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shown that oestradiol (E 2 ) and related SERMs differentially regulate target gene expression via ERα or ERβ ( Kian et al. 2004 , Stossi et al. 2004 , Monroe et al. 2005 ). Recently, it has been demonstrated, in various human cell types
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endothelial cell migration and re-endothelialisation ( Umetani et al . 2007 ). In contrast, in the absence of E2, 27HC is reported to act as an agonist to ERα (ESR1) to increase cell adhesion and expression of pro-inflammatory cytokines such as tumour
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-enriched and triple negative BC (TNBC). Luminal A and B subtypes, representing around 40 and 20% of BC, respectively, express ERα. The HER2-enriched subtype behaves more aggressively than luminal subtypes but is sensitive to therapies targeting the HER2
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Department of Nutritional Sciences, Department of Molecular Carcinogenesis, Dell Pediatric Research Institute, University of Texas, 1400 Barbara Jordan Boulevard, DPRI 2.834, Austin, Texas 78722, USA
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Introduction The prevalence of obesity, an established risk and progression factor for estrogen receptor α (ERα)-positive luminal A breast cancer, has dramatically increased in the USA and many other parts of the world over the past 25 years
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are recognized as co-mediators of tumor progression rather than as merely bystanders. Estrogen is well recognized as a mitogen for breast cancer cells. Traditionally, estrogenic effects have been ascribed to the nuclear estrogen receptors (ERα and ERβ
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(ERα) and amplifies the receptor's transactivation ( Han et al . 2007 ). The LRP16 gene was originally isolated from human lymphocyte cells and predominantly localizes in the nucleus ( Han et al . 2001 , 2002 ). Although the expression pattern of
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Introduction Approximately 70% of breast cancers express estrogen receptor α (ERα) and require endocrine therapies, such as the ER antagonist, tamoxifen (TAM) ( EBCTCG. 2005 ). However, ER-positive breast cancer frequently acquires resistance
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are mediated by two subtypes of ER, ERα and ERβ. Both receptors belong to a family of ligand-activated nuclear transcription factors ( Evans 1988 ) and share a high degree of homology in their DNA binding domains ( Kuiper et al. 1996 ). However, they
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classical (ERα and ERβ) and nonclassical (G protein-coupled receptor 30, GPR30) receptors ( Manavathi & Kumar 2006 ), there is only one receptor (PRLR) for PRL, albeit it exists in several isoforms which couple to different signaling pathways ( Swaminathan
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Signaling, Danvers, MA, USA). Ovaries were also collected and homogenized; ovarian lysate served as a positive control for both ERα and ERβ. After centrifugation, the solubilized proteins were separated by 12% SDS-PAGE and blotted onto nitrocellulose