Mutations of Tyrosine 537 in the Human Estrogen Receptor-α Selectively Alter the Receptor's Affinity for Estradiol and the Kinetics of the Interaction†

Biochemistry ◽  
2002 ◽  
Vol 41 (13) ◽  
pp. 4209-4217 ◽  
Author(s):  
L. Zhong ◽  
D. F. Skafar
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptor Α ◽  
Human Estrogen Receptor ◽  
Tyrosine 537 ◽  
Kinetics Of

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

Biophysical studies of the interaction between calmodulin and the R287-T311 region of human estrogen receptor α reveals an atypical binding process

2012 ◽  
Vol 419 (2) ◽  
pp. 356-361 ◽  
Author(s):  
Ludovic Carlier ◽  
Cillian Byrne ◽  
Emeric Miclet ◽  
Sandrine Bourgoin-Voillard ◽  
Magali Nicaise ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptor Α ◽  
Binding Process ◽  
Biophysical Studies ◽  
Human Estrogen Receptor

Human estrogen receptor α gene is a target of Runx2 transcription factor in osteoblasts

2007 ◽  
Vol 313 (8) ◽  
pp. 1548-1560 ◽  
Author(s):  
Elisabetta Lambertini ◽  
Letizia Penolazzi ◽  
Elisa Tavanti ◽  
Gian Pietro Schincaglia ◽  
Margherita Zennaro ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Transcription Factor ◽  
Estrogen Receptor Α ◽  
Human Estrogen Receptor ◽  
Estrogen Receptor Α Gene

scholarly journals The Human Estrogen Receptor-α Isoform hERα46 Antagonizes the Proliferative Influence of hERα66 in MCF7 Breast Cancer Cells

Endocrinology ◽  
2005 ◽  
Vol 146 (12) ◽  
pp. 5474-5484 ◽  
Author(s):  
Graziella Penot ◽  
Christine Le Péron ◽  
Yohann Mérot ◽  
Eva Grimaud-Fanouillère ◽  
François Ferrière ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cell Cycle ◽  
Estrogen Receptor ◽  
Cell Growth ◽  
Activation Function ◽  
Estrogen Receptor Α ◽  
Breast Cancer Cell Lines ◽  
Mcf7 Cells ◽  
Exact Function ◽  
Human Estrogen Receptor

The expression of two human estrogen receptor-α (hERα) isoforms has been characterized within estrogen receptor-α-positive breast cancer cell lines such as MCF7: the full-length hERα66 and the N terminally deleted hERα46, which is devoid of activation function (AF)-1. Although hERα66 is known to mediate the mitogenic effects that estrogens have on MCF7 cells, the exact function of hERα46 in these cells remains undefined. Here we show that, during MCF7 cell growth, hERα46 is mainly expressed in the nucleus at relatively low levels, whereas hERα66 accumulates in the nucleus. When cells reach confluence, the situation reverses, with hERα46 accumulating within the nucleus. Although hERα46 expression remains rather stable during an estrogen-induced cell cycle, its overexpression in proliferating MCF7 cells provokes a cell-cycle arrest in G0/G1 phases. To gain further details on the influence of hERα46 on cell growth, we used PC12 estrogen receptor-α-negative cell line, in which stable transfection of hERα66 but not hERα46 allows estrogens to behave as mitogens. We next demonstrate that, in MCF7 cells, overexpression of hERα46 inhibits the hERα66-mediated estrogenic induction of all AF-1-sensitive reporters: c-fos and cyclin D1 as well as estrogen-responsive element-driven reporters. Our data indicate that this inhibition occurs likely through functional competitions between both isoforms. In summary, hERα46 antagonizes the proliferative action of hERα66 in MCF7 cells in part by inhibiting hERα66 AF-1 activity.

Sign in / Sign up

Export Citation Format

Share Document