Estrogen-Receptor Interaction

Jensen, Elwood V.; DeSombre, Eugene R.

doi:10.1126/science.182.4108.126

Cited by 699 publications

(101 citation statements)

References 77 publications

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“…For a number of years it has been accepted that the ER is located in the cytosol and translocates to the nucleus after estrogen binding and activation (35). The monoclonal antibody against ER used in this study has already been shown to bind to the cytoplasmic as well as to the nuclear form of ER (22).…”

Section: Methodsmentioning

confidence: 96%

Immunocytochemical staining of estrogen receptor in paraffin sections of human breast cancer by use of monoclonal antibody: comparison with that in frozen sections.

Shimada¹,

Kimura²,

Abe³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

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Estrogen receptor (ER) in human breast cancer tissues was demonstrated in paraffin sections as well as in frozen sections by immunoperoxidase methods using monoclonal antibody (H222) against ER. The avidin-biotin-peroxidase complex method was used for the paraffin sections fixed in cold buffered formalin, and the peroxidase-antiperoxidase method was used for the fixed frozen sections. The results were compared with the ER content in the respective tumor tissue determined by dextran-coated charcoal assay. The specific staining for ER was located exclusively in the nuclei of cancer cells in both paraffin and frozen sections. Differences in the intensity and distribution of nuclear staining within a section were often observed, suggesting heterogeneity of the ER content of individual breast cancer cells. In 24 breast cancer tissues studied simultaneously by both paraffin and frozen section methods, 21 (88%) showed similar evaluation of the presence of ER. (6).In order to circumvent these disadvantages of the current ER assay, many immunocytochemical methods using antiestradiol antibody (7-11) and cytochemical methods using fluorescein-or peroxidase-labeled estradiol (12-15) have been proposed. However, sucrose gradient analysis revealed that the antibodies against estradiol do not necessarily detect the estradiol-ER complex (16). In addition, affinity of the estradiol-conjugate for ER was shown to be extremely low when compared with that of free estradiol (17)(18)(19). Although these published methods were aimed at visualizing the specific binding of estrogen to ER, the methods of tissue preparation used in these studies could not prevent the loss of ER through diffusion or the reduced ability of estrogen to bind to its receptor (20). Therefore, it is reasonable to conclude that the stains obtained by these immunocytochemical and cytochemical methods are not specific for ER (16)(17)(18)(19)(20).Recently, monoclonal antibodies to human ER were developed by Greene et al. (21) and Miller et al. (22). By use of these monoclonal antibodies against ER, King and Greene first demonstrated ER in frozen tissue sections prepared from human breast cancer and other sources (23). These monoclonal antibodies are highly specific for ER and could serve as a more reliable probe for detecting ER in tissues. However, frozen sections have limitations in their use for detailed examination of tumor morphology and for retrospective studies.In this study, methods were developed to demonstrate ER in cold formalin-fixed paraffin sections as well as in frozen sections of human breast cancer tissues by use ofone of these monoclonal antibodies. The utility of immunocytochemical staining of ER was evaluated by comparing the results with the results of determining ER content by the dextran-coated charcoal (DCC) assay. MATERIALS AND METHODSBreast Cancer Tissues. One hundred and thirteen breast cancer tumors (104 primary and 9 metastatic tumor tissues) were obtained at surgery at the National Cancer Center Hospital and Keio University Hosp...

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Section: Methodsmentioning

confidence: 96%

Immunocytochemical staining of estrogen receptor in paraffin sections of human breast cancer by use of monoclonal antibody: comparison with that in frozen sections.

Shimada¹,

Kimura²,

Abe³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

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“…As a seven-transmembrane G-protein-coupled receptor, GPR30 was once believed to locate in plasma membrane. However, recent studies revealed that GPR30 existed in the endoplasmic reticulum/Golgi (12). Estrogens were the lipophilic ligands with membrane-permeable potential, making GPR30 transmit signals as a G-protein-coupled receptor.…”

Section: Gpr30 In Breast Cancers 233mentioning

confidence: 99%

The Correlation between GPR30 and Clinicopathologic Variables in Breast Carcinomas

Yang

et al. 2009

Technol Cancer Res Treat

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The G-protein-coupled-receptor 30 (GPR30) is a new membrane estrogen receptor. The aim of the present study was to determine the correlations among GPR30, ERα, PR, CerbB-2, p53, TNM stage, and pathologic grade in breast carcinomas. Two hundred forty-one biopsy specimens were evaluated with immunohistochemical assays, and then correlations were analyzed. Low negative correlations of GPR30 with ERα (r = -0.144, P<0.05) and PR (r = -0.214, P<0.01) were observed. Associations of GPR30 with C-erbB-2, p53, TNM stage, and pathologic grade were not confirmed. These findings indicated that GPR30 might be an independent prognostic factor in breast carcinomas.

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“…The steroid hormone estrogen produces a variety of cell responses, many of which can be attributed to the activation of two known estrogen receptors a and b (ERa and ERb), which function as transcription factors (Jensen & DeSombre 1973, Mosselman et al 1996. However, a number of cell responses are induced in seconds to minutes following estrogen stimulation, for example, nitric oxide generation, calcium mobilization, and activation of tyrosine kinases (Morley et al 1992, Brubaker & Gay 1999, Karpuzoglu et al 2006.…”

Section: Introductionmentioning

confidence: 99%

Distribution and characterization of estrogen receptor G protein-coupled receptor 30 in the rat central nervous system

Brǎiloiu¹,

Dun²,

Brailoiu³

et al. 2007

Journal of Endocrinology

445

331

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The G protein-coupled receptor 30 (GPR 30) has been identified as the non-genomic estrogen receptor, and G-1, the specific ligand for GPR30. With the use of a polyclonal antiserum directed against the human C-terminus of GPR30, immunohistochemical studies revealed GPR30-immunoreactivity (irGPR30) in the brain of adult male and nonpregnant female rats. A high density of irGPR30 was noted in the Islands of Calleja and striatum. In the hypothalamus, irGPR30 was detected in the paraventricular nucleus and supraoptic nucleus. The anterior and posterior pituitary contained numerous irGPR30 cells and terminal-like endings. Cells in the hippocampal formation as well as the substantia nigra were irGPR30. In the brainstem, irGPR30 cells were noted in the area postrema, nucleus of the solitary tract, and dorsal motor nucleus of the vagus; a cluster of cells were prominently labeled in the nucleus ambiguus. Tissue sections processed with pre-immune serum showed no irGPR30, affirming the specificity of the antiserum. G-1 (100 nM) caused a large increase of intracellular calcium concentrations [Ca 2C ] i in dissociated and cultured rat hypothalamic neurons, as assessed by microfluorometric Fura-2 imaging. The calcium response to a second application of G-1 showed a marked homologous desensitization. Our result shows a high expression of irGPR30 in the hypothalamic-pituitary axis, hippocampal formation, and brainstem autonomic nuclei; and the activation of GPR30 by G-1 is associated with a mobilization of calcium in dissociated and cultured rat hypothalamic neurons.

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Estrogen-Receptor Interaction

Cited by 699 publications

References 77 publications

Immunocytochemical staining of estrogen receptor in paraffin sections of human breast cancer by use of monoclonal antibody: comparison with that in frozen sections.

Immunocytochemical staining of estrogen receptor in paraffin sections of human breast cancer by use of monoclonal antibody: comparison with that in frozen sections.

The Correlation between GPR30 and Clinicopathologic Variables in Breast Carcinomas

Distribution and characterization of estrogen receptor G protein-coupled receptor 30 in the rat central nervous system

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