Inhibition of Sulfotransferase E1 (SULT1E1)

FMA:83376

FMA Estrogen

GO:0035937

GO estrogen secretion

WIKI increased

WCS_9606

common toxicological species human

10116

NCBI rat

10095

NCBI mice

Inhibition of Sulfotransferase E1 (SULT1E1)

SULT1E1 inhibition

Molecular

Both SULT1E1 expression and function can be measured in tissues and in recombinant systems, such as e.g., Salmonella typhimurium (Kester et al., 2002), Escherichia coli (Parker et al., 2018), V79-1E1 Chinese hamster cells line (Hamers et al., 2006) and in HepG2 cell (Maiti et al., 2007). Expression (gene expression and proteins level) <ul> <li>qRT-PCRn, Northern blotting: SULT1E1 expression (Konings et al., 2018)</li> <li>Western blotting: SULT1E1 protein levels (Konings et al., 2018)</li> <li>Immunohistochemistry: protein levels (Konings et al., 2018)</li> </ul>   Activity (formation of E2 sulfate) <ul> <li>Sulfotransferase kinetic assay: radiometric assays (Hempel et al., 2000; Falany et al., 1995)</li> </ul> In these assays, different types of inhibition of SULT activity, such as competitive, non-competitive and mixed type can be also determined by Lineweaver-Burk analysis (Kester et al., 2002; Hamers et al., 2006). <ul> <li>Levels of sulphated estrogens and/or ratio of conjugated E2/non conjugated E2 (in tissue or in plasma): <ul> <li>liquid chromatography/mass spectrometry (LC/MS); LC-MS/MS after chemical or enzymatic hydrolysis and extraction (Borghoff et al., 2016, Wudy et al., 2018).</li> <li>Radioimmuno Assay (RIA)</li> </ul> </li> <li>Computational models for SULTE1 activation and such as QSAR model for E2-SULT inhibition are also used to demonstrate the criteria for potent inhibition of estrogen sulfotransferase (Harju et al., 2007; Gosavi et al., 2013). </li> </ul>

Taxonomic Applicability: Vertebrates and Invertebrates. Life Stage applicability: all life stages; this AOP specifically refer to the adulthood Sex Applicability: both sexes, this AOP specifically refer to the females

