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De plus, ERα36 régule l’effet antiprolifératif de la progestéroneĮstrogens are implicated in a diverse range of functions varying from reproduction, circulation, skeletal health to neuroprotection. En effet, nous avons montré d’une part que ERα36 interagit avec PR dans le noyau de cellules cancéreuses et d’autre part que ERα36 agit comme un corégulateur de l’expression de gènes cibles de PR. Pour la première fois, nous avons identifié un lien fonctionnel entre ERα36 et PR. De manière intéressante, le mauvais pronostic d’ERα36 était retrouvé uniquement dans la sous-catégorie PR-positive et non dans la sous-catégorie PR-négative, suggérant que ERα36 pourrait interférer avec la signalisation de PR. Nous avons étudié son expression ainsi que sa valeur pronostique dans des sous-catégories tumorales mammaires (PR-positives et PR-négatives). ERα36 est une protéine de 36 kDa exprimée indépendamment d’ERα, et qui possède un fort potentiel prolifératif et métastatique dans le cancer du sein. Il y a quelques années, une isoforme d’ERα : ERα36 a été identifiée.
#Get serum serial number splice plus#
A ce jour, plus de 75% des tumeurs mammaires nouvellement diagnostiquées expriment ERα. Ces deux hormones vont se lier à leurs récepteurs respectifs : ERα et PR, qui sont des biomarqueurs clés de la progression tumorale. Le cancer du sein est le cancer le plus diagnostiqué chez la femme et sa progression se fait le plus souvent via les hormones stéroïdes ovariennes : les œstrogènes et la progestérone. Finally, we will explain how studying the regulation of ERα36 expression could provide new clues to counteract resistance to cancer treatments in hormone-sensitive tumors. We will then report recent data on the impact of ERα36 expression and/or activity in normal breast and testicular cells, but also in different types of tumors including mammary tumors, highlighting why ERα36 can now be considered as a marker of malignancy. In this review, we will first specify the place that ERα36 currently occupies within the diversity of nuclear and membrane estrogen receptors. The estrogen receptor variant, ERα36, was cloned in 2005 and is mainly described in the literature to be involved in the progression of mammary tumors and in the acquired resistance to anti-estrogen drugs, such as tamoxifen. However, numerous isoforms have been identified, stimulating unconventional estrogen response pathways leading to complex cellular and tissue responses. The results of the present study indicated that ER-α30 might represent a potential biomarker for breast cancer.Įstrogen nuclear receptors, represented by the canonical forms ERα66 and ERβ1, are the main mediators of the estrogen-dependent pathophysiology in mammals. The 30 kDa protein was expressed in stably transfected MDA-MB-231 cells, and the overexpression of ER-α30 in MDA-MB-231 cells enhanced malignant biological behaviors, including cellular proliferation, migration and invasion in vitro. The expression of ER-α30 was associated with ER-α66-negative and progesterone receptor-negative breast cancer. The ER-α30 sequence lacked a ligand-binding domain and a ligand-dependent transcriptional activation domain but retained the N-terminal transcriptional activation domain, the DNA-binding domain and a partial hinge domain, and possesses a unique 10-amino-acid domain.
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In the present study, a novel hER-α splice variant, ER-α30, was identified and cloned from clinical breast cancer tissue.
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Since the early 1990s, multiple human estrogen receptor-α (hER-α) splice variants have been identified, of which the majority contain ≥1 deleted exon, and some are expressed as proteins with modified functions from the wild-type 66 kDa hER-α (ER-α66).