Estrogen Receptor-ß: An Important Player in Estrogen Action

2001 ◽  
pp. 144-148
Author(s):  
Jan-Åke Gustafsson
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Action ◽  
Important Player

scholarly journals A transcriptionally active estrogen receptor mutant is a novel type of dominant negative inhibitor of estrogen action.

1996 ◽  
Vol 10 (12) ◽  
pp. 1519-1526 ◽  
Author(s):  
E M McInerney ◽  
B A Ince ◽  
D J Shapiro ◽  
B S Katzenellenbogen
Keyword(s):  
Estrogen Receptor ◽  
Dominant Negative ◽  
Estrogen Action ◽  
Dominant Negative Inhibitor ◽  
Receptor Mutant

scholarly journals Estrogen Receptor β, But Not Estrogen Receptor α, Is Present in the Vascular Endothelium of the Human and Nonhuman Primate Endometrium1

2001 ◽  
Vol 86 (3) ◽  
pp. 1370-1378 ◽  
Author(s):  
Hilary O. D. Critchley ◽  
Robert M. Brenner ◽  
Teresa A. Henderson ◽  
Karin Williams ◽  
Nihar R. Nayak ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Vascular Endothelium ◽  
Estrogen Receptor Β ◽  
Glandular Cell ◽  
Receptor Subtypes ◽  
Cell Nuclei ◽  
Perivascular Cells ◽  
Estrogen Action ◽  
Secretory Phase ◽  
Western Blots

Estrogen action is dependent upon the presence of specific ligand-activated receptors in target tissues. The aim of the present experiments was to compare the spatial and temporal pattern of expression of estrogen receptor β (ERβ) with that of ERα in full thickness endometrial samples (from the superficial to the basal zone) obtained from both women and rhesus macaques. Immunohistochemical localization with specific antibodies revealed that ERα and ERβ were both expressed in nuclei of the glands and stroma. Consistent with previous studies, expression of ERα declined in the glands and stroma of the functionalis during the secretory phase. The luminal epithelium also displayed positive immunoreactivity for ERβ. Expression of ERβ declined in glandular cell nuclei, but not stroma, within the functionalis during the late secretory phase. Levels of expression of ERα and ERβ in all cellular compartments remained unchanged in the basalis. Both receptor subtypes were detected on Western blots using proteins extracted from uterine samples obtained throughout the menstrual cycle. There was a striking contrast between the pattern of expression of ERα and ERβ in the vascular endothelium and the perivascular cells surrounding endometrial blood vessels; only ERβ was present in the endothelial cell population, although both forms of ER were expressed in perivascular cells. We conclude that estrogen action(s) within the vascular endothelium in the endometrium may be mediated via direct binding to the ERβ isoform and that these cells could therefore be a target for agonists or antagonists that selectively target the β form of the ER.

Identification of a Novel Isoform of Estrogen Receptor, a Potential Inhibitor of Estrogen Action, in Vascular Smooth Muscle Cells

1996 ◽  
Vol 219 (3) ◽  
pp. 766-772 ◽  
Author(s):  
Satoshi Inoue ◽  
Shin-jiro Hoshino ◽  
Hideyuki Miyoshi ◽  
Masahiro Akishita ◽  
Takayuki Hosoi ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Smooth Muscle ◽  
Vascular Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Vascular Smooth Muscle Cells ◽  
Muscle Cells ◽  
Estrogen Action ◽  
Potential Inhibitor

scholarly journals A Set of Time-Resolved Fluorescence Resonance Energy Transfer Assays for the Discovery of Inhibitors of Estrogen Receptor-Coactivator Binding

2009 ◽  
Vol 14 (2) ◽  
pp. 181-193 ◽  
Author(s):  
Jillian R. Gunther ◽  
Yuhong Du ◽  
Eric Rhoden ◽  
Iestyn Lewis ◽  
Brian Revennaugh ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Energy Transfer ◽  
Fluorescence Resonance Energy Transfer ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Time Resolved Fluorescence ◽  
Estrogen Action ◽  
Alternative Mode ◽  
Time Resolved ◽  
Fluorescence Resonance

Therapeutic block of estrogen action is typically achieved with conventional antagonists (CAs), compounds that displace estradiol from the estrogen receptor (ER) and induce formation of an ER conformation that cannot bind to coactivator proteins, such as the steroid receptor coactivators (SRCs). As an alternative mode for blocking estrogen action, the authors seek small molecules that act as coactivator binding inhibitors (CBIs)—that is, they compete directly with SRC3 for interaction with estradiol-bound ER. CBIs would be interesting mechanistic probes of estrogen action and might also provide an alternative, more durable endocrine therapy for hormone-responsive breast cancer, where cellular adaptations lead to resistance to CAs. The authors have designed and optimized a set of time-resolved fluorescence resonance energy transfer (TR-FRET) assays to monitor the interaction of ER with SRC3 and ligands, and they have used them in high-throughput screens to discover small-molecule CBIs that are able to disrupt this interaction. These assays also distinguish CBIs from CAs. These robust and sensitive “mix-and-measure” assays use low concentrations of ER labeled with a europium chelate as FRET donor and a Cy5-labeled SRC as acceptor. This multiplexed protocol produces excellent signal-to-noise ratios (>100) and Z′ values (>0.8). ( Journal of Biomolecular Screening 2009:181-193)

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