UBERON:0000995

UBERON uterus

CL:0002656

CL glandular cell of endometrium

Moderate Mixed

Moderate

Adult

Biswas DK, Singh S, Shi Q, Pardee AB and Iglehart JD, 2005. Crossroads of estrogen receptor and NF-kappaB signaling. Sci STKE, 2005:pe27. doi: 10.1126/stke.2882005pe27 Borghoff SJ, Wikoff D, Harvey S and Haws L, 2016. Dose- and time-dependent changes in tissue levels of tetrabromobisphenol A (TBBPA) and its sulfate and glucuronide conjugates following repeated administration to female Wistar Han Rats. Toxicol Rep, 3:190-201. doi: 10.1016/j.toxrep.2016.01.007 Britton DJ, Hutcheson IR, Knowlden JM, Barrow D, Giles M, McClelland RA, Gee JM and Nicholson RI, 2006. Bidirectional cross talk between ERalpha and EGFR signalling pathways regulates tamoxifen-resistant growth. Breast Cancer Res Treat, 96:131-146. doi: 10.1007/s10549-005-9070-2 Brooks SC, Rozhin J, Pack BA, Horn L, Godefroi VC, Locke ER, Zemlicka J and Singh DV, 1978. Role of sulfate conjugation in estrogen metabolism and activity. J Toxicol Environ Health, 4:283-300. doi: 10.1080/15287397809529662 Browne P, Judson RS, Casey WM, Kleinstreuer NC and Thomas RS, 2015. Screening Chemicals for Estrogen Receptor Bioactivity Using a Computational Model. Environmental Science & Technology, 49:8804-8814. doi: 10.1021/acs.est.5b02641 Chetrite GS, Cortes-Prieto J, Philippe JC, Wright F and Pasqualini JR, 2000. Comparison of estrogen concentrations, estrone sulfatase and aromatase activities in normal, and in cancerous, human breast tissues. J Steroid Biochem Mol Biol, 72:23-27. doi: 10.1016/s0960-0760(00)00040-6 Dao TL, Hayes C and Libby PR, 1974. Steroid Sulfatase Activities in Human Breast Tumors. Proceedings of the Society for Experimental Biology and Medicine, 146:381-384. doi: 10.3181/00379727-146-38109 Dubik D and Shiu RPC, 1992. Mechanism of estrogen activation of c-myc oncogene expression. Oncogene, 7 8:1587-1594 ECB, 2006  European  Union  Risk  Assessment  Report.  2,2’,6,6’-tetrabromo-4,4’-isopropylidenediphenol,  (tetrabromobisphenol-A  or  TBBP-A).  Part  II –  human health. Luxembourg: Office for Official Publications of the European Communities, European  Commission –  Joint  Research  Centre  Institute for  Health  and  Consumer  Protection. ECHA, 2006. 2,2’,6,6’-TETRABROMO-4,4’-ISOPROPYLIDENEDIPHENOL (TETRABROMOBISPHENOL-A or TBBP-A) Part II – human health United Kingdom, European Chemicals Agency. Ellmann S, Sticht H, Thiel F, Beckmann MW, Strick R and Strissel PL, 2009. Estrogen and progesterone receptors: from molecular structures to clinical targets. Cell Mol Life Sci, 66:2405-2426. doi: 10.1007/s00018-009-0017-3 Falany JL, Azziz R and Falany CN, 1998. Identification and characterization of cytosolic sulfotransferases in normal human endometrium. Chem Biol Interact, 109:329-339. doi: 10.1016/s0009-2797(97)00143-9 Fox EM, Andrade J and Shupnik MA, 2009. Novel actions of estrogen to promote proliferation: integration of cytoplasmic and nuclear pathways. Steroids, 74:622-627. doi: 10.1016/j.steroids.2008.10.014 Gosavi RA, Knudsen GA, Birnbaum LS and Pedersen LC, 2013. Mimicking of estradiol binding by flame retardants and their metabolites: a crystallographic analysis. Environ Health Perspect, 121:1194-1199. doi: 10.1289/ehp.1306902 Gourdy P, Guillaume M, Fontaine C, Adlanmerini M, Montagner A, Laurell H, Lenfant F and Arnal J-F, 2018. Estrogen receptor subcellular localization and cardiometabolism. Molecular Metabolism, 15:56-69. doi: <a href="https://doi.org/10.1016/j.molmet.2018.05.009" style="color:#0563c1; text-decoration:underline">https://doi.org/10.1016/j.molmet.2018.05.009</a> Hamers T, Kamstra JH, Sonneveld E, Murk AJ, Kester MH, Andersson PL, Legler J and Brouwer A, 2006. In vitro profiling of the endocrine-disrupting potency of brominated flame retardants. Toxicol Sci, 92:157-173. doi: 10.1093/toxsci/kfj187 Heldring N, Pike, A., Andersson, S., Matthews, J., Cheng, G., Hartman, J., Tujague, M., Ström, A., Treuter, E., Warner, M., & Gustafsson, J., 2007. Estrogen Receptors: How Do They Signal and What Are Their Targets. Physiological Reviews, 87:905–931 ISO, 2018a. ISO 19040-1:2018 Water quality — Determination of the estrogenic potential of water and waste water — Part 1: Yeast estrogen screen (Saccharomyces cerevisiae). Place. ISO, 2018b. ISO 19040-2:2018 