binds ligands that serve as antiestrogens. The pure (type II) antiestrogens, exemplified by ICI 164,384 and ICI 182,780, are unable to activate the ER in nearly all instances and efficiently antagonize ER function (10, 11). In contrast, mixed antiestrogens, such as trans-4-hydroxytamoxifen (4HT), inhibit ER activity in a selective manner and may even activate transcription under certain conditions (12). The latter group of antihormones engender a conformational change in the ligand-binding domain distinct from that induced by estradiol (E2) and are thought to inhibit the activity of the hormone-dependent AF2 but not AF1 (3, 13, 14). The biocharacter (agonist versus antagonist activity) of mixed antiestrogens varies among different tissues, cells and promoters, but it may also deviate within a given biological context. For example, tamoxifen, the metabolic precursor of 4HT, is initially an antagonist of MCF-7 breast cancer cells grown in nude mice but eventually stimulates tumor growth via an ER-agonistic action that can be blocked by the pure antiestrogen, ICI 164,384, and is not dependent upon the host animal (15, 16, 17).
When steroid receptors are occupied with agonists, the AF2 domain is thought to serve as a focal point for interaction with coactivator proteins, which are thought to act as adapters to the general transcriptional machinery and modulators of chromatin structure (18, 19, 20). In addition, it is hypothesized that the distinct, antiestrogen-induced conformation of the ligand-binding domain does not promote AF2-coactivator interactions and thereby impedes the ability of the DNA-bound receptor to activate transcription (21). However, the ER can stimulate transcription via its AF1 domain, and in some contexts 4HT is a relatively good ER agonist (8), suggesting that a mechanism(s) must exist to enable the ER and the general transcription machinery to productively associate under these conditions. In addition, the acquisition of agonist activity by 4HT in cells in which it formerly was an antagonist suggests that the differential expression of cell-specific factors may facilitate a shift in 4HT biocharacter.
Therefore, to test whether increased expression of a positively acting factor could enhance the agonist activity of a mixed antiestrogen, we examined the ability of a coactivator for the steroid receptor superfamily, steroid receptor coactivator-1 (SRC-1; 22 to stimulate ER transcriptional activity in cell/promoter contexts where 4HT is either an agonist or antagonist of ER function. We found that SRC-1 overexpression stimulated the agonist activity of 4HT, but was unable to reverse the antagonist action of this antiestrogen. We also have demonstrated that the silencing mediator of retinoic acid and thyroid hormone receptors (SMRT) protein (23), identified as a corepressor of several members of the nuclear receptor superfamily including the thyroid hormone receptor (TR) and retinoic acid receptor (RAR), could negatively influence the ability of a mixed antiestrogen to activate ER-dependent gene expression.
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RESULTS |
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TOPABSTRACTINTRODUCTIONRESULTSDISCUSSIONMATERIALS AND METHODSREFERENCES |
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1000 ng) of an expression vector for human
SRC-1 were cotransfected into these cells, basal, estrogen- and
4HT-stimulated gene expression was increased in a dose-dependent manner
(Fig. 1A
). In contrast, the type II antiestrogen ICI 164,384
did not activate transcription of the C3 target gene in these cells,
and exogenous SRC-1 expression had little or no effect on ER
transcriptional activity in the presence of this pure antagonist.
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). In parallel experiments, cotransfection of an
identical amount of SRC-1 expression vector increased E2-
and 4HT-stimulated expression of the intact C3 promoter (pC3-Luc) by
5-fold (see Fig. 1A), indicating that the ability of SRC-1 to
coactivate ER-dependent transcription may be influenced by promoter
context.
Previous studies have demonstrated that SRC-1 (also known as
p160) binds to the carboxy-terminal portion of the hER (amino acids
282–595), but not to a shorter ER mutant (
534) lacking the last 61
amino acids (21). This deleted region encompasses sequences required
for AF2 function (28), and it has been suggested that SRC-1 may be a
mediator of this estrogen-dependent activation domain (21).
Introduction of three amino acid substitutions (D538A/E542A/D545A) to
the ER’s ligand-binding domain disrupts AF2 activity but not receptor
dimerization or hormone-binding affinity (28). To determine whether an
intact AF2 domain is required for SRC-1 coactivation of ER-dependent
transcription, HepG2 cells were transfected with expression vectors for
wild type (pRST7-hER) or AF2 mutant
(pRST7-hER-3x) ER and the pC3-Luc target gene, and
transcriptional activity was assessed in the absence and presence of
exogenous SRC-1. In accordance with a previous report (8), these
three-point mutations significantly decreased 4HT agonist activity but
had little effect on E2-stimulated transcription of pC3-Luc
in HepG2 cells. When SRC-1 expression levels were increased,
transcription of the target gene by estrogen-activated wild type or AF2
(D538A/E542A/D545A) mutant ER was enhanced to a similar extent (Fig. 2 and data not shown) and indicates that an intact AF2
domain is not required for SRC-1 activity in this cell and promoter
context.
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6-fold, and ectopic SRC-1 expression further stimulated
gene expression by 13-fold (Fig. 3). In contrast to the data
obtained from Hep G2 cells, 4HT was a poor agonist in HeLa cells, and
exogenous SRC-1 stimulated reporter gene expression by only 4-fold
in cells treated with vehicle or 4HT. As expected, ER transcriptional
activity was very low in the presence of the pure antiestrogen ICI
164,384, whether or not exogenous SRC-1 was present.
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) indicating that SRC-1 can
significantly increase ER transcriptional activity in the absence of
ligand when cells are appropriately stimulated. In parallel
experiments, SRC-1 increased estrogen-stimulated activity by 4-fold
(Fig. 4). To ensure that forskolin/IBMX-induced transcription was
ER-dependent, CAT gene expression was assessed in the presence of the
pure antiestrogen ICI 164,384 with or without exogenous SRC-1, and no
significant activity was observed.
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). Since 4HT is normally
an antagonist in these cells (29), these ligand-independent activation
pathways also encourage a shift in the balance of this mixed
antiestrogen’s activity from antagonist to agonist. The ability of
exogenous SRC-1 to further enhance forskolin/IBMX- stimulated ER
activity in the presence of 4HT (4-fold) suggests that this
coactivator also contributes to this mechanism of gene expression.
