The Complete Primary Structure of Human Estrogen Receptor β (hERβ) and Its Heterodimerization with ER αin Vivoandin Vitro

Ogawa, Sumito; Inoue, Satoshi; Watanabe, Tôru; Hiroi, Hisahiko; Orimo, Akira; Hosoi, Takayuki; Ouchi, Yasuyoshi; Muramatsu, Masami

doi:10.1006/bbrc.1997.7893

Cited by 467 publications

(279 citation statements)

References 22 publications

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“…Similarly Western blotting indicated that the monoclonal antibody identified ERb but not ERa in breast cancers. Most of the ERb1 protein detected in the extracts from the breast cancers migrated with the same apparent size as the 'long' and 'short' forms of recombinant ERb1, which are formed by translation from different ATGs in the mRNA (Mosselman et al, 1996;Ogawa et al, 1998a). We did not detect proteins corresponding in size to those that could be translated from mRNAs deleted in exons 5 or 6 (Lu et al, 1998;Brandenberger et al, 1999) predicted to be 16.8 and 13 Kd respectively.…”

Section: Molecular and Cellular Pathologymentioning

confidence: 58%

“…Upon completion of the incubation, the sample cDNAs were each diluted to a final volume of 60 ml, and 20 ml used in individual PCR reactions containing primers specific for ERa, ERb or alpha-actin (positive control). The primers employed were as follows: human ERa (Green et al, 1986), forward 5'-GGCCAGTAC-CAATGACAAGGGAAG-3' (nucleotides 787 -811); ERa, reverse 5'-CCAGCAAGCATGTCGAAGATCTCC-3' (nucleotides 1558 -1580); human ERb (Ogawa et al, 1998a), forward 5'-GTTGC-GCCAGCCCTGTTAC-3' (nucleotides 493 -512); ERb, reverse 5'-CTCGTCGGCACTTCTCTGTCTC-3' (nucleotides 788 -809); alpha-actin forward, 5'-GGAGCAATGATCTTGATCTT-3'; alphaactin reverse, 5'-CCTTCCTGGGCATGGAGTCCT-3'. The primers used to amplify the oestrogen receptor cDNAs were chosen to span regions separated by two intronic regions.…”

Section: Detection Of Era and Erb By Reverse Transcriptionpolymerase mentioning

confidence: 99%

“…These were hERb1 'short', a *53 Kd form of the receptor (bs) synthesized from a cDNA (Mosselman et al, 1996) lacking the first potential start site for translation (Ogawa et al, 1998a), and hERb1 'long' (bL) the larger protein (*59 Kd) synthesized from the full length cDNA (Ogawa et al, 1998a). Recombinant hERa (*66 Kd) was also obtained from Pan Vera.…”

Section: Western Analysismentioning

confidence: 99%

“…These results were consistent with previously published data (Saunders et al, 2000); no binding of the ERb specific monoclonal to ERa was observed (Figure 2, lower panel, lane a). The anti-hERb monoclonal that was directed against a peptide at the C-terminus of hERb bound to both short (Mosselman et al, 1996) and long (Ogawa et al, 1998a) forms of ERb. This result is consistent with data that has demonstrated that the difference in size of the long and short forms of ERb is due to use of alternative start sites for translation within the full length mRNA and that the C-termini of both proteins are identical.…”

Section: Specificity Of Antisera and Extraction Of Er Proteins From Bmentioning

confidence: 99%

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Expression of oestrogen receptor beta (ERβ1) protein in human breast cancer biopsies

et al. 2002

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Oestrogen action is mediated via specific receptors that act as ligand-activated transcription factors. A monoclonal antibody specific to the C-terminus of human oestrogen receptor beta has been characterized and the prevalence of expression of oestrogen receptor beta protein investigated in a well defined set of breast cancers. Reverse transcription-polymerase chain reaction analysis of RNA from tissue biopsies detected oestrogen receptor beta in all samples examined. The anti-oestrogen receptor beta antibody cross reacted specifically with both long (*59 Kd) and short (*53 Kd) forms of recombinant oestrogen receptor beta. Western blot analysis of breast tumours contained both forms of oestrogen receptor beta protein although in some samples lower molecular weight species (32 -45 Kd) were identified. Fifty-one breast cancer biopsies were examined using immunohistochemistry; 41 (80%) were immunopositive for oestrogen receptor alpha, 48 (94%) were immunopositive for oestrogen receptor beta and 38 (74.5%) co-expressed both receptors. Expression of oestrogen receptor beta was exclusively nuclear and occurred in multiple cell types. There was no quantitative relationship between staining for the two ERs although in tumours in which both receptors were present immunoexpression of oestrogen receptor alpha was invariably more intense. The significance of oestrogen receptor beta protein expression in breast cancers to therapy remains to be determined but the availability of a well characterized antibody capable of detecting oestrogen receptor beta in archive material will facilitate the process.

