scholarly journals Mechanisms of transcriptional activation of the mouse claudin-5 promoter by estrogen receptor alpha and beta

2014 ◽  
Vol 392 (1-2) ◽  
pp. 144-151 ◽  
Author(s):  
Malgorzata Burek ◽  
Katrin Steinberg ◽  
Carola Y. Förster
Keyword(s):  
Estrogen Receptor ◽  
Transcriptional Activation ◽  
Estrogen Receptor Alpha ◽  
Receptor Alpha

Requirement of protein l-isoaspartyl O-methyltransferase for transcriptional activation of trefoil factor 1 (TFF1) gene by estrogen receptor alpha

2012 ◽  
Vol 420 (2) ◽  
pp. 223-229 ◽  
Author(s):  
Jong Woo Park ◽  
Jae Cheol Lee ◽  
Shin Won Ha ◽  
So Young Bang ◽  
Eun Kyung Park ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Transcriptional Activation ◽  
Estrogen Receptor Alpha ◽  
Trefoil Factor ◽  
Protein L ◽  
Receptor Alpha ◽  
Trefoil Factor 1

scholarly journals BCAS2 Enhances Carcinogenic Effects of Estrogen Receptor Alpha in Breast Cancer Cells

2019 ◽  
Vol 20 (4) ◽  
pp. 966 ◽  
Author(s):  
Ángel Salmerón-Hernández ◽  
María Noriega-Reyes ◽  
Albert Jordan ◽  
Noemi Baranda-Avila ◽  
Elizabeth Langley
Keyword(s):  
Breast Cancer ◽  
Estrogen Receptor ◽  
Cancer Cells ◽  
Transcriptional Activation ◽  
Cancer Biology ◽  
Breast Cancer Cells ◽  
Estrogen Receptor Alpha ◽  
Receptor Alpha

Estrogen receptor alpha (ERα) has an established role in breast cancer biology. Transcriptional activation by ERα is a multistep process modulated by coactivator and corepressor proteins. Breast Cancer Amplified Sequence 2 (BCAS2), is a poorly studied ERα coactivator. In this work, we characterize some of the mechanisms through which this protein increases ERα activity and how this promotes carcinogenic processes in breast cancer cells. Using protein-protein interaction and luciferase assays we show that BCAS2 interacts with ERα both in vitro and in vivo and upregulates transcriptional activation of ERα directly through its N-terminal region (AF-1) and indirectly through its C-terminal (AF-2) region, acting in concert with AF-2 interacting coactivators. Elevated expression of BCAS2 positively affects proliferation, clonogenicity and migration of breast cancer cells and directly activates ERα regulated genes which have been shown to play a role in tumor growth and progression. Finally, we used signal transduction pathway inhibitors to elucidate how BCAS2 is regulated in these cells and observed that BCAS2 is preferentially regulated by the PI3K/AKT signaling pathway. BCAS2 is an AF-1 coactivator of ERα whose overexpression promotes carcinogenic processes, suggesting an important role in the development of estrogen-receptor positive breast cancer.

scholarly journals Estrogen response element binding induces alterations in estrogen receptor-alpha conformation as revealed by susceptibility to partial proteolysis

2001 ◽  
Vol 27 (3) ◽  
pp. 275-292 ◽  
Author(s):  
TL Ramsey ◽  
CM Klinge
Keyword(s):  
Estrogen Receptor ◽  
Conformational Changes ◽  
Transcriptional Activation ◽  
Estrogen Receptor Alpha ◽  
Single Copy ◽  
Trypsin Digestion ◽  
Western Blots ◽  
Receptor Alpha ◽  
Estrogen Response ◽  
Increased Sensitivity

Genes whose expression is highly induced by estradiol (E(2)) contain multiple estrogen response elements (EREs) in their promoters. Previously we reported that estrogen receptor-alpha (ERalpha) binds cooperatively to and E(2) synergistically activates reporter gene expression from three or four tandem copies of a consensus ERE (EREc38). Here we evaluated how ERalpha binding to one, two, three or four tandem copies of EREc38 affects ERalpha conformation as detected by altered ERalpha trypsin digestion patterns in Western blots. E(2)- or 4hydroxytamoxifen (4-OHT)-occupied ERalpha bound to the pS2 ERE or to a single copy of EREc38 showed enhanced susceptibility to trypsin digestion compared to E(2)- or 4-OHT-ERalpha incubated with DNA lacking an ERE. ERalpha binding to multiple tandem copies of EREc38 further increased sensitivity to trypsin digestion. These results correlate with synergistic transcription and cooperativity of ERalpha binding to multiple tandem copies of EREc38. These observations suggest that EREc38 binding alters the overall conformation of ERalpha and that multiple tandem copies of EREc38 enhance these conformational changes. We hypothesize that ERE-induced alterations in ERalpha conformation modulate interaction with coregulatory proteins, resulting in synergistic transcriptional activation.

Die Kaffee-vermittelte Induktion von UDP-Glukuronosyltransferasen wird durch den Estrogen-Receptor-alpha (ESR-1) geschlechtspezifisch reguliert

2011 ◽  
Vol 49 (08) ◽  
Author(s):  
S Kalthoff ◽  
A Winkler ◽  
N Freiberg ◽  
M Manns ◽  
C Strassburg
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptor Alpha ◽  
Receptor Alpha

Mice lacking estrogen receptor [alpha] in hypothalamic POMC neurons display enhanced estrogenic response on cortical bone mass

2016 ◽  
Author(s):  
Helen Farman ◽  
Sara Windahl ◽  
Deborah Clegg ◽  
Shang Kui Xie ◽  
Lars Westberg ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Bone Mass ◽  
Cortical Bone ◽  
Estrogen Receptor Alpha ◽  
Receptor Alpha ◽  
Cortical Bone Mass
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