The Corepressor, SMRT, Inhibits 4HT Agonist Activity
It is clear that in comparison to estrogens, the relative ability
of 4HT to activate ER-dependent transcription varies between cell and
tissue types (14, 24, 33), and it has been postulated that cellular
coregulatory proteins contribute to the differential biocharacter of
4HT (12). Although SRC-1 stimulated 4HT agonist activity in Hep G2
cells, it was unable to convert 4HT from an antagonist to agonist in
HeLa cells. Therefore, the possibility that a corepressor protein may
help to define the agonist/antagonist balance of 4HT activity was
examined. In HepG2 cells, where 4HT is a relatively good ER agonist,
exogenous SMRT did not decrease E2-dependent transcription
(Fig. 5A). However, SMRT attenuated 4HT’s agonist activity
(>70%) with the result that the ability of 4HT to activate
transcription was significantly attenuated in comparison to estrogen.
SMRT also decreased basal ER activity by 60%. In contrast, SMRT had
little effect on the already low activity of ER in the presence of the
pure antiestrogen ICI 164,384. Overall changes in gene expression are
unlikely to account for SMRT inhibition of 4HT-stimulated ER activity
because exogenous SMRT did not influence ß-galactosidase activity
expressed from a SV40- or cytomegalovirus (CMV)-regulated constitutive
expression vector (data not shown). When SMRT was expressed ectopically
in HeLa cells, it did not inhibit estrogen-stimulated expression of the
ERE-E1b-CAT reporter gene (Fig. 5B). However, it further decreased the
low 4HT agonist activity observed in these cells. Taken together, these
data indicate that ectopic expression of this corepressor decreases 4HT
agonist activity whether it is weak (HeLa cells) or relatively strong
(Hep G2 cells).
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). In comparison to the input
lane, significant levels of SMRT were retained by GST-ER regardless of
the presence of estrogen or antiestrogen. Thus, SMRT and ER interact
in vitro, but in a hormone-independent manner.
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; compare lanes 5 and 6 to 2 and 3).
Increasing SRC-1 expression in these cells did not restore 4HT agonist
activity relative to E2, even when 50% less SMRT
expression vector was cotransfected (compare lanes 11 and 12 to 5 and
6). As anticipated, in the absence of exogenous SMRT, ectopic SRC-1
increased the ER transcriptional activity induced by E2 and
4HT equally well. Thus, within a given cell, elevated expression of
SMRT shifts the balance of 4HT activity from an agonist to antagonist,
and overexpression of SRC-1 was unable to reverse this process.
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DISCUSSION |
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TOPABSTRACTINTRODUCTIONRESULTSDISCUSSIONMATERIALS AND METHODSREFERENCES |
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AF2 Is Not Required for SRC-1 Coactivation
Steroid receptor coactivator-1 (p160) was postulated to act as a
coactivator/mediator for the AF2 domain of steroid receptor superfamily
members (22), and it was predicted that SRC-1 would not interact
functionally with the ER when liganded with antiestrogens (21).
However, the demonstration that SRC-1 enhanced 4HT-stimulated,
AF1-dependent ER transcriptional activity in Hep G2 cells and
efficiently coactivates the E2-stimulated transcriptional
activity of an AF2-defective ER mutant (D538A/E542A/D545A) suggests
that this coactivator may act through regions in addition to AF2. In
support of this, a recently published study utilizing a modified
mammalian two-hybrid approach in Chinese hamster ovary cells indicated
that SRC-1 facilitated the physical interaction between the
amino-terminal (containing AF1) and carboxy-terminal (containing AF2)
regions of ER (34). Furthermore, SRC-1 binds to an ER534 mutant when
examined in the context of the full-length receptor (35) instead of the
ligand-binding domain alone (21). The remaining studies reporting a
lack of 4HT-dependent interaction between SRC-1 (p160) and ER were
conducted with the ligand-binding domain alone or in MCF-7 cells in
which 4HT is typically a weak agonist or antagonist (21) and AF1
contributions to SRC-1 interaction(s) with the ER were not likely to
have been assessed.
SRC-1 and Ligand-Independent Activation of the ER
The coactivation of forskolin/IBMX-stimulated ER transcriptional
activity by SRC-1 in the absence of exogenous ligand suggests that a
hormone-independent mechanism exists to facilitate a functional
interaction of ER and this coactivator. Furthermore, the ability of
ligand-independent signaling pathways to shift 4HT activity from
antagonist to agonist and thereby enable SRC-1 to strongly enhance 4HT
activity in a cell/promoter context where this antiestrogen is
typically a relatively poor agonist, supports this hypothesis. Because
all agents (i.e. dopamine, cAMP, growth factors) capable of
ligand-independently activating the ER initiate or alter the activity
of an intracellular signal transduction cascade and presumably kinases
and/or phosphatases (reviewed in 36 , it is possible that
phosphorylation of the ER and/or SRC-1 may contribute to their ability
to functionally interact with one another or with other accessory
transcription factors (e.g. CREB binding protein; CBP)
necessary for steroid receptor-dependent transcription (37).
Interestingly, CBP serves as a coactivator for numerous, diverse
transcription factors (e.g. CREB, Elk-1, c-Jun, c-Myb,
c-Fos), and at least some of these interactions are dependent and/or
enhanced by the phosphorylation of the site-specific activator
(38, 39, 40, 41, 42).
SMRT Regulation of 4HT Biocharacter
Since SRC-1 was unable to alter the agonist/antagonist balance of
4HT activity, SMRT was tested for its ability to alter 4HT’s
agonist/antagonist activity to determine whether a corepressor has the
potential to regulate mixed antiestrogen activity. In both
cell/promoter contexts tested, ectopic expression of SMRT decreased the
ability of 4HT to activate transcription while having little or no
effect on estrogen-stimulated gene expression; this suggests that full
agonists enable the ER to overcome corepressor function, while partial
agonist/antagonists do not. Although the experiments presented in this
paper used a SMRT expression vector lacking the coding region for the
first 28 amino acids, they have been repeated with another expression
vector (pCMX-SMRT) that directs the expression of a SMRT isoform
containing the authentic amino terminus with essentially identical
results (data not shown). This indicates that the first 28 amino acids
of this corepressor are not required to modulate 4HT’s ability to
activate ER-dependent gene expression.
