scholarly journals Human Estrogen Receptor β 548 Is Not a Common Variant in Three Distinct Populations

Endocrinology ◽  
2003 ◽  
Vol 144 (8) ◽  
pp. 3541-3546 ◽  
Author(s):  
Li Xu ◽  
Qiang Pan-Hammarström ◽  
Asta Försti ◽  
Kari Hemminki ◽  
Lennart Hammarström ◽  
...  
Keyword(s):  
Amino Acids ◽  
Estrogen Receptor ◽  
Base Pair ◽  
Estrogen Receptor Β ◽  
Common Variant ◽  
Human Populations ◽  
Functional Characteristics ◽  
Human Estrogen Receptor

Abstract Several isoforms of estrogen receptor (ER) β (also known as NR3A2) have been reported, including variants with different N-terminal ends. In rodents, two in-frame initiation codons (ATGs) are used to produce proteins of 530 and 549 amino acids, respectively. In humans, the upstream ATG is out of frame in all clones reported, until recently, when human clones with an extra A-T base pair placing the upstream ATG in frame were reported. The authors suggested that this could represent a novel polymorphism in the ERβ gene. Because human ERβ548 (hERβ548) and hERβ530 display different functional characteristics in vitro, it is of interest to determine if this variant constitutes a polymorphism in human populations. We therefore determined the frequency of this novel isoform in several populations including African (n = 96), Caucasian (n = 100), and Asian (n = 128) subjects using denaturing HPLC. We did not detect any alleles that correspond to hERβ548 in these samples or in additional samples of heterogeneous origin. It is concluded that hERβ548 is not a common variant in Africans, Caucasians, or Asians.

In vivo and in vitro phosphorylation of the human estrogen receptor

1995 ◽  
Vol 52 (2) ◽  
pp. 159-171 ◽  
Author(s):  
Steven F. Arnold ◽  
John D. Obourn ◽  
Matthew R. Yudt ◽  
Timothy H. Carter ◽  
Angelo C. Notides
Keyword(s):  
Estrogen Receptor ◽  
Human Estrogen Receptor

scholarly journals Agonists and knockdown of estrogen receptor β differentially affect invasion of triple-negative breast cancer cells in vitro

BMC Cancer ◽  
2016 ◽  
Vol 16 (1) ◽  
Author(s):  
Susanne Schüler-Toprak ◽  
Julia Häring ◽  
Elisabeth C. Inwald ◽  
Christoph Moehle ◽  
Olaf Ortmann ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Estrogen Receptor ◽  
Cancer Cells ◽  
Triple Negative Breast Cancer ◽  
Breast Cancer Cells ◽  
Triple Negative ◽  
Estrogen Receptor Β

scholarly journals The Effects of Mono-(2-Ethylhexyl) Phthalate (MEHP) on Human Estrogen Receptor (hER) and Androgen Receptor (hAR) by YES/YAS In Vitro Assay

Molecules ◽  
2019 ◽  
Vol 24 (8) ◽  
pp. 1558 ◽  
Author(s):  
Kim ◽  
Park ◽  
Kim ◽  
Kim
Keyword(s):  
Estrogen Receptor ◽  
Androgen Receptor ◽  
Endocrine System ◽  
Yeast Cells ◽  
Signal Recovery ◽  
Vitro Assay ◽  
Recovery Test ◽  
Human Estrogen Receptor ◽  
Ethylhexyl Phthalate

Endocrine active compounds with structural similarities to natural hormones such as 17β-estradiol (E2) and androgen are suspected to affect the human endocrine system by inducing hormone-dependent effects. This study aimed to detect the (anti-)estrogenic and (anti-)androgenic activities of mono-(2-ethylhexyl) phthalate (MEHP) by yeast estrogen/androgen bioassay (YES/YAS). In addition, the mechanism and uptake of MEHP to receptors during agonistic and antagonistic activities were investigated through the activation signal recovery test and chromatographic analysis using liquid chromatography and tandem mass spectrometry (LC-MS/MS). Estrogenic and androgenic activities of MEHP were not observed. However, MEHP exhibited anti-estrogenic (IC50 = 125 μM) and anti-androgenic effects (IC50 = 736 μM). It was confirmed that these inhibitory effects of MEHP were caused by receptor-mediated activity of the estrogen receptor and non-receptor-mediated activity of the androgen receptor in an activation signal recovery test. When IC50 concentrations of anti-estrogenic and androgenic activity of MEHP were exposed to yeast cells, the uptake concentration observed was 0.0562 ± 0.0252 μM and 0.143 ± 0.0486 μM by LC-MS/MS analysis.

scholarly journals Identification of Amino Acids in the Hormone Binding Domain of the Human Estrogen Receptor Important in Estrogen Binding

1996 ◽  
Vol 271 (33) ◽  
pp. 20053-20059 ◽  
Author(s):  
Kirk Ekena ◽  
Karen E. Weis ◽  
John A. Katzenellenbogen ◽  
Benita S. Katzenellenbogen
Keyword(s):  
Amino Acids ◽  
Estrogen Receptor ◽  
Binding Domain ◽  
Hormone Binding ◽  
Human Estrogen Receptor ◽  
Estrogen Binding ◽  
Hormone Binding Domain

scholarly journals Prenatal LHRH Neurons in Nasal Explant Cultures Express Estrogen Receptor β Transcript

Endocrinology ◽  
2002 ◽  
Vol 143 (7) ◽  
pp. 2503-2507 ◽  
Author(s):  
Neda Sharifi ◽  
Andree E. Reuss ◽  
Susan Wray
Keyword(s):  
Central Nervous System ◽  
Estrogen Receptor ◽  
Sex Steroids ◽  
Estrogen Receptor Β ◽  
Reproductive State ◽  
Specific Primers ◽  
Explant Cultures ◽  
The Central Nervous System ◽  
Express Estrogen Receptor

Abstract Sex steroids influence LHRH neuronal activity, exerting a negative or positive feedback action, depending on the reproductive state of the animal. Recent evidence indicates that LHRH neurons possess the estrogen receptor β (ERβ) subtype postnatally, suggesting that estrogen may act, in part, directly on LHRH neurons. In this study, we identified ERβ transcript in prenatal LHRH neurons as a function of age. Single-cell cDNA pools were made from LHRH neurons maintained for 7, 14, and 28 d in vitro (div). Screening of the cDNA pools by PCR with ERβ-specific primers revealed ERβ-positive LHRH neurons at all three ages. However, the number of LHRH cells coexpressing ERβ transcript decreased dramatically between 14 (6/10) and 28 div (1/10). None of the LHRH cells were positive for ERα transcript. These results indicate that developing LHRH neurons express the transcript for ERβ and suggest that continued expression of ERβ is either a characteristic of LHRH neurons that may require cues from the central nervous system and/or periphery or predetermined to be maintained in a subpopulation of LHRH neurons.

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