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17β-estradiol 3-sulfate |
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CHEBI:4866 |
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17beta-estradiol 3-sulfate |
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A steroid sulfate obtained by the formal condensation of sulfuric acid with the 3-hydroxy group of 17β-estradiol. |
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This entity has been manually annotated by the ChEBI Team.
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ZINC000004097545 |
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Molfile
XML
SDF
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more structures >>
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call loadScript javascripts\jsmol\core\package.js call loadScript javascripts\jsmol\core\core.z.js -- required by ClazzNode call loadScript javascripts\jsmol\J\awtjs2d\WebOutputChannel.js
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InChI=1S/C18H24O5S/c1- 18- 9- 8- 14- 13- 5- 3- 12(23- 24(20,21) 22) 10- 11(13) 2- 4- 15(14) 16(18) 6- 7- 17(18) 19/h3,5,10,14- 17,19H,2,4,6- 9H2,1H3,(H,20,21,22) /t14- ,15- ,16+,17+,18+/m1/s1 |
QZIGLSSUDXBTLJ-ZBRFXRBCSA-N |
C1=C2C(CC[C@]3([C@@]4(CC[C@@H]([C@]4(CC[C@@]32[H])C)O)[H])[H])=CC(=C1)OS(O)(=O)=O |
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mammalian metabolite
Any animal metabolite produced during a metabolic reaction in mammals.
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View more via ChEBI Ontology
17β-hydroxyestra-1(10),2,4-trien-3-yl hydrogen sulfate
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(17β)-17-hydroxyestra-1(10),2,4-trien-3-yl hydrogen sulfate
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ChEBI
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17β-hydroxyestra-1,3,5(10)-trien-3-yl hydrogen sulfate
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IUPAC
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estradiol 3-sulphate
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ChemIDplus
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Estradiol-17beta 3-sulfate
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KEGG COMPOUND
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estradiol-3-sulfate
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ChemIDplus
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3220773
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Reaxys Registry Number
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Reaxys
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481-96-9
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CAS Registry Number
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ChemIDplus
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Kumar V, Johnson AC, Nakada N, Yamashita N, Tanaka H (2012) De-conjugation behavior of conjugated estrogens in the raw sewage, activated sludge and river water. Journal of hazardous materials 227-228, 49-54 [PubMed:22664257] [show Abstract] The fate and behavior of estrone-3-sulfate (E1-3S), estradiol-3-sulfate (E2-3S), estrone-3-glucuronide (E1-3G) and estradiol-3-glucuronide (E2-3G) were studied in raw sewage, activated sludge and river water using microcosms. The glucuronide conjugates had a half-life of 0.4h in raw sewage, yielding 40-60% of their free estrogens. Field observations at three activated sludge processes suggested complete transformation of the glucuronide conjugates in the sewer. In river water glucuronide conjugates half-lives extended to over 2d yielding 60-100% of their free parent estrogens. Transformation of the sulfate conjugates in raw sewage and river water was slow with little formation of the parent estrogens. Sulfate conjugates could readily be detected in sewage influent in the field studies. In activated sludge the sulfate conjugates had half-lives of 0.2h with the transient formation of 10-55% of the free parent estrogens. Field studies indicated transformation of sulfate conjugates across the sewage treatment, although a proportion escaped into the effluent. These results broadly support the view that glucuronide conjugates will be entirely transformed within the sewer largely to