The corepressor SMRT was reported to bind to TR and RAR in the absence, but not the presence, of their cognate ligands via a portion of the hinge region referred to as the CoR box (23, 43, 44). Although there is no homology between the CoR box and any region of the ER, three other structural motifs have been implicated in the association between corepressors and two orphans of the steroid receptor superfamily, Rev-ErbA and COUP-TF1; none displays significant homology to the CoR box or the ER (45, 46, 47). Thus, dissimilar receptor sequences facilitate interaction between different nuclear receptor superfamily members and SMRT. Although SMRT preferentially bound to a GST-ER fusion protein in comparison to GST alone, no hormone-dependent interaction was observed, and this could reflect differences between in vitro and in vivo binding conditions. For example, if hormone-dependent, ER-coactivator interactions contribute to the displacement/inactivation of corepressor in vivo, differences in ER-SMRT in vitro interactions are not likely to be observed. Alternatively, SMRT may interact with the hormone-independent AF1 domain of ER. Importantly, our data should not be used to implicate SMRT itself as the authentic, native corepressor for the ER. It is equally likely that another unidentified protein(s) regulates ER transcriptional activity with improved specificity and/or affinity.
Roles of Potential ER Corepressors
Although heat shock protein interactions contribute to maintaining
the ER in a transcriptionally inactive state within the cell (48),
under certain conditions ER is present within the nucleus and able to
bind DNA in the absence of ligand (49), suggesting that another
mechanism may inhibit this receptor’s basal transcriptional activity.
For instance, corepressors could recruit histone deacetylase activity
to a target gene promoter and thereby maintain chromatin in an inactive
state, directly interact with and inhibit the general transcription
complex formed at the promoter (TATA), inhibit functional
ER-coactivator interactions, or block the transcriptional synergism
between AF1 and AF2 required for full ER activity in most cell/promoter
contexts (6, 8, 9). Thus, it is postulated that the unliganded ER is
bound to a corepressor(s) that either dissociates or is inactivated
upon estrogen binding; the resulting conformational change would enable
the ER to preferentially associate with coactivator(s) and directly
and/or indirectly encourage the general transcriptional machinery to
activate target gene expression. In contexts where they act as
antagonists, mixed antiestrogens may induce a ligand-binding domain
conformation that enables the receptor to retain its ability to
interact with corepressor(s) and/or decreases its affinity for SRC-1
such that corepressors are not efficiently inactivated. Alternatively,
if the mixed antiestrogen-occupied ER simultaneously binds coactivators
and corepressors under these conditions, the repressor domain(s) of
corepressors may inhibit ER transcriptional activity by blocking the
activation function of coactivators.
The agonist activity of 4HT may manifest itself in tissues and cells where corepressor expression is low, ER transcriptional activity is stimulated by corepressor-insensitive coactivators and/or cell-specific corepressors are unable to bind to ER liganded with mixed antiestrogens. In support of the concept that an authentic ER corepressor may exist is the demonstration of a repressor domain within the ER’s ligand-binding domain (amino acids 370–470) that functions independently of heat shock protein interaction (50). Furthermore, there is a precedent for the existence of a corepressor(s) for "steroid" as opposed to a orphan (Rev-ErbA) or type II (TR and RAR) receptor. A repressor domain has been mapped within the extreme carboxy terminus of the progesterone receptor, and it appears to require an additional cellular factor(s) to inhibit transcription (51).
Implications of Coregulators for 4HT Biocharacter
Collectively, these data accumulated in model transfection assays
indicate that cellular coactivators and corepressors have the potential
to contribute to the overall ability of a mixed antiestrogen to
regulate ER target gene expression. At the tissue/organ mRNA level, the
coactivators and corepressors examined to date appear to be
ubiquitously expressed (22, 52, 53, 54, 55, 56), and presumably most, if not all,
cells contain both forms of coregulators. However, the relative
expression levels of known coactivators and corepressors have not been
assessed, and it is likely that novel coregulators of the nuclear
receptor superfamily remain to be identified. It is possible that
authentic ER corepressor proteins may be expressed at relatively high
levels in cells where 4HT is an antagonist and/or coactivators are
present in comparatively large amounts in contexts where 4HT is an
agonist. It is also likely that promoters contribute to the relative
balance of 4HT agonist/antagonist activity by imposing spatial
constraints on the ability of ER and coactivators/corepressors to make
protein-protein interactions.
Tamoxifen, in its role as an antiestrogen, is an important endocrine therapy for the treatment of breast cancer and more recently is being tested as a chemopreventative agent in women with a high risk of developing this disease (57). However, it also exerts estrogen-like effects in bone, liver and urogenital tissues; of which some (e.g. an increased occurrence rate of endometrial cancer) are clearly not beneficial (58). Our data highlights the necessity to understand the role that native intracellular factors play in the interpretation of tamoxifen/4HT biocharacter in cells/tissues that endogenously express ER and provides a theoretical rationale for the contribution of coregulatory proteins to the tissue-specific and gene-specific activity of ER agonists and antagonists.
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MATERIALS AND METHODS |
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TOPABSTRACTINTRODUCTIONRESULTSDISCUSSIONMATERIALS AND METHODSREFERENCES |
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Plasmid DNAs
The mammalian expression vectors for full-length hER (pSVMT-wER)
and the AF2 (D538A/E542A/D545A) mutant ER (pRST7-hER-3x)
and its corresponding wild type ER counterpart (pRST7-hER)
have been described previously (8, 29). The synthetic target genes,
ERE-E1b-CAT (29), pC3-Luc (8), and TK-C3ER1&2-Luc (24) have been used
in previous studies. Mammalian expression vectors for SMRT
(pABgalSMRT or pCMX-SMRT) and SRC-1 (pBK-SRC-1) and the
corresponding parent vectors (pABgal and pBK-CMV) were described
previously (22, 23, 47), as was the baculoviral expression vector,
pGST-hER (3).
