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Literature summary for 2.8.2.4 extracted from

  • Mungenast, F.; Aust, S.; Vergote, I.; Vanderstichele, A.; Sehouli, J.; Braicu, E.; Mahner, S.; Castillo-Tong, D.C.; Zeillinger, R.; Thalhammer, T.
    Clinical significance of the estrogen-modifying enzymes steroid sulfatase and estrogen sulfotransferase in epithelial ovarian cancer (2017), Oncol. Lett., 13, 4047-4054 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.8.2.4

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
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 Homo sapiens 5829
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3'-phosphoadenylyl sulfate + 17beta-estradiol Homo sapiens
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 adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
 ?
3'-phosphoadenylyl sulfate + estrone Homo sapiens
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 adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P49888
-
-

Source Tissue

Source Tissue Comment Organism Textmining
epithelial ovarian cancer cell determination of the levels of SULT1E1, STS and estrogen receptor alpha (ERalpha) protein in paraffin-embedded specimens from 206 patients with Federation of Gynecology and Obstetrics stage II-IV EOC treated with debulking surgery and standard platinum-based adjuvant chemotherapy. Significantly higher SULT1E1 levels are observed in better differentiated EOC tumors compared to grade 3 EOC tumors. STS and SULT1E1 levels are positively associated with ERalpha abundance Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3'-phosphoadenylyl sulfate + 17beta-estradiol
-
 Homo sapiens adenosine 3',5'-bisphosphate + 17beta-estradiol 3-sulfate
-
 ?
3'-phosphoadenylyl sulfate + estrone
-
 Homo sapiens adenosine 3',5'-bisphosphate + estrone 3-sulfate
-
 ?

Synonyms

Synonyms Comment Organism
estrogen sulfotransferase
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 Homo sapiens
SULT1E1
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 Homo sapiens

General Information

General Information Comment Organism
physiological function 17beta-estradiol (E2) can contribute to the progression of epithelial ovarian cancer (EOC). Although the majority of patients with EOC are postmenopausal woman, when de novo estrogen production in the ovary has ceased, ovarian cancer cells remain exposed to estrogens synthesized locally in the cancer cells from inactive sulfonated steroid hormone precurxadsors, such as estrone sulfate taken up from the circulation via the sulfatase pathway. An abundance of the estrogen-modixadfying enzymes, including estrogen-activating steroid sulfatase (STS, EC 3.1.6.2) and estrogen-inactivating estrogen-sulfotransferase (SULT1E1), is important for providing active estrogen to EOC cells. In advanced stage high-grade serous EOC, the most frequent and lethal type of ovarian cancer, SULT1E1 expression is significantly associated with a better overall survival rate. Importance of SULT1E1-mediated estrogen inactivation in EOC, particularly high-grade serous EOC (HGSOC). Therefore, targeting the sulfatase pathway is a potenxadtial endocrine therapeutic intervention for certain patients with estrogen-responsive EOC Homo sapiens