their parent estrogens. The sulfate conjugates may persist in raw sewage and river water but are transformable in activated sludge and, in the case of E2-3S, reform a high proportion of the parent estrogen. | Rabaglino MB, Richards E, Denslow N, Keller-Wood M, Wood CE (2012) Genomics of estradiol-3-sulfate action in the ovine fetal hypothalamus. Physiological genomics 44, 669-677 [PubMed:22570439] [show Abstract] In fetal sheep during late gestation sulfoconjugated estrogens in plasma reach a concentration 40-100 times greater than unconjugated estrogens. The objective of the present study was to determine the genomics of estradiol-3-sulfate (E(2)S) action in the ovine fetal brain. The hypothesis was that E(2)S stimulates genes involved in the neuroendocrine pathways that direct or facilitate fetal development at the end of gestation. Four sets of chronically catheterized ovine twin fetuses were studied (gestational age: 120-127 days gestation) with one infused with E(2)S intracerebroventricularly (1 mg/day) and the other remaining untreated (control). After euthanasia, mRNA samples were extracted from fetal brains. Only hypothalamic samples were employed for this study given the important function of this brain region in the control of the hypothalamus-pituitary-adrenal axis. Microarray analysis was performed following the Agilent protocol for one-color 8 × 15 microarrays, designed for Ovis aries. A total of 363 known genes were significantly upregulated by the E(2)S treatment (P < 0.05). Network and enrichment analyses were performed using the Cytoscape/Bingo software, and the results validated by quantitative real-time PCR. The main overrepresented biological processes resulting from this analysis were feeding behavior, hypoxia response, and transforming growth factor signaling. Notably, the genes involved in the feeding behavior (neuropeptide Y and agouti-related protein) were the most strongly induced by the E(2)S treatment. In conclusion, E(2)S may be an important component of the mechanism for activating orexigenic, hypoxia responsiveness and neuroprotective pathways in the lamb as it approaches postnatal life. | Wood CE (2011) Fetal hypothalamus-pituitary-adrenal responses to estradiol sulfate. Endocrinology 152, 4966-4973 [PubMed:21952234] [show Abstract] Estradiol (E(2)) is an important modifier of the activity of the fetal hypothalamus-pituitary-adrenal axis. We have reported that estradiol-3-sulfate (E(2)SO(4)) circulates in fetal blood in far higher concentrations than E(2) and that the fetal brain expresses steroid sulfatase, required for local deconjugation of E(2)SO(4). We performed the present study to test the hypothesis that chronic infusion of E(2)SO(4) chronically increases ACTH and cortisol secretion and that it shortens gestation. Chronically catheterized fetal sheep were treated with E(2)SO(4) intracerebroventricular (n = 5), E(2)SO(4) iv (n = 4), or no steroid infusion (control group, n = 5). Fetuses were subjected to arterial blood sampling every other day until spontaneous birth for plasma hormone analysis. Treatment with E(2)SO(4) attenuated preparturient increases in ACTH secretion near term without affecting the ontogenetic rise in plasma cortisol. Infusion of E(2)SO(4) intracerebroventricularly significantly increased plasma E(2), plasma E(2)SO(4), and plasma progesterone and shortened gestation compared with all other groups. These results are consistent with the conclusion that E(2)SO(4): 1) interacts with the hypothalamus-pituitary-adrenal axis primarily by stimulating cortisol secretion and inhibiting ACTH and pro-ACTH secretion by negative feedback; and 2) stimulates the secretion of E(2) and E(2)SO(4). We conclude that the endocrine response to E(2)SO(4) in the fetus is not identical with the response to E(2). | Winikor J, Schlaerth C, Rabaglino MB, Cousins R, Sutherland M, Wood CE (2011) Complex actions of estradiol-3-sulfate in late gestation fetal brain. Reproductive sciences (Thousand Oaks, Calif.) 