The in vitro transcription vector for SMRT, pT7-SMRT(29–1495), was constructed as follows. First, human skeletal muscle poly(A)+ RNA (Clontech, Palo Alto, CA) was reverse transcribed using the primer, 5'-GCTGGCATGTTCCTGCACCG-3', and this material was used as a template cDNA for PCR amplification using the primers, 5'-AGCTGACGTCGACGCCTCGTG-3' and 5'-CTGCACCGCCTGGCTTCTAT-3'. The resulting product was cloned into the TA cloning vector, pCR3 (Invitrogen, Carlsbad, CA) to produce pCR3-SMRT(565–1289). Subsequently, this vector was digested with EcoRV and BglII and ligated with the EcoRI (filled) to BglII fragment of pGAD10-SMRT(1192–1495) to yield the pCR3-SMRT(565–1495) vector. The cDNA insert of pGAD10-SMRT(1192–1495) was isolated from a brain cDNA library by yeast two-hybrid assay using the ligand-binding domain of the human TR as bait. The SalI-XhoI fragment of pCR3-SMRT(565–1495) was isolated, repaired with Klenow DNA polymerase, and cloned into the NcoI-EcoRI (filled) site of the pT7ßSal vector (59) to produce pT7-SMRT(565–1495). Next, human skeletal muscle was reverse transcribed using the primer, 5'-GTGCGGGACTTGGCGATCT-3', and the resulting cDNA was amplified by PCR with the primers, 5'-AAGATTCCGAGCTCTGCTAC-3' and 5'-CACGAGGCGTCGACGTCAGC-3'. This PCR product was TA Cloned (Invitrogen) to create pCR3-SMRT(29–564). Finally, to construct pT7-SMRT(29–1495), the SalI fragment of pCR3-SMRT(29–564) was inserted into the SalI site of pT7-SMRT(565–1495).
Cell Culture and Transfections
HeLa and HepG2 cells were routinely maintained in DMEM
supplemented with 10% FBS. Twenty-four hours before transfection,
3 x 105 HeLa or 8 x 105 HepG2 cells
were seeded per well of a six-well multiwell dish in phenol red-free
DMEM containing 5% dextran-coated charcoal-stripped serum. Cells were
transfected with the indicated DNAs using Lipofectin (Life
Technologies, Grand Island, NY) according to the manufacturer’s
guidelines. Six hours later, the DNA/Lipofectin mixture was removed and
cells were fed with phenol red-free media containing 5% stripped serum
and the hormone treatments indicated in the figure legends. Twenty-four
hours thereafter, cells were harvested and extracts were assayed for
CAT (29) or luciferase activity using the Luciferase Assay System
(Promega, Madison, WI). Duplicate samples were measured in each
experiment, and data are presented as the average ±
SEM of at least three experiments.
Protein-Protein Interaction by GST Pull-down Assay
The full-length hER was expressed as a GST fusion protein in a
baculovirus expression system in the presence of ethanol (vehicle), 1
µM estradiol, or 1 µM tamoxifen and
purified using glutathione-Sepharose affinity chromatography as
described previously (60). Radiolabeled SMRT (amino acids 29–1495) was
produced from the pT7-SMRT(29–1495) vector with the TNT-Coupled
Reticulocyte Lysate System for in vitro transcription and
translation as recommended by the manufacturer (Promega).
To assess protein-protein interactions, equivalent levels of GST alone or GST-hER (as assessed by Coomassie staining) were incubated with glutathione-Sepharose 4B beads (Pharmacia, Piscataway, NJ) in NENT buffer (20 mM Tris, pH 8.0 containing 100 mM NaCl, 1 mM EDTA, and 0.5% NP-40) containing either ethanol, 1 µM E2, or 1 µM tamoxifen for 60 min at room temperature. Subsequently, the supernatant was removed and the beads were washed twice with NENT buffer. Eight microliters of 35S-labeled SMRT were incubated with the beads in NENT buffer containing vehicle, estrogen, or tamoxifen for 2 h at room temperature. Beads were washed five times with NENT buffer, dried, resuspended in 50 µl SDS-PAGE loading buffer, resolved by 7.5% SDS-PAGE, and visualized by fluorography.
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ACKNOWLEDGMENTS |
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FOOTNOTES |
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A portion of this work was presented at the 10th International Congress of Endocrinology, San Francisco, CA, June 12–15, 1996.
This work was supported by NIH Grant DK-48896 (to B.W.O.).
Received for publication February 14, 1997. Accepted for publication March 18, 1997.
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REFERENCES |
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TOPABSTRACTINTRODUCTIONRESULTSDISCUSSIONMATERIALS AND METHODSREFERENCES |
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is dependent on the signature motif and helix 5 in the
ligand binding domain: silencing does not involve an interaction with
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M. Lupien, M. Jeyakumar, E. Hebert, K. Hilmi, D. Cotnoir-White, C. Loch, A. Auger, G. Dayan, G.-A. Pinard, J.-M. Wurtz, et al. Raloxifene and ICI182,780 Increase Estrogen Receptor-{alpha} Association with a Nuclear Compartment via Overlapping Sets of Hydrophobic Amino Acids in Activation Function 2 Helix 12 Mol. Endocrinol., April 1, 2007; 21(4): 797 - 816. [Abstract] [Full Text] [PDF]
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J. N. Miner, W. Chang, M. S. Chapman, P. D. Finn, M. H. Hong, F. J. Lopez, K. B. Marschke, J. Rosen, W. Schrader, R. Turner, et al. An Orally Active Selective Androgen Receptor Modulator Is Efficacious on Bone, Muscle, and Sex Function with Reduced Impact on Prostate Endocrinology, January 1, 2007; 148(1): 363 - 373. [Abstract] [Full Text] [PDF]
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M. Mc Ilroy, F. J Fleming, Y. Buggy, A. D K Hill, and L. S Young Tamoxifen-induced ER-{alpha}-SRC-3 interaction in HER2 positive human breast cancer; a possible mechanism for ER isoform specific recurrence Endocr. Relat. Cancer, December 1, 2006; 13(4): 1135 - 1145. [Abstract] [Full Text] [PDF]