Water quality — Determination of the estrogenic potential of water and waste water — Part 2: Yeast estrogen screen (A-YES, Arxula adeninivorans). Place. James MO, Li W, Summerlot DP, Rowland-Faux L and Wood CE, 2010. Triclosan  is a potent inhibitor of estradiol and estrone sulfonation in sheep placenta. Environ Int, 36:942-949. doi: 10.1016/j.envint.2009.02.004 Jung EM, An BS, Choi KC and Jeung EB, 2012. Potential estrogenic activity of Triclosan  in the uterus of immature rats and rat pituitary GH3 cells. Toxicol Lett, 208:142-148. doi: 10.1016/j.toxlet.2011.10.017 Kester MH, Bulduk S, van Toor H, Tibboel D, Meinl W, Glatt H, Falany CN, Coughtrie MW, Schuur AG, Brouwer A and Visser TJ, 2002. Potent inhibition of estrogen sulfotransferase by hydroxylated metabolites of polyhalogenated aromatic hydrocarbons reveals alternative mechanism for estrogenic activity of endocrine disrupters. J Clin Endocrinol Metab, 87:1142-1150. doi: 10.1210/jcem.87.3.8311 Konings G, Brentjens L, Delvoux B, Linnanen T, Cornel K, Koskimies P, Bongers M, Kruitwagen R, Xanthoulea S and Romano A, 2018. Intracrine Regulation of Estrogen and Other Sex Steroid Levels in Endometrium and Non-gynecological Tissues; Pathology, Physiology, and Drug Discovery. Frontiers in pharmacology, 9:940. Doi:<a href="https://doi.org/10.3389/fphar.2018.00940" style="color:#0563c1; text-decoration:underline">10.3389/fphar.2018.00940.</a> Available online: <a href="http://europepmc.org/abstract/MED/30283331" style="color:#0563c1; text-decoration:underline">http://europepmc.org/abstract/MED/30283331</a> Kousteni S, Bellido T, Plotkin LI, O'Brien CA, Bodenner DL, Han L, Han K, DiGregorio GB, Katzenellenbogen JA, Katzenellenbogen BS, Roberson PK, Weinstein RS, Jilka RL and Manolagas SC, 2001. Nongenotropic, sex-nonspecific signaling through the estrogen or androgen receptors: dissociation from transcriptional activity. Cell, 104:719-730 Li G, Zhang J, Jin K, He K, Zheng Y, Xu X, Wang H, Wang H, Li Z, Yu X, Teng X, Cao J and Teng L, 2013. Estrogen receptor-α36 is involved in development of acquired tamoxifen resistance via regulating the growth status switch in breast cancer cells. Mol Oncol, 7:611-624. doi: 10.1016/j.molonc.2013.02.001 Louis GW, Hallinger DR and Stoker TE, 2013. The effect of Triclosan  on the uterotrophic response to extended doses of ethinyl estradiol in the weanling rat. Reprod Toxicol, 36:71-77. doi: 10.1016/j.reprotox.2012.12.001 Montagnini BG, Pernoncine KV, Borges LI, Costa NO, Moreira EG, Anselmo-Franci JA, Kiss ACI and Gerardin DCC, 2018. Investigation of the potential effects of Triclosan  as an endocrine disruptor in female rats: Uterotrophic assay and two-generation study. Toxicology, 410:152-165. doi: 10.1016/j.tox.2018.10.005 Nilsson S, Mäkelä S, Treuter E, Tujague M, Thomsen J, Andersson G, Enmark E, Pettersson K, Warner M and Gustafsson JA, 2001. Mechanisms of estrogen action. Physiol Rev, 81:1535-1565. doi: 10.1152/physrev.2001.81.4.1535 OECD, 2007. Test No. 440: Uterotrophic Bioassay in Rodents. OECD, 2009. Test No. 230: 21-day Fish Assay. OECD, 2012. Test No. 457: BG1Luc Estrogen Receptor Transactivation Test Method for Identifying Estrogen Receptor Agonists and Antagonists. OECD, 2015a. Test No. 455: Performance-Based Test Guideline for Stably Transfected Transactivation In Vitro Assays to Detect Estrogen Receptor Agonists and Antagonists. OECD, 2015b. Test No. 493: Performance-Based Test Guideline for Human Recombinant Estrogen Receptor (hrER) In Vitro Assays to Detect Chemicals with ER Binding Affinity. OECD, 2018. Revised Guidance Document 150 on Standardised Test Guidelines for Evaluating Chemicals for Endocrine Disruption. OECD, 2021. Test No. 250: EASZY assay - Detection of Endocrine Active Substances, acting through estrogen receptors, using transgenic tg(CYP19A1B:GFP) Zebrafish embrYos. PACK BA and BROOKS SC, 1974. Cyclic Activity of Estrogen Sulfotransferase in the Gilt Uterus. Endocrinology, 95:1680-1690. doi: 10.1210/endo-95-6-1680 Pasqualini JR and Chetrite GS, 1999. Estrone sulfatase versus estrone sulfotransferase in human breast cancer: potential clinical applications. J Steroid Biochem Mol Biol, 69:287-292. doi: 10.1016/s0960-0760(99)00082-5 Pasqualini JR, Gelly C and Lecerf F, 1986. Biological effects and morphological responses