Characterization of a zebrafish estrogen-sulfating cytosolic sulfotransferase: inhibitory effects and mechanism of action of phytoestrogens

Identification of differential hepatic proteins in rare minnow (Gobiocypris rarus) exposed to pentachlorophenol (PCP) by proteomic analysis

“…Sulfonation of E2 has been reported in human liver, carp and zebrafish (Thibaut and Porte, 2004;Ohkimoto et al, 2004;Jurgella et al, 2006). There is evidence that xenobiotics found in polluted environments can inhibit the phase II conjugating enzymes in fish, including those that catalyze sulfonation and glucuronidation of steroids, and potentially disrupt steroid hormone homeostasis (Wang and James, 2006).…”

Sulfonation of 17β-estradiol and inhibition of sulfotransferase activity by polychlorobiphenylols and celecoxib in channel catfish, Ictalurus punctatus

“…The possible existence of two SULT isoforms metabolizing E2, with K m values of 17 nM and 3.2 μM has been reported in carp (Thibaut and Porte, 2004). A putative estrogen-sulfating zebrafish SULT has been characterized and its K m values for estrone and E2 were 12.5 and 13 μM, respectively (Ohkimoto et al, 2004). SULTs that have K m values in the nanomolar range for estrogen sulfonation have been observed in freshwater (Kirk et al, 2003) and marine fish liver (Martin-Skilton et al, 2006).…”

“…However, knowledge of sulfonation in fish species is rather limited. Sulfonation of E2 has been reported in carp and zebrafish, but not whether the 3-or 17-sulfate was formed (Thibaut and Porte, 2004;Ohkimoto et al, 2003Ohkimoto et al, ,2004. Jurgella et al (2006) showed that incubation of E2 with lake trout liver and kidney tissues resulted in the formation of several metabolites, including E2-17-sulfate and E2 3-and 17-glucuronides.…”

“…Sugahara et al (2003a) studied an expressed recombinant zebrafish with sequence similarity to the SULT1 family, which displayed activity towards a number of endogenous compounds including estrone, dopamine and thyroid hormones as well as xenobiotic compounds including some flavonoids, isoflavonoids, and other phenolic compounds. Further studies showed that this zebrafish SULT had activity with E2, however the K m was 13 μM, considerably higher than mammalian SULT1E1 (Ohkimoto et al, 2004). A putative hydroxysteroid SULT2 enzyme has been identified in zebrafish, and this isoform displayed 44%, 43% and 40% amino acid identity with mouse SULT2B1, human SULT2B1 and human SULT2A1, respectively (Sugahara et al 2003b).…”

Steroid catabolism in marine and freshwater fish

“…Several zebrafish SULT isoforms have been identified, expressed and studied with different steroid and non-steroid substrates [96][97][98][99][100][101]. SULTs with similarity to mammalian 1, 2 and 3 families are present in zebrafish [102].…”