Comparison of sex steroid receptor determinations in human breast cancer by enzyme immunoassay and radioligand binding

1990 ◽  
Vol 4 (6) ◽  
pp. 430-436 ◽  
Author(s):  
Resad Pasic ◽  
Benjamin Djulbegovic ◽  
James L. Wittliff
Keyword(s):  
Breast Cancer ◽  
Enzyme Immunoassay ◽  
Human Breast Cancer ◽  
Radioligand Binding ◽  
Steroid Receptor ◽  
Sex Steroid ◽  
Human Breast

Determination of Estrogen Receptors in Human Breast Cancer: Comparison between Enzyme Immunoassay and Dextran-Coated Charcoal Method

1986 ◽  
Vol 72 (5) ◽  
pp. 511-514 ◽  
Author(s):  
Cecilia Bozzetti ◽  
Nadia Naldi ◽  
Annamaria Guazzi ◽  
Rita Nizzoli ◽  
Magda Benecchi ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Estrogen Receptor ◽  
Estrogen Receptors ◽  
Enzyme Immunoassay ◽  
Strong Correlation ◽  
Human Breast Cancer ◽  
Human Breast ◽  
Dextran Coated Charcoal ◽  
The Mean

Estrogen receptor determination was performed on 120 breast cancer cytosols, using the dextran-coated charcoal method (DCC) and an enzyme immunoassay (EIA) to compare the efficiency of the two techniques. A strong correlation was noted between ER concentrations determined by DCC and EIA (P < 0.001). The mean ER-EIA value was significantly higher than the mean ER-DCC value in premenopausal (P < 0.001) as well in postmenopausal (P < 0.001) patients.

scholarly journals Tamoxifen-induced ER-α–SRC-3 interaction in HER2 positive human breast cancer; a possible mechanism for ER isoform specific recurrence

2006 ◽  
Vol 13 (4) ◽  
pp. 1135-1145 ◽  
Author(s):  
Marie Mc Ilroy ◽  
Fergal J Fleming ◽  
Yvonne Buggy ◽  
Arnold D K Hill ◽  
Leonie S Young
Keyword(s):  
Breast Cancer ◽  
Growth Factor ◽  
Cell Cultures ◽  
Human Breast Cancer ◽  
Molecular Model ◽  
Steroid Receptor ◽  
Model Systems ◽  
Endocrine Treatment ◽  
Human Breast ◽  
Her2 Positive

Differential signalling between the two oestrogen receptor (ER) isoforms in the presence of tamoxifen has been described. We hypothesise that differential recruitment of the steroid receptor co-activator, SRC-3 to ER-α and ER-β may in part explain associations between ER isoforms and response to endocrine treatment. SRC-3 was localised within epithelial cells of breast tumour tissue and was co-localised with ER-α and ER-β, (n = 112). Expression of SRC-3 was found to be positively associated with ER-α (P = 0.0021) and inversely with ER-β (P < 0.0001). Uniquely, this study utilises primary cell cultures derived from patient tumours, thus providing samples not readily available in most molecular model systems. These samples have enabled us to investigate the influence of growth factor pathways on steroid receptor-co-activator interactions. In HER2 (human epidermal growth factor receptor 2) positive primary tumour cell cultures 17β-estradiol induced a decrease in SRC-3, whereas upregulated SRC-3 expression. Furthermore, treatment with tamoxifen-induced SRC-3 recruitment to the ER-oestrogen response element and enhanced interaction between SRC-3 and ER-α, but not ER-β. Knockdown of SRC-3 results in a concomitant loss of expression of the oestrogen target gene pS2. Furthermore, silencing of SRC-3 resensitizes endocrine resistant, HER2 positive cells to the anti-proliferative effects of tamoxifen. The ability of ER-α, but not ER-β to recruit SRC-3 in the presence of tamoxifen may in part explain the differential ER isoform associations with recurrence in human breast cancer.

Quality Assurance for Steroid Receptor Assay in Human Breast Cancer: Six Years Experience of the Italian Committee

1985 ◽  
Vol 71 (6) ◽  
pp. 589-595 ◽  
Author(s):  
Adriano Piffanelli ◽  
Dario Pelizzola ◽  
Michele De Bortoli ◽  
Fulvio Agrimonti ◽  
Roberto Fraina ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Quality Assurance ◽  
Human Breast Cancer ◽  
Steroid Receptor ◽  
Human Breast ◽  
Receptor Assay
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