18, 654-665 [PubMed:21273638] [show Abstract] The most abundant form of estrogen circulating in fetal plasma is sulfo-conjugated estrogen; for example, estradiol-3-sulfate (E(2)SO(4)) is more highly abundant than estradiol (E(2)). The present study investigated the ontogeny of the deconjugating (steroid sulfatase [STS]) and conjugating (estrogen sulfotransferase [STF]) enzymes in ovine fetal brain and tested the hypothesis that treatment with E(2)SO(4) would alter the expression of one or both enzymes. Steroid sulfatase was more highly expressed than STF, and both changed as a function of gestational age. Estradiol-3-sulfate infused intracerebroventricularly (icv) significantly increased plasma adrenocorticotropic hormone (ACTH) and cortisol concentrations. Plasma E(2) and E(2)SO(4) were increased, and brain expression of estrogen receptor α was decreased. The proteins STS and STF were up- and downregulated, respectively. Pituitary proopiomelanocortin (POMC) and follicle-stimulating hormone (FSH) and hypothalamic corticotrophin-releasing hormone (CRH) messenger RNA (mRNA) was decreased. We conclude that E(2)SO(4) has complex actions on the fetal brain, which might involve deconjugation by STS, but that the net result of direct E(2)SO(4) icv infusion is more complex than can be accounted for by infusion of E(2) alone. | Scherr FF, Sarmah AK, Di HJ, Cameron KC (2009) Degradation and metabolite formation of 17beta-estradiol-3-sulphate in New Zealand pasture soils. Environment international 35, 291-297 [PubMed:18694598] [show Abstract] Estrogens-sulphates such as 17beta-estradiol-3-sulphate and estrone-3-sulphate are excreted by livestock in the urine. These conjugates are precursors to the free counterparts 17beta-estradiol and estrone, which are endocrine disrupting chemicals. In this study microcosm laboratory experiments were conducted in three pasture soils from New Zealand to study the aerobic degradation and metabolite formation kinetics of 17beta-estradiol-3-sulphate at three different incubation temperatures. The degradation of 17beta-estradiol-3-sulphate followed a first-order kinetic and the temperature dependence of the rate constants was sufficiently described by the Arrhenius equation. Degradation was different between the three investigated soils and the rate constants across the soils were significantly correlated to the arylsulphatase activity at 7.5 and 15 degrees C. Estrone-3-sulphate and 17beta-estradiol were identified as primary metabolites and estrone as a secondary metabolite. Results suggest arylsulphatase activity originating from soil microbial biomass is the main driver for the degradation of 17beta-estradiol-3-sulphate. | Wang LQ, James MO (2005) Sulfotransferase 2A1 forms estradiol-17-sulfate and celecoxib switches the dominant product from estradiol-3-sulfate to estradiol-17-sulfate. The Journal of steroid biochemistry and molecular biology 96, 367-374 [PubMed:16011896] [show Abstract] Using recombinant sulfotransferases (SULTs) expressed in E. coli, beta-estradiol (E2) sulfonation was examined to determine which SULT enzyme is responsible for producing E2-17-sulfate (E2-17-S). SULTs 1A1*1, 1A1*2, 1A3, 1E1 and 2A1 all sulfated E2 to varying extents. No activity was observed with SULT1B1. Among the SULTs studied, SULT2A1 produced primarily E2-3-sulfate (E2-3-S), but also some E2-17-S and trace amounts of E2 disulfate. SULT2A1 had a K(m) value of 1.52 microM for formation of E2-3-S and 2.95 microM for formation of E2-17-S. SULT2A1 had the highest V(max) of 493 pmol/min/mg protein for formation of E2-3-S, which was 8.8- and 47-fold higher than the maximal rates of formation of E2-17-S and E2 disulfate, respectively. SULT2A1 formed E2-3-S more efficiently. However, when celecoxib (0-160 microM) was included in the incubation with either SULT2A1 or human liver cytosol, sulfonation switched from E2-3-S to E2-17-S in a concentration-dependent manner. The ratio of E2-17-S/E2-3-S went up to 15 with SULT2A1, and was saturated at 1 with human liver cytosol. In both cases, more E2-17-S was formed, with the unreacted E2 remained unchanged, suggesting celecoxib probably bound to a separate effector site to cause a conformational change in SULT2A1, which favored production of E2-17-S. The ability of celecoxib to alter the position of sulfonation of E2 may in part explain its success in the experimental prevention and treatment of breast cancer. |
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