Cloning and In Vitro Expression and Characterization of the Androgen Receptor and Isolation of Estrogen Receptor α from the Fathead Minnow (Pimephales promelas)

2004 ◽  
Vol 38 (23) ◽  
pp. 6314-6321 ◽  
Author(s):  
Vickie S. Wilson ◽  
Mary C. Cardon ◽  
Joseph Thornton ◽  
Joseph J. Korte ◽  
Gerald T. Ankley ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Androgen Receptor ◽  
Fathead Minnow ◽  
Pimephales Promelas ◽  
Estrogen Receptor Α ◽  
In Vitro Expression

scholarly journals Sex Hormone Receptor Signaling in Bladder Cancer: A Potential Target for Enhancing the Efficacy of Conventional Non-Surgical Therapy

Cells ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 1169
Author(s):  
Hiroki Ide ◽  
Hiroshi Miyamoto
Keyword(s):  
Bladder Cancer ◽  
Estrogen Receptor ◽  
Androgen Receptor ◽  
Surgical Therapy ◽  
Urothelial Cancer ◽  
Hormone Receptors ◽  
Estrogen Receptor Α ◽  
Vital Role ◽  
Sex Hormone ◽  
Sex Steroid Hormone

There have been critical problems in the non-surgical treatment for bladder cancer, especially residence to intravesical pharmacotherapy, including BCG immunotherapy, cisplatin-based chemotherapy, and radiotherapy. Recent preclinical and clinical evidence has suggested a vital role of sex steroid hormone-mediated signaling in the progression of urothelial cancer. Moreover, activation of the androgen receptor and estrogen receptor pathways has been implicated in modulating sensitivity to conventional non-surgical therapy for bladder cancer. This may indicate the possibility of anti-androgenic and anti-estrogenic drugs, apart from their direct anti-tumor activity, to function as sensitizers of such conventional treatment. This article summarizes available data suggesting the involvement of sex hormone receptors, such as androgen receptor, estrogen receptor-α, and estrogen receptor-β, in the progression of urothelial cancer, focusing on their modulation for the efficacy of conventional therapy, and discusses their potential of overcoming therapeutic resistance.

scholarly journals Functional characterization of somatic point mutations of the human estrogen receptor α (hERα) in adenomyosis uteri

2004 ◽  
Vol 10 (12) ◽  
pp. 853-860 ◽  
Author(s):  
Martin K. Oehler ◽  
Holger Greschik ◽  
Dagmar-C. Fischer ◽  
Xiaowen Tong ◽  
Roland Schuele ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Functional Characterization ◽  
Point Mutations ◽  
Estrogen Receptor Α ◽  
Human Estrogen Receptor

Environmental Gestagens Activate Fathead Minnow (Pimephales promelas) Nuclear Progesterone and Androgen Receptors in Vitro

2014 ◽  
Vol 48 (14) ◽  
pp. 8179-8187 ◽  
Author(s):  
Laura E. Ellestad ◽  
Mary Cardon ◽  
Ian G. Chambers ◽  
Jennifer L. Farmer ◽  
Phillip Hartig ◽  
...  
Keyword(s):  
Fathead Minnow ◽  
Androgen Receptors ◽  
Pimephales Promelas

scholarly journals The Phosphorylated Estrogen Receptor α (ER) Cistrome Identifies a Subset of Active Enhancers Enriched for Direct ER-DNA Binding and the Transcription Factor GRHL2

2018 ◽  
Vol 39 (3) ◽  
Author(s):  
Kyle T. Helzer ◽  
Mary Szatkowski Ozers ◽  
Mark B. Meyer ◽  
Nancy A. Benkusky ◽  
Natalia Solodin ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Transcription Factor ◽  
Dna Binding ◽  
Protein Interactions ◽  
Posttranslational Modifications ◽  
Binding Sites ◽  
Protein Function ◽  
Estrogen Receptor Α ◽  
Binding Activity

ABSTRACT Posttranslational modifications are key regulators of protein function, providing cues that can alter protein interactions and cellular location. Phosphorylation of estrogen receptor α (ER) at serine 118 (pS118-ER) occurs in response to multiple stimuli and is involved in modulating ER-dependent gene transcription. While the cistrome of ER is well established, surprisingly little is understood about how phosphorylation impacts ER-DNA binding activity. To define the pS118-ER cistrome, chromatin immunoprecipitation sequencing was performed on pS118-ER and ER in MCF-7 cells treated with estrogen. pS118-ER occupied a subset of ER binding sites which were associated with an active enhancer mark, acetylated H3K27. Unlike ER, pS118-ER sites were enriched in GRHL2 DNA binding motifs, and estrogen treatment increased GRHL2 recruitment to sites occupied by pS118-ER. Additionally, pS118-ER occupancy sites showed greater enrichment of full-length estrogen response elements relative to ER sites. In an in vitro DNA binding array of genomic binding sites, pS118-ER was more commonly associated with direct DNA binding events than indirect binding events. These results indicate that phosphorylation of ER at serine 118 promotes direct DNA binding at active enhancers and is a distinguishing mark for associated transcription factor complexes on chromatin.

Characterization of rodent constitutively active estrogen receptor α variants and their constitutive transactivation mechanisms

2017 ◽  
Vol 248 ◽  
pp. 16-26 ◽  
Author(s):  
Hirotaka Ishii ◽  
Yujiro Hattori ◽  
Arisa Munetomo ◽  
Hiroshi Watanabe ◽  
Yasuo Sakuma ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptor Α ◽  
Constitutively Active

In vivo characterization of estrogen receptor modulators with reduced genomic versus nongenomic activity in vitro

2008 ◽  
Vol 111 (1-2) ◽  
pp. 95-100 ◽  
Author(s):  
Christiane Otto ◽  
Iris Fuchs ◽  
Helga Altmann ◽  
Mario Klewer ◽  
Gilda Schwarz ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptor Modulators ◽  
In Vivo Characterization ◽  
Receptor Modulators
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