Exon deletions and variants of human estrogen receptor mRNA in endometrial hyperplasia and adenocarcinoma

2000 ◽  
Vol 10 (2) ◽  
pp. 128-136 ◽  
Author(s):  
G. Horvath ◽  
G. Leser ◽  
M. Hahlin ◽  
M. Henriksson
2002 ◽  
Vol 80 (3) ◽  
pp. 335-341 ◽  
Author(s):  
Laura L Hart ◽  
James R Davie

The human estrogen receptor is a steroid nuclear receptor found in breast cancer and a variety of other tissues. Located in the nucleus, it can exist either loosely or tightly associated with the nuclear matrix depending on whether or not it is bound to ligand. When bound to ligand, it is responsible for the transcriptional regulation of estrogen-responsive genes through recruitment of coactivators and corepressors of transcription. The estrogen receptor is also capable of ligand-independent transcriptional activation via the mitogen-activated protein kinase pathway. Ligands have been implicated in the regulation of estrogen receptor levels via changing the levels and stability of estrogen receptor mRNA and protein. The resulting levels of estrogen receptor and the type of ligand bound to it have a direct impact on the transcription of estrogen-responsive genes.Key words: estrogen receptor, transcription factor, mitogen-activated protein kinase, MAPK, estrogen-responsive genes.


1990 ◽  
Vol 10 (12) ◽  
pp. 6674-6682
Author(s):  
E A McKenzie ◽  
N A Cridland ◽  
J Knowland

We generate pure estrogen receptor protein in Xenopus oocytes by injecting them with estrogen receptor mRNA synthesized in vitro. A chromosomal vitellogenin gene, which normally responds to estrogen only in liver cells, is activated. Primer extension shows that initiation is accurate, and ribonuclease mapping shows that the first exon is correctly spliced out of the initial transcript. Long transcripts are produced, one being equal in length to poly(A)- vitellogenin mRNA. Immunochemical estimates of receptor levels in the oocyte nuclei suggest that pure receptor, acting alone, cannot activate oocyte vitellogenin genes unless unusually large amounts are present. However, when a receptor-free extract from liver cells is also injected, the amount of receptor required is reduced. Such an extract, but not pure receptor, can also activate albumin genes in oocytes.


1990 ◽  
Vol 10 (12) ◽  
pp. 6674-6682 ◽  
Author(s):  
E A McKenzie ◽  
N A Cridland ◽  
J Knowland

We generate pure estrogen receptor protein in Xenopus oocytes by injecting them with estrogen receptor mRNA synthesized in vitro. A chromosomal vitellogenin gene, which normally responds to estrogen only in liver cells, is activated. Primer extension shows that initiation is accurate, and ribonuclease mapping shows that the first exon is correctly spliced out of the initial transcript. Long transcripts are produced, one being equal in length to poly(A)- vitellogenin mRNA. Immunochemical estimates of receptor levels in the oocyte nuclei suggest that pure receptor, acting alone, cannot activate oocyte vitellogenin genes unless unusually large amounts are present. However, when a receptor-free extract from liver cells is also injected, the amount of receptor required is reduced. Such an extract, but not pure receptor, can also activate albumin genes in oocytes.


2012 ◽  
Vol 178 (3) ◽  
pp. 556-561 ◽  
Author(s):  
James J. Nagler ◽  
Timothy D. Cavileer ◽  
Joseph S. Verducci ◽  
Irvin R. Schultz ◽  
Sharon E. Hook ◽  
...  

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