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Section: Molecular and Cellular Pathologymentioning

confidence: 58%

Section: Detection Of Era and Erb By Reverse Transcriptionpolymerase mentioning

confidence: 99%

Section: Western Analysismentioning

confidence: 99%

Section: Specificity Of Antisera and Extraction Of Er Proteins From Bmentioning

confidence: 99%

See 2 more Smart Citations

Expression of oestrogen receptor beta (ERβ1) protein in human breast cancer biopsies

et al. 2002

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“…In 1996, a second ER isoform, ERβ, was first cloned as a 477 aminoacid polypeptide from a prostate cDNA library [4, 137]. Two years later ERβ was definitively identified as a 530 residue protein [138]. ERα and ERβ are the products of two genes belonging to different chromosomes (6q25.1 and 14q23-24.1 respectively) [139, 140].…”

Section: Molecular Mechanismsmentioning

confidence: 99%

Combating Malaria with Plant Molecules: A Brief Update

Negi¹,

Gupta²,

Hamid

2013

CMC

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Observations on the role of ovarian hormones in breast cancer growth, as well as interest in contraception, stimulated research into the biology of estrogens. The identification of the classical receptors ERα and ERβ and the transmembrane receptor GPER and the resolution of the structure of the ligand bound to its receptor established the principal molecular mechanisms of estrogen action. The presence of estrogen-like compounds in many plants used in traditional medicine or ingested as food ingredients, phytoestrogens, as well as the estrogenic activities of many industrial pollutants and pesticides, xenoestrogens, have prompted investigations into their role in human health. Phyto- and xenoestrogens bind to the estrogen receptors with a lower affinity than the endogenous estrogens and can compete or substitute the hormone. Xenoestrogens, which accumulate in the body throughout life, are believed to increase breast cancer risk, especially in cases of prenatal and prepuberal exposure whereas the role of phytoestrogens is still a matter of debate. At present, the application of phytoestrogens appears to be limited to the treatment of post-menopausal symptoms in women where the production of endogenous estrogens has ceased. In this review we discuss chemistry, structure and classification, estrogen signaling and the consequences of the interactions of estrogens, phytoestrogens and xenoestrogens with their receptors, the complex interactions of endogenous and exogenous ligands, the evaluation of the health risks related to xenoestrogens, and the perspectives toward the synthesis of potent third generation selective estrogen receptor modulators (SERMs).

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Oestrogen receptor and its potential role in breast cancer development

Walker

1999

J. Pathol.

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The first studies of oestrogen receptor (ER) focused on measurements of levels in breast cancers and relationship to hormonal response, but the introduction of antibodies which can be used on fixed tissue has meant that ER can be studied in detail in normal and precancerous tissue. Cloning and sequencing of ER has resulted in more detailed understanding of structure and function, with the identification of variant forms in both tumours and normal, followed by the discovery that ER has two forms, the classical ER‐α and ER‐β. Analyses of both forms in normal and preneoplastic breast will be important for our understanding of the role of ER in the development of breast cancer and its possible prevention. Copyright © 1999 John Wiley & Sons, Ltd.

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The Complete Primary Structure of Human Estrogen Receptor β (hERβ) and Its Heterodimerization with ER αin Vivoandin Vitro

Cited by 467 publications

References 22 publications

Expression of oestrogen receptor beta (ERβ1) protein in human breast cancer biopsies

Expression of oestrogen receptor beta (ERβ1) protein in human breast cancer biopsies

Combating Malaria with Plant Molecules: A Brief Update

Oestrogen receptor and its potential role in breast cancer development

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