Estradiol-induced Down-regulation of estrogen receptor. Effect of various modulators of protein synthesis and expression

Borrás, M.; Hardy, Linda; Lempereur, F.; Khissiin, A.H. El; Legros, Nicole; Gol-Winkler, Rose; Leclercq, Guy

doi:10.1016/0960-0760(94)90072-8

Cited by 116 publications

(71 citation statements)

References 51 publications

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“…It has been suggested that the loss of hormone-binding capacity may be due to receptor inactivation by dephosphorylation [26]. Inhibition of receptor synthesis was shown in rat uteri and MCF-7 cells, where E2 induced suppression of ER mRNA a few hours after treatment [1,39]. Furthermore, the apparent decrease in the total number of measurable binding sites after a hormone challenge in rat uteri is due to degradation of the protein [20,39].…”

Section: Introductionmentioning

confidence: 99%

A biphasic action of estradiol on estrogen and progesterone receptor expression in the lamb uterus

et al. 2000

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-Regulation of the uterine expression of estrogen and progesterone receptors was studied in 20 three-month-old lambs that were not treated or treated with estradiol-17β. Determinations of receptors were performed by binding assays in the nuclear and cytosolic fractions, receptor mRNAs by solution hybridization, and estrogen receptor protein by an enzyme-immunoassay. Estradiol treatment decreased the receptor binding capacity of both receptors and the levels of immunoreactive estrogen receptor 12 h after injection in the absence of decreased receptor mRNAs, suggesting that the initial decrease is due to degradation of the proteins or that mRNAs are translated into new receptor proteins at a reduced rate. The mRNA levels increased after estradiol treatment suggesting that the replenishment phase consists of synthesis of new receptors rather than recycling of inactivated receptors.estrogen / progesterone / receptor / uterus / lamb Résumé -Action biphasique de l'oestradiol sur l'expression des récepteurs aux oestrogènes et à la progestérone dans l'utérus de l'agnelle. La régulation de l'expression des récepteurs aux oestrogènes et à la progestérone au niveau de l'utérus a été étudiée chez des agnelles immatures âgées de 3 mois (n = 20), traitées et non traitées avec oestradiol-17β. Les déterminations des récepteurs ont été faites par des essais de liaison dans les fractions nucléaires et cytosoliques, les ARNm des récepteurs par la méthode d'hybridation en solution et la protéine du récepteur aux oestrogènes par un essai immuno-enzymatique. Le traitement à l'oestradiol réduit la capacité de liaison des deux récepteurs et les niveaux des récepteurs aux oestrogènes immunoréactifs 12 h après l'injection en absence d'une diminution des ARNm des récepteurs, suggèrent que la réduction initiale est due à la dégradation des Reprod. Nutr. Dev. 40 (2000) 283-293 283

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Section: Introductionmentioning

confidence: 99%

A biphasic action of estradiol on estrogen and progesterone receptor expression in the lamb uterus

et al. 2000

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“…Estrogen may stabilize endometrial ER mRNAs by inducing proteins to bind to specific sequences in the 3'-UTR. However, studies show that treatment with estrogen induces down-regulation of ERα mRNA that appears to be caused by its reduced stability (Borras et al, 1994;Saceda et al, 1998). Relatively little is known about the ability of estrogen to regulate the expression of ERs in pigeon oviduct epithelial cells (POECs).…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning, expression, and regulation of estrogen receptors in pigeon oviduct epithelial cells

Zhang¹,

Chen²,

Li³

et al. 2014

Genet. Mol. Res.

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ABSTRACT. Estrogen regulates reproductive behavior and drives the proliferation and differentiation of several cell types. These physiological functions of estrogen are mediated by estrogen receptors (ERs), and each ER isoform plays a distinct role. To clarify the molecular mechanism of estrogen action and to evaluate the effect of ERs on the secretion of ovalbumin (OVA) in pigeon oviduct epithelial cells (POECs), we determined the complete coding sequences encoding ER alpha (ERα) and ER beta (ERβ) in pigeons. The abundance of pigeon ERα and ERβ mRNA was detected using quantitative polymerase chain reaction. These results revealed that pigeon ERα is highly expressed in the oviduct, while pigeon ERb is highly expressed in the ovary and kidney. We hypothesize that ERα mRNA predominates over that of ERβ in the oviduct. The expression of ERα can be down- 1927©FUNPEC-RP www.funpecrp.com.br Genetics and Molecular Research 13 (1): 1926-1937 (2014 Characterization and regulation of pigeon ERs regulated by 17β-estradiol, and the knockdown of ERα promoted OVA mRNA expression in cultured POECs, indicating that ERα may play an important role in OVA secretion.

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“…Estradiol-induced down-regulation of ERa protein was inhibited by 100 nM okadaic acid, suggesting that a dephosphorylation event via either PP2A or PP1A was required (Borras et al 1994). On the other hand, experimental reduction of PP2A activity, through either expression of siRNA specific to the catalytic subunit of PP2A or by the addition of okadaic acid, decreased the stability of ERa mRNA and reduced receptor protein levels (Keen et al 2005).…”

Section: Discussionmentioning

confidence: 98%

“…PP2A plays a role in the regulation of multiple cellular signaling pathways, including regulation of steroid receptor activity (Sola et al 1991, Borras et al 1994, Galigniana et al 1999, Bhattacharjee et al 2001, and aberrant expression of the enzyme may be involved in cancer etiology (Csortos et al 1996, Smith 1998, Schonthal 2001, Sontag 2001. PP2A and another protein phosphate PP5, have been previously implicated in regulation of ER action.…”

Section: Discussionmentioning

confidence: 99%

Striatin-3γ inhibits estrogen receptor activity by recruiting a protein phosphatase

Tan¹,

Long

Nakshatri

et al. 2008

Journal of Molecular Endocrinology

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A splicing variant of rat striatin-3 (rSTRN3g) was found to associate with estrogen receptor-a (ERa) in a ligand-dependent manner. In two-hybrid and pull-down analyses, estradiol induced an interaction between rSTRN3g and ERa. STRN3g protein was found in nuclear extracts from rat uterus and human cell lines. Overexpression of rSTRN3g induced a decrease in ERa transcriptional activity but had no effect on ERb activity. Immunoprecipitation analyses showed that rSTRN3g interacts with both the ERa and the catalytic subunit of protein phosphatase 2A (PP2A(C)). The transrepressor action of rSTRN3g was overcome by okadaic acid, an inhibitor of PP2A(C), and by cotransfection of PP2A(C) siRNA. rSTRN3g caused dephosphorylation of ERa at serine 118 and this was abrogated by okadaic acid. ERa lacking phosphorylation sites at either serine 118 or 167 was insensitive to the corepressor action of rSTRN3g. These observations suggest that an rSTRN3g-PP2A(C) complex is recruited to agonist-activated ERa, thereby leading to its dephosphorylation and inhibiting transcription.

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Estradiol-induced Down-regulation of estrogen receptor. Effect of various modulators of protein synthesis and expression

Cited by 116 publications

References 51 publications

A biphasic action of estradiol on estrogen and progesterone receptor expression in the lamb uterus

A biphasic action of estradiol on estrogen and progesterone receptor expression in the lamb uterus

Molecular cloning, expression, and regulation of estrogen receptors in pigeon oviduct epithelial cells

Striatin-3γ inhibits estrogen receptor activity by recruiting a protein phosphatase

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