to estriol, estriol-3-sulfate, estriol-17-sulfate and tamoxifen in a tamoxifen-resistant cell line (R-27) derived from MCF-7 human breast cancer cells. European Journal of Cancer and Clinical Oncology, 22:1495-1501. doi: 10.1016/0277-5379(86)90086-6 Pedram A, Razandi M, Blumberg B and Levin ER, 2016. Membrane and nuclear estrogen receptor α collaborate to suppress adipogenesis but not triglyceride content. Faseb j, 30:230-240. doi: 10.1096/fj.15-274878 Pedram A, Razandi M, Lewis M, Hammes S and Levin ER, 2014. Membrane-localized estrogen receptor α is required for normal organ development and function. Dev Cell, 29:482-490. doi: 10.1016/j.devcel.2014.04.016 Qian YM, Sun XJ, Tong MH, Li XP, Richa J and Song W-C, 2001. Targeted Disruption of the Mouse Estrogen Sulfotransferase Gene Reveals a Role of Estrogen Metabolism in Intracrine and Paracrine Estrogen Regulation. Endocrinology, 142:5342-5350. doi: 10.1210/endo.142.12.8540 Reinen J and Vermeulen NP, 2015. Biotransformation of endocrine disrupting compounds by selected phase I and phase II enzymes--formation of estrogenic and chemically reactive metabolites by cytochromes P450 and sulfotransferases. Curr Med Chem, 22:500-527. doi: 10.2174/0929867321666140916123022 Rodríguez PE and Sanchez MS, 2010. Maternal exposure to Triclosan  impairs thyroid homeostasis and female pubertal development in Wistar rat offspring. J Toxicol Environ Health A, 73:1678-1688. doi: 10.1080/15287394.2010.516241 Sanders JM, Coulter SJ, Knudsen GA, Dunnick JK, Kissling GE and Birnbaum LS, 2016. Disruption of estrogen homeostasis as a mechanism for uterine toxicity in Wistar Han rats treated with tetrabromobisphenol A. Toxicology and Applied Pharmacology, 298:31-39. doi: <a href="https://doi.org/10.1016/j.taap.2016.03.007" style="color:#0563c1; text-decoration:underline">https://doi.org/10.1016/j.taap.2016.03.007</a> Shevtsov S, Petrotchenko EV, Pedersen LC and Negishi M, 2003. Crystallographic analysis of a hydroxylated polychlorinated biphenyl (OH-PCB) bound to the catalytic estrogen binding site of human estrogen sulfotransferase. Environ Health Perspect, 111:884-888. doi: 10.1289/ehp.6056 Shupnik MA, 2004. Crosstalk between steroid receptors and the c-Src-receptor tyrosine kinase pathways: implications for cell proliferation. Oncogene, 23:7979-7989. doi: 10.1038/sj.onc.1208076 Sinreih M, Knific T, Anko M, Hevir N, Vouk K, Jerin A, Frković Grazio S and Rižner TL, 2017. The Significance of the Sulfatase Pathway for Local Estrogen Formation in Endometrial Cancer. Frontiers in pharmacology, 8. doi: 10.3389/fphar.2017.00368 Stoker TE, Gibson EK and Zorrilla LM, 2010. Triclosan  exposure modulates estrogen-dependent responses in the female wistar rat. Toxicol Sci, 117:45-53. doi: 10.1093/toxsci/kfq180 Tong MH, Jiang H, Liu P, Lawson JA, Brass LF and Song WC, 2005. Spontaneous fetal loss caused by placental thrombosis in estrogen sulfotransferase-deficient mice. Nat Med, 11:153-159. doi: 10.1038/nm1184 USEPA, 2009. Endocrine disruptor screening program test guidelines OPPTS 890.1250: estrogen receptor binding (rat uterine cytosol). . EPA (ed.). Washington DC. Utsunomiya H, Ito K, Suzuki T, Kitamura T, Kaneko C, Nakata T, Niikura H, Okamura K, Yaegashi N and Sasano H, 2004. Steroid sulfatase and estrogen sulfotransferase in human endometrial carcinoma. Clin Cancer Res, 10:5850-5856. doi: 10.1158/1078-0432.Ccr-04-0040 Wang LQ and James MO, 2006. Inhibition of sulfotransferases by xenobiotics. Curr Drug Metab, 7:83-104. doi: 10.2174/138920006774832596 Wilson VS, Bobseine K and Gray LE, Jr., 2004. Development and Characterization of a Cell Line That Stably Expresses an Estrogen-Responsive Luciferase Reporter for the Detection of Estrogen Receptor Agonist and Antagonists. Toxicological Sciences, 81:69-77. doi: 10.1093/toxsci/kfh180 Yang J, Singleton DW, Shaughnessy EA and Khan SA, 2008. The F-domain of estrogen receptor-alpha inhibits ligand induced receptor dimerization. Mol Cell Endocrinol, 295:94-100. doi: 10.1016/j.mce.2008.08.001 Zheng A, Kallio A and Härkönen P, 2007. Tamoxifen-induced rapid death of MCF-7 breast cancer cells is mediated via extracellularly signal-regulated kinase signaling and can be abrogated by estrogen. Endocrinology, 148:2764-2777. doi: 10.1210/en.2006-1269 AOPWiki 2023-07-28T06:39:56