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B. Moy and P. E. Goss Estrogen Receptor Pathway: Resistance to Endocrine Therapy and New Therapeutic Approaches. Clin. Cancer Res., August 15, 2006; 12(16): 4790 - 4793. [Abstract] [Full Text] [PDF]
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D. Sharma, N. K. Saxena, N. E. Davidson, and P. M. Vertino Restoration of Tamoxifen Sensitivity in Estrogen Receptor-Negative Breast Cancer Cells: Tamoxifen-Bound Reactivated ER Recruits Distinctive Corepressor Complexes. Cancer Res., June 15, 2006; 66(12): 6370 - 6378. [Abstract] [Full Text] [PDF]
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H.-G. Yoon and J. Wong The Corepressors Silencing Mediator of Retinoid and Thyroid Hormone Receptor and Nuclear Receptor Corepressor Are Involved in Agonist- and Antagonist-Regulated Transcription by Androgen Receptor Mol. Endocrinol., May 1, 2006; 20(5): 1048 - 1060. [Abstract] [Full Text] [PDF]
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L. Lipfert, J. E. Fisher, N. Wei, A. Scafonas, Q. Su, J. Yudkovitz, F. Chen, S. Warrier, E. T. Birzin, S. Kim, et al. Antagonist-Induced, Activation Function-2-Independent Estrogen Receptor {alpha} Phosphorylation Mol. Endocrinol., March 1, 2006; 20(3): 516 - 533. [Abstract] [Full Text] [PDF]
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A. Vivacqua, D. Bonofiglio, A. G. Recchia, A. M. Musti, D. Picard, S. Ando, and M. Maggiolini The G Protein-Coupled Receptor GPR30 Mediates the Proliferative Effects Induced by 17{beta}-Estradiol and Hydroxytamoxifen in Endometrial Cancer Cells Mol. Endocrinol., March 1, 2006; 20(3): 631 - 646. [Abstract] [Full Text] [PDF]
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T. Iwasaki, A. Takeshita, W. Miyazaki, W. W. Chin, and N. Koibuchi The Interaction of TR{beta}1-N Terminus with Steroid Receptor Coactivator-1 (SRC-1) Serves a Full Transcriptional Activation Function of SRC-1 Endocrinology, March 1, 2006; 147(3): 1452 - 1457. [Abstract] [Full Text] [PDF]
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S. H. Baek, K. A. Ohgi, C. A. Nelson, D. Welsbie, C. Chen, C. L. Sawyers, D. W. Rose, and M. G. Rosenfeld Ligand-specific allosteric regulation of coactivator functions of androgen receptor in prostate cancer cells PNAS, February 28, 2006; 103(9): 3100 - 3105. [Abstract] [Full Text] [PDF]
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M. Albers, B. Blume, T. Schlueter, M. B. Wright, I. Kober, C. Kremoser, U. Deuschle, and M. Koegl A Novel Principle for Partial Agonism of Liver X Receptor Ligands: COMPETITIVE RECRUITMENT OF ACTIVATORS AND REPRESSORS J. Biol. Chem., February 24, 2006; 281(8): 4920 - 4930. [Abstract] [Full Text] [PDF]
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S. P. Linke, T. M. Bremer, C. D. Herold, G. Sauter, and C. Diamond A Multimarker Model to Predict Outcome in Tamoxifen-Treated Breast Cancer Patients Clin. Cancer Res., February 15, 2006; 12(4): 1175 - 1183. [Abstract] [Full Text] [PDF]
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H. Zhang, X. Xie, X. Zhu, J. Zhu, C. Hao, Q. Lu, L. Ding, Y. Liu, L. Zhou, Y. Liu, et al. Stimulatory Cross-talk between NFAT3 and Estrogen Receptor in Breast Cancer Cells J. Biol. Chem., December 30, 2005; 280(52): 43188 - 43197. [Abstract] [Full Text] [PDF]
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J. Huang, X. Li, C. A. Maguire, R. Hilf, R. A. Bambara, and M. Muyan Binding of Estrogen Receptor {beta} to Estrogen Response Element in Situ Is Independent of Estradiol and Impaired by Its Amino Terminus Mol. Endocrinol., November 1, 2005; 19(11): 2696 - 2712. [Abstract] [Full Text] [PDF]
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S. J. Han, J. Jeong, F. J. DeMayo, J. Xu, S. Y. Tsai, M.-J. Tsai, and B. W. O'Malley Dynamic Cell Type Specificity of SRC-1 Coactivator in Modulating Uterine Progesterone Receptor Function in Mice Mol. Cell. Biol., September 15, 2005; 25(18): 8150 - 8165. [Abstract] [Full Text] [PDF]
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J. Frasor, J. M. Danes, C. C. Funk, and B. S. Katzenellenbogen Estrogen down-regulation of the corepressor N-CoR: Mechanism and implications for estrogen derepression of N-CoR-regulated genes PNAS, September 13, 2005; 102(37): 13153 - 13157. [Abstract] [Full Text] [PDF]
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K-M Rau, H-Y Kang, T-L Cha, S A Miller, and M-C Hung The mechanisms and managements of hormone-therapy resistance in breast and prostate cancers Endocr. Relat. Cancer, September 1, 2005; 12(3): 511 - 532. [Abstract] [Full Text] [PDF]
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D. Wang and S. S. Simons Jr. Corepressor Binding to Progesterone and Glucocorticoid Receptors Involves the Activation Function-1 Domain and Is Inhibited by Molybdate Mol. Endocrinol., June 1, 2005; 19(6): 1483 - 1500. [Abstract] [Full Text] [PDF]
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E. K. Keeton and M. Brown Cell Cycle Progression Stimulated by Tamoxifen-Bound Estrogen Receptor-{alpha} and Promoter-Specific Effects in Breast Cancer Cells Deficient in N-CoR and SMRT Mol. Endocrinol., June 1, 2005; 19(6): 1543 - 1554. [Abstract] [Full Text] [PDF]
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B. W. O'Malley A Life-Long Search for the Molecular Pathways of Steroid Hormone Action Mol. Endocrinol., June 1, 2005; 19(6): 1402 - 1411. [Abstract] [Full Text] [PDF]
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R.-C. Wu, C. L. Smith, and B. W. O'Malley Transcriptional Regulation by Steroid Receptor Coactivator Phosphorylation Endocr. Rev., May 1, 2005; 26(3): 393 - 399. [Abstract] [Full Text] [PDF]
