Differential Expression of Estrogen Receptors α and β mRNA During Differentiation of Human Osteoblast SV-HFO Cells

Arts, Janine; Kuiper, George G. J. M.; Janssen, J.M.M.F.; Gustafsson, Jan‐Åke; Löwik, Clemens W.G.M.; Pols, Huibert A. P.; Leeuwen, Johannes P. T. M. van

doi:10.1210/endo.138.11.5652

Cited by 245 publications

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“…In the male genital tract, Hess et al (1997) detected mRNA encoding ERβ in the efferent ductules, all regions of the epididymis, the vas deferens and prostate of adult male rats. Consistent with the documented effects of oestrogens on bone physiology (Turner et al, 1994), expression of mRNAs encoding ERα and ERβ have been detected in rat osteoblasts isolated from 1-day-old rat bone (Onoe et al, 1997) and a human osteoblast cell line (Arts et al, 1997). In both rat and human osteoblasts, expression of mRNA encoding ERβ detected by semi-quantitative PCR appeared to be differentially regulated compared with mRNA encoding ERα (Arts et al, 1997;Onoe et al, 1997).…”

Section: Pattern Of Expression Of Mrna Encoding Erβsupporting

confidence: 56%

Oestrogen receptor beta (ER beta)

Saunders¹

1998

Reviews of Reproduction

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, oestrogens, androgens and progestagens) regulate cell function via specific intracellular receptors expressed in their target tissues. The cloning of the cDNAs encoding a number of steroid receptors and comparison of their sequences has revealed that, together with the receptors for thyroid hormones, they belong to a large superfamily of genes that function as ligand-activated transcription factors (reviewed by Carson-Jurnica et al., 1990). A cDNA encoding a receptor that bound oestrogens in vitro was isolated from a human breast cancer cell line in 1986 (Green et al., 1986) and homologous receptors, all with significant sequence homology, were swiftly isolated from rat, mouse and chicken (for example, see White et al., 1987). However, despite an intensive period of research, and identification of many new members of the steroid-thyroid hormone receptor superfamily (reviewed in Mangelsdorf et al., 1995), it was 10 years after the identification of the original oestrogen receptor (ER) that the identification of a second oestrogen-specific receptor was reported (Kuiper et al., 1996). This novel ER, first cloned from a rat prostate cDNA library, has been named oestrogen receptor beta (ERβ) to distinguish it from the previously identified ER which has now been re-named oestrogen receptor alpha (ERα; for review, see .

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Section: Pattern Of Expression Of Mrna Encoding Erβsupporting

confidence: 56%

Oestrogen receptor beta (ER beta)

Saunders¹

1998

Reviews of Reproduction

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“…Studies by our own and other groups have indeed shown that ERβ is expressed in osteoblasts of growing bone in the rat. ERβ is also detected in osteoblastic cell lines, pointing to a possible role of ERβ in bone formation (Onoe et al 1997, Arts et al 1998. The relevance of these observations in the human is, however, unclear, since the only known human patient lacking functional ERα displays severe osteoporosis (Smith et al 1994).…”

Section: Human Erβmentioning

confidence: 99%

Estrogen receptor beta - a novel receptor opens up new possibilities for cancer diagnosis and treatment

Enmark

Gustafsson

1998

Endocrine Related Cancer

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“…The primer at aa-3 has an overlapping region (about 15-20 bp) that begins at the next amino acid in the deletion construct (i.e. aa 51 in ⌬3-50 hER ␣/␤ ) In a separate, simultaneous reaction, another set of primers that span from the last amino acid deleted (this primer also contains an overlap region of about [15][16][17][18][19][20] bp that begins at aa 3 and spans to upstream sequences in the vector) to the EcoRV site in pcDNA3.1hER ␣/␤ are PCR-amplified. The PCR products from both reactions were purified using Wizard PCR Prep DNA purification system (Promega, Madison, WI).…”

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confidence: 99%

Ligand-, Cell-, and Estrogen Receptor Subtype (α/β)-dependent Activation at GC-rich (Sp1) Promoter Elements

Saville¹,

Wormke²,

Wang³

et al. 2000

Journal of Biological Chemistry

378

290

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17␤-Estradiol (E2) induces expression of several genes via estrogen receptor (ER)-Sp1 protein interactions with GC-rich promoter elements in which The estrogen receptor (ER)1 is a member of the nuclear receptor superfamily of transcription factors that exhibit several common structural/functional domains (1, 2). Estrogens, the endogenous ER ligands, influence gene expression and physiological responses in multiple target tissues (3, 4), and mechanisms associated with selective estrogen and antiestrogen action have been extensively investigated. 17␤-Estradiol (E2)-induced transactivation in specific cell types is modulated by multiple factors, including expression of the ER, coactivator and corepressor proteins, other nuclear factors, and accessibility of responsive elements in target gene promoters (5-9). The recent discovery of a second form of the ER (i.e. ER ␤ ) extends the potential tissue-specific selectivity for induction of estrogenic and antiestrogenic responses (10, 11).ER ␣ and ER ␤ exhibit both differential and overlapping expression in various tissues and cell lines (10 -21). For example, in rats, ER ␤ mRNA transcripts were highly expressed in the prostate and ovary; moderate expression was observed in testis, uterus, lung, and bladder; and low ER ␤ expression was observed in the spinal cord, various brain sections, pituitary, epididymis, and thymus (10). In many of these same tissues, both ER ␤ and ER ␣ are co-expressed; however, it was evident that in tissues such as the epididymis, uterus, kidney, and adrenal, which express high levels of ER ␣ mRNA, low to nondetectable ER ␤ mRNA was detected. The functional tissuespecific differences in ER subtypes have not yet been delineated; however, estrogenic responses observed in murine neuronal cells, vascular tissue, and the male reproductive tract of ER ␣ knockout mice suggest that in these tissues, ER ␤ is active in addition to ER ␣ (22-24).There is considerable overlap in the ligand binding and functional properties of ER ␣ and ER ␤ (12,(25)(26)(27)(28)(29)(30). Both proteins bind a diverse spectrum of ligands with similar (but not identical) relative binding affinities; ER ␣ and ER ␤ form homo-and heterodimers that bind estrogen-responsive elements (EREs) in gel mobility shift assays. ER ␣ and ER ␤ activate transcription from ERE-and AP1-containing constructs; however, the effects are ligand-, cell type-, and promoter-dependent (11, 25, 28 -34). A recent study reported that mutation of a conserved tyrosine to asparagine in the ligand binding domains of ER ␣ and ER ␤ conferred hormone-independent activation properties to both ER subtypes (31).Recent studies in our laboratory have demonstrated physical and functional interactions between ER ␣ and the nuclear transcription factor Sp1 (35). E2 induced reporter gene activity in breast cancer cells transfected with pSp1, a construct containing a consensus GC-rich oligonucleotide insert linked to a bacterial CAT reporter gene (35). Sp1 protein plays an important role in regulation of mammalian and viral gene...

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Differential Expression of Estrogen Receptors α and β mRNA During Differentiation of Human Osteoblast SV-HFO Cells

Cited by 245 publications

References 0 publications

Oestrogen receptor beta (ER beta)

Oestrogen receptor beta (ER beta)

Estrogen receptor beta - a novel receptor opens up new possibilities for cancer diagnosis and treatment

Ligand-, Cell-, and Estrogen Receptor Subtype (α/β)-dependent Activation at GC-rich (Sp1) Promoter Elements

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