2023-08-14T06:35:55

Increased, estrogens

Cellular

Biological state: The most predominant form of estrogens is 17β-estradiol (E2) which is sex hormone. In women having premenopausal it is mainly produced in the ovaries. For postmenopausal women, it E2 primarily is sythesized from testosterone by aromatase enzyme in extragonadal tissues(Simpson, 2003). Estradiol stimulates both cell growth and cholesterogenesis in the MCF-7 line (breast cancer cell line) (Cypriani et al., 1988). Cholesterol increases neuronal estradiol release into the medium through synapse formation(Fester et al., 2009). Biological compartments: Estrogen is considered as the risk of developing cholesterol gallstones by enhancing the hepatic secretion of biliary cholesterol leading to an increase in cholesterol(Wang et al., 2009). General role in biology: When estrogen levels decline, levels of low-density lipoprotein, the harmful kind of cholesterol increases, and levels of high-density lipoprotein, the positive kind of cholesterol decrease, due to which fat build up in the body and cholesterol in the arteries that causes heart attack and stroke(Fåhraeus, 1988; Wahl et al., 1983). Granulosa cells are the primary cell which provides the support and microenvironment required for the developing oocyte in the ovary(Sen and Hammes, 2010; Sterneck et al., 1997).

Radioimmunoassay (RIA) and analytical method based on mass spectroscopic are used for estrogen measurement present in serum (Smy and Straseski, 2018; Giese, 2003).