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K. Chwalisz, M. C. Perez, D. DeManno, C. Winkel, G. Schubert, and W. Elger Selective Progesterone Receptor Modulator Development and Use in the Treatment of Leiomyomata and Endometriosis Endocr. Rev., May 1, 2005; 26(3): 423 - 438. [Abstract] [Full Text] [PDF]
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C. K. Osborne and R. Schiff Estrogen-Receptor Biology: Continuing Progress and Therapeutic Implications J. Clin. Oncol., March 10, 2005; 23(8): 1616 - 1622. [Full Text] [PDF]
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C. J. Fabian and B. F. Kimler Selective Estrogen-Receptor Modulators for Primary Prevention of Breast Cancer J. Clin. Oncol., March 10, 2005; 23(8): 1644 - 1655. [Full Text] [PDF]
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J A Vendrell, I Bieche, C Desmetz, E Badia, S Tozlu, C Nguyen, J C Nicolas, R Lidereau, and P A Cohen Molecular changes associated with the agonist activity of hydroxy-tamoxifen and the hyper-response to estradiol in hydroxy-tamoxifen-resistant breast cancer cell lines Endocr. Relat. Cancer, March 1, 2005; 12(1): 75 - 92. [Abstract] [Full Text] [PDF]
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Y. M. Shah and B. G. Rowan The Src Kinase Pathway Promotes Tamoxifen Agonist Action in Ishikawa Endometrial Cells through Phosphorylation-Dependent Stabilization of Estrogen Receptor {alpha} Promoter Interaction and Elevated Steroid Receptor Coactivator 1 Activity Mol. Endocrinol., March 1, 2005; 19(3): 732 - 748. [Abstract] [Full Text] [PDF]
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M. C. Hodgson, I. Astapova, S. Cheng, L. J. Lee, M. C. Verhoeven, E. Choi, S. P. Balk, and A. N. Hollenberg The Androgen Receptor Recruits Nuclear Receptor CoRepressor (N-CoR) in the Presence of Mifepristone via Its N and C Termini Revealing a Novel Molecular Mechanism for Androgen Receptor Antagonists J. Biol. Chem., February 25, 2005; 280(8): 6511 - 6519. [Abstract] [Full Text] [PDF]
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J. Jyrkkarinne, B. Windshugel, J. Makinen, M. Ylisirnio, M. Perakyla, A. Poso, W. Sippl, and P. Honkakoski Amino Acids Important for Ligand Specificity of the Human Constitutive Androstane Receptor J. Biol. Chem., February 18, 2005; 280(7): 5960 - 5971. [Abstract] [Full Text] [PDF]
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S. Cho, B. L. Kagan, J. A. Blackford Jr., D. Szapary, and S. S. Simons Jr. Glucocorticoid Receptor Ligand Binding Domain Is Sufficient for the Modulation of Glucocorticoid Induction Properties by Homologous Receptors, Coactivator Transcription Intermediary Factor 2, and Ubc9 Mol. Endocrinol., February 1, 2005; 19(2): 290 - 311. [Abstract] [Full Text] [PDF]
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C. K. Osborne, J. Shou, S. Massarweh, and R. Schiff Crosstalk between Estrogen Receptor and Growth Factor Receptor Pathways as a Cause for Endocrine Therapy Resistance in Breast Cancer Clin. Cancer Res., January 15, 2005; 11(2): 865s - 870s. [Abstract] [Full Text] [PDF]
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D. P. McDonnell The Molecular Pharmacology of Estrogen Receptor Modulators: Implications for the Treatment of Breast Cancer Clin. Cancer Res., January 15, 2005; 11(2): 871s - 877s. [Abstract] [Full Text] [PDF]
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V. Pogenberg, J.-F. Guichou, V. Vivat-Hannah, S. Kammerer, E. Perez, P. Germain, A. R. de Lera, H. Gronemeyer, C. A. Royer, and W. Bourguet Characterization of the Interaction between Retinoic Acid Receptor/Retinoid X Receptor (RAR/RXR) Heterodimers and Transcriptional Coactivators through Structural and Fluorescence Anisotropy Studies J. Biol. Chem., January 14, 2005; 280(2): 1625 - 1633. [Abstract] [Full Text] [PDF]
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A. Ring and M. Dowsett Mechanisms of tamoxifen resistance Endocr. Relat. Cancer, December 1, 2004; 11(4): 643 - 658. [Abstract] [Full Text] [PDF]
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M. H. Herynk and S. A. W. Fuqua Estrogen Receptor Mutations in Human Disease Endocr. Rev., December 1, 2004; 25(6): 869 - 898. [Abstract] [Full Text] [PDF]
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C E Waters, A Stevens, A White, and D W Ray Analysis of co-factor function in a glucocorticoid-resistant small cell carcinoma cell line J. Endocrinol., November 1, 2004; 183(2): 375 - 383. [Abstract] [Full Text] [PDF]
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M. A. Loven, R. E. Davis, C. D. Curtis, N. Muster, J. R. Yates, and A. M. Nardulli A Novel Estrogen Receptor {alpha}-Associated Protein Alters Receptor-Deoxyribonucleic Acid Interactions and Represses Receptor-Mediated Transcription Mol. Endocrinol., November 1, 2004; 18(11): 2649 - 2659. [Abstract] [Full Text] [PDF]
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C M Klinge, S C Jernigan, K A Mattingly, K E Risinger, and J Zhang Estrogen response element-dependent regulation of transcriptional activation of estrogen receptors {alpha} and {beta} by coactivators and corepressors J. Mol. Endocrinol., October 1, 2004; 33(2): 387 - 410. [Abstract] [Full Text] [PDF]
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D. Masiello, S.-Y. Chen, Y. Xu, M. C. Verhoeven, E. Choi, A. N. Hollenberg, and S. P. Balk Recruitment of {beta}-Catenin by Wild-Type or Mutant Androgen Receptors Correlates with Ligand-Stimulated Growth of Prostate Cancer Cells Mol. Endocrinol., October 1, 2004; 18(10): 2388 - 2401. [Abstract] [Full Text] [PDF]
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A. H. Talukder, A. Gururaj, S. K. Mishra, R. K. Vadlamudi, and R. Kumar Metastasis-Associated Protein 1 Interacts with NRIF3, an Estrogen-Inducible Nuclear Receptor Coregulator Mol. Cell. Biol., August 1, 2004; 24(15): 6581 - 6591. [Abstract] [Full Text] [PDF]
