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Interaction of Estrogenic Chemicals and Phytoestrogens with Estrogen Receptor β.
The estrogenic activity of environmental chemicals and phytoestrogens in competition binding assays with ERα or ERβ protein, and in a transient gene expression assay using cells in which an acute estrogenic response is created by cotransfecting cultures with recombinant human ERβ complementary DNA (cDNA) in the presence of an estrogen-dependent reporter plasmid are investigated. Expand
Comparison of the ligand binding specificity and transcript tissue distribution of estrogen receptors alpha and beta.
The messenger RNA expression of both ER subtypes in rat tissues by RT-PCR is investigated and the ligand binding specificity of the ER sub types is compared to contribute to the selective action of ER agonists and antagonists in different tissues. Expand
Cloning of a novel receptor expressed in rat prostate and ovary.
- G. Kuiper, E. Enmark, M. Pelto-huikko, S. Nilsson, J. Gustafsson
- Biology, Medicine
- Proceedings of the National Academy of Sciences…
- 11 June 1996
It is concluded that clone 29 cDNA encodes a novel rat ER, which is suggested be named rat ERbeta to distinguish it from the previously cloned ER (ERalpha) from rat uterus. Expand
Interaction of estrogenic chemicals and phytoestrogens with estrogen receptor beta.
The estrogenic potency of phytoestrogens is significant, especially for ER beta, and they may trigger many of the biological responses that are evoked by the physiological estrogens. Expand
Comparison of the Ligand Binding Specificity and Transcript Tissue Distribution of Estrogen Receptors α and β.
The messenger RNA expression of both ER subtypes in rat tissues by RT-PCR is investigated and the ligand binding specificity of the ER sub types is compared, revealing a single binding component for 16β-estradiol with high affinity. Expand
Differential ligand activation of estrogen receptors ERalpha and ERbeta at AP1 sites.
The transactivation properties of the two estrogen receptors, ERalpha and ERbeta, were examined with different ligands in the context of an estrogen response element and an AP1 element, suggesting that the two ERs may play different roles in gene regulation. Expand
A mutation in the ligand binding domain of the androgen receptor of human LNCaP cells affects steroid binding characteristics and response to anti-androgens.
- J. Veldscholte, C. Ris-Stalpers, +7 authors E. Mulder
- Biology, Medicine
- Biochemical and biophysical research…
- 14 December 1990
In the LNCaP androgen receptor a single point mutation is discovered changing the sense of codon 868 (Thr to Ala) in the ligand binding domain, which influences both binding and the induction of gene expression by different steroids and antisteroids. Expand
Potent inhibition of estrogen sulfotransferase by hydroxylated PCB metabolites: a novel pathway explaining the estrogenic activity of PCBs.
It is demonstrated that various environmentally relevant PCB-OHs are extremely potent inhibitors of human estrogen sulfotransferase, strongly suggesting that they indirectly induce estrogenic activity by increasing estradiol bioavailability in target tissues. Expand
Ligand-, cell-, and estrogen receptor subtype (alpha/beta)-dependent activation at GC-rich (Sp1) promoter elements.
Transcriptional activation studies showed that only ER(alpha/beta) can activate transcription from an Sp1 element, not ER(beta/alpha), which indicates that the AF-1 domain from ER( alpha) is responsible for activation at an Sp 1 element, independent of ER subtype context. Expand
Association between mutations in a thyroid hormone transporter and severe X-linked psychomotor retardation
It is suggested that this novel syndrome of X-linked psychomotor retardation is due to a defect in T3 entry into neurons through MCT8, resulting in impaired T3 action and metabolism. Expand