It is applicable in reproduction system, cell growth and cell function

UBERON:0003133

UBERON reproductive organ

CL:0000174

CL steroid hormone secreting cell

High Female Moderate Male

High

Adult, reproductively mature

High High High

Adashi, E., & Hsueh, A. (1982). Estrogens augment the stimulation of ovarian aromatase activity by follicle-stimulating hormone in cultured rat granulosa cells. Journal of Biological Chemistry, 257(11), 6077-6083. Cypriani, B., Tabacik, C., & Descomps, B. (1988). Effect of estradiol and antiestrogens on cholesterol biosynthesis in hormone-dependent and-independent breast cancer cell lines. Biochimica et Biophysica Acta (BBA)-Bioenergetics, 972(2), 167-178. Darabi, M., Rabbani, M., Ani, M., Zarean, E., Panjehpour, M., & Movahedian, A. (2011). Increased leukocyte ABCA1 gene expression in post-menopausal women on hormone replacement therapy. Gynecological Endocrinology, 27(9), 701-705. Fåhraeus, L. (1988). The effects of estradiol on blood lipids and lipoproteins in postmenopausal women. Obstetrics and gynecology, 72(5 Suppl), 18S-22S. Fester, L., Zhou, L., Bütow, A., Huber, C., Von Lossow, R., Prange‐Kiel, J., et al. (2009). Cholesterol‐promoted synaptogenesis requires the conversion of cholesterol to estradiol in the hippocampus. Hippocampus, 19(8), 692-705. Giese, R. W. (2003). Measurement of endogenous estrogens: analytical challenges and recent advances. Journal of Chromatography A, 1000(1), 401-412. doi:https://doi.org/10.1016/S0021-9673(03)00306-6. Mao, Z., Li, J., & Zhang, W. (2018). Hormonal regulation of cholesterol homeostasis. Cholesterol-Good, Bad and the Heart. Park, Y., Maizels, E. T., Feiger, Z. J., Alam, H., Peters, C. A., Woodruff, T. K., et al. (2005). Induction of cyclin D2 in rat granulosa cells requires FSH-dependent relief from FOXO1 repression coupled with positive signals from Smad. Journal of Biological Chemistry, 280(10), 9135-9148. Sen, A., & Hammes, S. R. (2010). Granulosa cell-specific androgen receptors are critical regulators of ovarian development and function. Molecular endocrinology, 24(7), 1393-1403. Simpson, E. R. (2003). Sources of estrogen and their importance. The Journal of steroid biochemistry and molecular biology, 86(3-5), 225-230. Smy, L., & Straseski, J. A. (2018). Measuring estrogens in women, men, and children: Recent advances 2012-2017. Clin Biochem, 62, 11-23. Sterneck, E., Tessarollo, L., & Johnson, P. F. (1997). An essential role for C/EBPβ in female reproduction. Genes & development, 11(17), 2153-2162. Wahl, P., Walden, C., Knopp, R., Hoover, J., Wallace, R., Heiss, G., et al. (1983). Effect of estrogen/progestin potency on lipid/lipoprotein cholesterol. New England Journal of Medicine, 308(15), 862-867. Wang, H. H., Liu, M., Clegg, D. J., Portincasa, P., & Wang, D. Q.-H. (2009). New insights into the molecular mechanisms underlying effects of estrogen on cholesterol gallstone formation. Biochimica et Biophysica Acta (BBA)-Molecular and Cell Biology of Lipids, 1791(11), 1037-1047. AOPWiki 2022-02-25T23:56:25

2022-03-01T06:58:15

<upstream-id>18d024a1-f0db-4772-9ee8-ce23515a1ab0</upstream-id> <downstream-id>46114827-b2d5-4017-bf7e-26829d46a110</downstream-id>

#<Reference::ActiveRecord_Associations_CollectionProxy:0x00005eb8a324b458> AOPWiki 2023-07-28T07:03:07

2023-07-28T07:03:07

SULT1E1 inhibition leading to uterine adenocarcinoma via increased estrogen availability at target organ level

SULT1E1 inhibition and increased oestradiol availability

Allie Always

Anna Lanzoni Martina Panzarea

2.5

adjacent

Not Specified

<div> <table class="table table-bordered table-fullwidth"> <thead> <tr> <th>Modulating Factor (MF)</th> <th>Influence or Outcome</th> <th>KER(s) involved</th> </tr> </thead> <tbody> <tr> <td> </td> <td> </td> <td> </td> </tr> </tbody> </table> </div>

AOPWiki 2023-07-28T06:28:31

2023-09-25T16:27:15