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M. B. Buck, K. Pfizenmaier, and C. Knabbe Antiestrogens Induce Growth Inhibition by Sequential Activation of p38 Mitogen-Activated Protein Kinase and Transforming Growth Factor-{beta} Pathways in Human Breast Cancer Cells Mol. Endocrinol., July 1, 2004; 18(7): 1643 - 1657. [Abstract] [Full Text] [PDF]
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Q. Wang, J. A. Blackford Jr., L.-N. Song, Y. Huang, S. Cho, and S. S. Simons Jr. Equilibrium Interactions of Corepressors and Coactivators with Agonist and Antagonist Complexes of Glucocorticoid Receptors Mol. Endocrinol., June 1, 2004; 18(6): 1376 - 1395. [Abstract] [Full Text] [PDF]
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N. Heldring, M. Nilsson, B. Buehrer, E. Treuter, and J.-A. Gustafsson Identification of Tamoxifen-Induced Coregulator Interaction Surfaces within the Ligand-Binding Domain of Estrogen Receptors Mol. Cell. Biol., April 15, 2004; 24(8): 3445 - 3459. [Abstract] [Full Text] [PDF]
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X.-f. Liu and M. K. Bagchi Recruitment of Distinct Chromatin-modifying Complexes by Tamoxifen-complexed Estrogen Receptor at Natural Target Gene Promoters in Vivo J. Biol. Chem., April 9, 2004; 279(15): 15050 - 15058. [Abstract] [Full Text] [PDF]
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B. J. Long, D. Jelovac, V. Handratta, A. Thiantanawat, N. MacPherson, J. Ragaz, O. G. Goloubeva, and A. M. Brodie Therapeutic Strategies Using the Aromatase Inhibitor Letrozole and Tamoxifen in a Breast Cancer Model J Natl Cancer Inst, March 17, 2004; 96(6): 456 - 465. [Abstract] [Full Text] [PDF]
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J. Frasor, F. Stossi, J. M. Danes, B. Komm, C. R. Lyttle, and B. S. Katzenellenbogen Selective Estrogen Receptor Modulators: Discrimination of Agonistic versus Antagonistic Activities by Gene Expression Profiling in Breast Cancer Cells Cancer Res., February 15, 2004; 64(4): 1522 - 1533. [Abstract] [Full Text] [PDF]
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C. L. Smith and B. W. O'Malley Coregulator Function: A Key to Understanding Tissue Specificity of Selective Receptor Modulators Endocr. Rev., February 1, 2004; 25(1): 45 - 71. [Abstract] [Full Text] [PDF]
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A. Vienonen, S. Miettinen, M. Blauer, P. M. Martikainen, E. Tomas, P. K. Heinonen, and T. Ylikomi Expression of Nuclear Receptors and Cofacotrs in Human Endometrium and Myometrium Reproductive Sciences, February 1, 2004; 11(2): 104 - 112. [Abstract] [PDF]
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L.-N. Song, M. Coghlan, and E. P. Gelmann Antiandrogen Effects of Mifepristone on Coactivator and Corepressor Interactions with the Androgen Receptor Mol. Endocrinol., January 1, 2004; 18(1): 70 - 85. [Abstract] [Full Text] [PDF]
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V. Y. Lin, E. M. Resnick, and M. A. Shupnik Truncated Estrogen Receptor Product-1 Stimulates Estrogen Receptor {alpha} Transcriptional Activity by Titration of Repressor Proteins J. Biol. Chem., October 3, 2003; 278(40): 38125 - 38131. [Abstract] [Full Text] [PDF]
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D. Chen, M. J. Lucey, F. Phoenix, J. Lopez-Garcia, S. M. Hart, R. Losson, L. Buluwela, R. C. Coombes, P. Chambon, P. Schar, et al. T:G Mismatch-specific Thymine-DNA Glycosylase Potentiates Transcription of Estrogen-regulated Genes through Direct Interaction with Estrogen Receptor {alpha} J. Biol. Chem., October 3, 2003; 278(40): 38586 - 38592. [Abstract] [Full Text] [PDF]
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J. Xu and Q. Li Review of the in Vivo Functions of the p160 Steroid Receptor Coactivator Family Mol. Endocrinol., September 1, 2003; 17(9): 1681 - 1692. [Abstract] [Full Text] [PDF]
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I. U. Agoulnik, W. C. Krause, W. E. Bingman III, H. T. Rahman, M. Amrikachi, G. E. Ayala, and N. L. Weigel Repressors of Androgen and Progesterone Receptor Action J. Biol. Chem., August 15, 2003; 278(33): 31136 - 31148. [Abstract] [Full Text] [PDF]
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A. J. Morrison, R. E. Herrera, E. C. Heinsohn, R. Schiff, and C. K. Osborne Dominant-Negative Nuclear Receptor Corepressor Relieves Transcriptional Inhibition of Retinoic Acid Receptor but Does Not Alter the Agonist/Antagonist Activities of the Tamoxifen-Bound Estrogen Receptor Mol. Endocrinol., August 1, 2003; 17(8): 1543 - 1554. [Abstract] [Full Text] [PDF]
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T. Fujita, Y. Kobayashi, O. Wada, Y. Tateishi, L. Kitada, Y. Yamamoto, H. Takashima, A. Murayama, T. Yano, T. Baba, et al. Full Activation of Estrogen Receptor {alpha} Activation Function-1 Induces Proliferation of Breast Cancer Cells J. Biol. Chem., July 11, 2003; 278(29): 26704 - 26714. [Abstract] [Full Text] [PDF]
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C. Zhao, A. Koide, J. Abrams, S. Deighton-Collins, A. Martinez, J. A. Schwartz, S. Koide, and D. F. Skafar Mutation of Leu-536 in Human Estrogen Receptor-{alpha} Alters the Coupling between Ligand Binding, Transcription Activation, and Receptor Conformation J. Biol. Chem., July 11, 2003; 278(29): 27278 - 27286. [Abstract] [Full Text] [PDF]
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M. Dutertre and C. L. Smith Ligand-Independent Interactions of p160/Steroid Receptor Coactivators and CREB-Binding Protein (CBP) with Estrogen Receptor-{alpha}: Regulation by Phosphorylation Sites in the A/B Region Depends on Other Receptor Domains Mol. Endocrinol., July 1, 2003; 17(7): 1296 - 1314. [Abstract] [Full Text] [PDF]
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S. K. Mishra, A. Mazumdar, R. K. Vadlamudi, F. Li, R.-A. Wang, W. Yu, V. C. Jordan, R. J. Santen, and R. Kumar MICoA, a Novel Metastasis-associated Protein 1 (MTA1) Interacting Protein Coactivator, Regulates Estrogen Receptor-{alpha} Transactivation Functions J. Biol. Chem., May 23, 2003; 278(21): 19209 - 19219. [Abstract] [Full Text] [PDF]
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A. Stevens, H. Garside, A. Berry, C. Waters, A. White, and D. Ray Dissociation of Steroid Receptor Coactivator 1 and Nuclear Receptor Corepressor Recruitment to the Human Glucocorticoid Receptor by Modification of the Ligand-Receptor Interface: The Role of Tyrosine 735 Mol. Endocrinol., May 1, 2003; 17(5): 845 - 859. [Abstract] [Full Text] [PDF]
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B. Farboud, H. Hauksdottir, Y. Wu, and M. L. Privalsky Isotype-Restricted Corepressor Recruitment: a Constitutively Closed Helix 12 Conformation in Retinoic Acid Receptors {beta} and {gamma} Interferes with Corepressor Recruitment and Prevents Transcriptional Repression Mol. Cell. Biol., April 15, 2003; 23(8): 2844 - 2858. [Abstract] [Full Text] [PDF]
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E. K. Keeton and M. Brown Coregulator Expression and Breast Cancer: Improving the Predictive Power of Estrogen Receptor {alpha} Clin. Cancer Res., April 1, 2003; 9(4): 1229 - 1230. [Full Text] [PDF]
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I. Girault, F. Lerebours, S. Amarir, S. Tozlu, M. Tubiana-Hulin, R. Lidereau, and I. Bieche Expression Analysis of Estrogen Receptor {alpha} Coregulators in Breast Carcinoma: Evidence That NCOR1 Expression Is Predictive of the Response to Tamoxifen Clin. Cancer Res., April 1, 2003; 9(4): 1259 - 1266. [Abstract] [Full Text] [PDF]
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C. K. Osborne, V. Bardou, T. A. Hopp, G. C. Chamness, S. G. Hilsenbeck, S. A. W. Fuqua, J. Wong, D. C. Allred, G. M. Clark, and R. Schiff Role of the Estrogen Receptor Coactivator AIB1 (SRC-3) and HER-2/neu in Tamoxifen Resistance in Breast Cancer J Natl Cancer Inst, March 5, 2003; 95(5): 353 - 361. [Abstract] [Full Text] [PDF]
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S. F. Doisneau-Sixou, P. Cestac, S. Chouini, J. S. Carroll, A. D. Hamilton, S. M. Sebti, M. Poirot, P. Balaguer, J.-C. Faye, R. L. Sutherland, et al. Contrasting Effects of Prenyltransferase Inhibitors on Estrogen-Dependent Cell Cycle Progression and Estrogen Receptor-Mediated Transcriptional Activity in MCF-7 Cells Endocrinology, March 1, 2003; 144(3): 989 - 998. [Abstract] [Full Text] [PDF]
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G. Liao, L.-Y. Chen, A. Zhang, A. Godavarthy, F. Xia, J. C. Ghosh, H. Li, and J. D. Chen Regulation of Androgen Receptor Activity by the Nuclear Receptor Corepressor SMRT J. Biol. Chem., February 7, 2003; 278(7): 5052 - 5061. [Abstract] [Full Text] [PDF]
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R. Schiff, S. Massarweh, J. Shou, and C. K. Osborne Breast Cancer Endocrine Resistance: How Growth Factor Signaling and Estrogen Receptor Coregulators Modulate Response Clin. Cancer Res., January 1, 2003; 9(1): 447s - 454s. [Abstract] [Full Text]
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E. Demirpence, A. Semlali, J. Oliva, P. Balaguer, E. Badia, M.-J. Duchesne, J.-C. Nicolas, and M. Pons An Estrogen-responsive Element-targeted Histone Deacetylase Enzyme Has an Antiestrogen Activity That Differs from That of Hydroxytamoxifen Cancer Res., November 15, 2002; 62(22): 6519 - 6528. [Abstract] [Full Text] [PDF]
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A. N. Moraitis, V. Giguere, and C. C. Thompson Novel Mechanism of Nuclear Receptor Corepressor Interaction Dictated by Activation Function 2 Helix Determinants Mol. Cell. Biol., October 1, 2002; 22(19): 6831 - 6841. [Abstract] [Full Text] [PDF]
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Y.-C. Hu, C.-R. Shyr, W. Che, X.-M. Mu, E. Kim, and C. Chang Suppression of Estrogen Receptor-mediated Transcription and Cell Growth by Interaction with TR2 Orphan Receptor J. Biol. Chem., September 6, 2002; 277(37): 33571 - 33579. [Abstract] [Full Text] [PDF]
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A. Takeshita, M. Taguchi, N. Koibuchi, and Y. Ozawa Putative Role of the Orphan Nuclear Receptor SXR (Steroid and Xenobiotic Receptor) in the Mechanism of CYP3A4 Inhibition by Xenobiotics J. Biol. Chem., August 30, 2002; 277(36): 32453 - 32458. [Abstract] [Full Text] [PDF]
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I. Dussault, M. Lin, K. Hollister, M. Fan, J. Termini, M. A. Sherman, and B. M. Forman A Structural Model of the Constitutive Androstane Receptor Defines Novel Interactions That Mediate Ligand-Independent Activity Mol. Cell. Biol., August 1, 2002; 22(15): 5270 - 5280. [Abstract] [Full Text] [PDF]
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 J D Tugwood and C T Montague Biology and toxicology of PPARg ligands Human and Experimental Toxicology, August 1, 2002; 21(8): 429 - 437. [Abstract] [PDF]
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H.-J. Huang, J. D. Norris, and D. P. McDonnell Identification of a Negative Regulatory Surface within Estrogen Receptor {alpha} Provides Evidence in Support of a Role for Corepressors in Regulating Cellular Responses to Agonists and Antagonists Mol. Endocrinol., August 1, 2002; 16(8): 1778 - 1792. [Abstract] [Full Text] [PDF]
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M. Schulz, M. Eggert, A. Baniahmad, A. Dostert, T. Heinzel, and R. Renkawitz RU486-induced Glucocorticoid Receptor Agonism Is Controlled by the Receptor N Terminus and by Corepressor Binding J. Biol. Chem., July 12, 2002; 277(29): 26238 - 26243. [Abstract] [Full Text] [PDF]
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