Sulfonation of environmental estrogens by zebrafish cytosolic sulfotransferases

Ohkimoto, Kei; Sugahara, Takuya; Sakakibara, Yoichi; Suiko, Masahito; Liu, Ming‐Yih; Carter, Glendora; Liu, Ming‐Cheh

doi:10.1016/s0006-291x(03)01524-9

Cited by 17 publications

(9 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Some studies have identified ST activity towards thyroid hormones in plaice (Osborn and Simpson, 1969) and rainbow trout 1997. The effects of environmental estrogens and other endocrine disrupters on ST-mediated conjugation have been studied showing additional implications of these pollutants on biotransformation capabilities (Nishiyama et al, 2002;Kirk et al, 2003;Ohkimoto et al, 2003). The present work corroborated that STs are lower capacity/higher affinity enzymes in comparison to UDPGTs.…”

Section: Sulfotransferase Kineticssupporting

confidence: 78%

Kinetics of hepatic phase I and II biotransformation reactions in eight finfish species

González

Reimschuessel

Shaikh

et al. 2009

Marine Environmental Research

View full text Add to dashboard Cite

Hepatic microsomes and cytosols of channel catfish (Ictalurus punctatus), rainbow trout (Oncorhynchus mykiss), Atlantic salmon (Salmo salar), red tilapia (Oreochromis sp.), largemouth bass (Micropterussalmoides), striped bass (Morone saxatilis), hybrid striped bass (M. saxatilis x M. crysops), and bluegill (Lepomis macrochuris) (n=8) were used to study the kinetics of phase I (ECOD, EROD, PROD, BROD) and phase II (UDP-glucuronosyltransferase (UDPGT)-, sulfotransferase (ST)- and glutathione-s-transferase (GST)-mediated) reactions. The best catalytic efficiency for ECOD and GST activities was performed by channel catfish, Atlantic salmon, rainbow trout and tilapia. The highest EROD catalytic efficiency was for Atlantic salmon. None of the species had either PROD or BROD activities. Rainbow trout had very similar UDPGT catalytic efficiency to tilapia, channel catfish, Atlantic salmon, largemouth bass and bluegill. Sulfotransferase conjugation had no significant differences among the species. In summary, tilapia, channel catfish, Atlantic salmon and rainbow trout had the best biotransforming capabilities; striped bass, hybrid striped bass and bluegill were low metabolizers and largemouth bass shared some capabilities with both groups.

show abstract

Section: Sulfotransferase Kineticssupporting

confidence: 78%

Kinetics of hepatic phase I and II biotransformation reactions in eight finfish species

González

Reimschuessel

Shaikh

et al. 2009

Marine Environmental Research

View full text Add to dashboard Cite

show abstract

“…Other xenobiotics, including alkyphenols and the organotin compounds tributyltin and triphenyltin showed inhibition of E2 sulfonation in fish species (Ohkimoto et al 2003;Ohkimoto et al 2005). The present study showed OH-PCBs were also inhibitors of E2-3S formation by catfish liver sulfotransferases.…”

Section: Discussionmentioning

confidence: 99%

“…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.…”

Section: Introductionmentioning

confidence: 99%

“…Van den Hurk et al (2002) found that several polychlorobiphenylols (OHPCBs) inhibited both the sulfonation and glucuronidation of 3-hydroxybenzo[a]pyrene in channel catfish, indicating that both SULT and glucuronosyltransferase (UGT) are targets for inhibition by xenobiotics in fish. Ohkimoto et al(2003) reported that bisphenol A, 4-nnonylphenol (NP), and 4-n-octylphenol (OP) exerted concentration-dependent inhibition of the sulfonation of E2 in zebrafish, implying a potential role of these environmental estrogens in interfering with the sulfonation of endogenous estrogens. In addition, alkylphenols have a strong inhibitory effect on the sulfonation of estrone in a cyprinid fish, the chub (Leuciscus cephalus) (Kirk et al, 2003), and tributyltin (TBT), triphenyltin (TPT), and nonylphenol (NP) were inhibitors of the sulfonation of E2 by carp (Cyprinus carpio) cytosolic fractions (Thibaut and Porte, 2004), with IC 50 values of 17-41 μM.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

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

Wang

James

2007

Aquatic Toxicology

View full text Add to dashboard Cite

The sulfonation of 17β-estradiol (E2) by human liver and recombinant sulfotransferases is influenced by environmental contaminants such as hydroxylated metabolites of polychlorinated biphenyls (OHPCBs), which are potent inhibitors, and the therapeutic drug, celecoxib, which affects positional sulfonation of E2. In some locations, the aquatic environment is contaminated by PCBs, OH-PCBs and widely used therapeutic drugs. The objectives of this study were to investigate the sulfonation kinetics of E2 in liver cytosol from channel catfish (Ictalurus punctatus); to examine the effect of OH-PCBs on E2 sulfonation; and to determine if celecoxib altered the position of E2 sulfonation, as it does with human liver cytosol. E2 was converted to both 3-and 17-sulfates by catfish liver cytosol. At E2 concentrations below 1 μM, formation of E2-3-sulfate (E2-3-S) predominated, but substrate inhibition was observed at higher concentrations. Rates of E2-3-S formation at different E2 concentrations were fit to a substrate inhibition model, with K′ m and V′ max values of 0.40 ± 0.10 μM and 91.0 ± 4.7 pmol/min/mg protein, respectively and K i of 1.08 ± 0.09 μM. The formation of E2-17-S fit Michaelis-Menten kinetics over the concentration range 25 nM to 2.5 μM, with K m and V max values of 1.07 ± 0.23 μM and 25.7 ± 4.43 pmol/min/mg protein, respectively. The efficiency (V max /K m ) of formation of E2-3-S was 9.8-fold higher than that of E2-17-S. Several OH-PCBs inhibited E2 3-sulfonation, measured at an E2 concentration of 1 nM. Of those tested, the most potent inhibitor was 4′-OH-CB79, with two chlorine atoms flanking the OH group (IC 50 : 94 nM). The inhibition of estrogen sulfonation by OH-PCBs may disrupt the endocrine system and thus contribute to the known toxic effects of these compounds. Celecoxib did not stimulate E2-17-S formation, as is the case with human liver cytosol, but did inhibit the formation of E2-3-S (IC 50 : 44 μM) and to a lesser extent, E2-17-S (IC 50 : >160 μM), suggesting the previously found effect of celecoxib on E2-17-S formation may be specific to human SULT2A1.

show abstract

“…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].…”

Section: Sulfonationmentioning

confidence: 99%

Steroid catabolism in marine and freshwater fish

James

2011

The Journal of Steroid Biochemistry and Molecular Biology

View full text Add to dashboard Cite

Sulfonation of environmental estrogens by zebrafish cytosolic sulfotransferases

Cited by 17 publications

References 20 publications

Kinetics of hepatic phase I and II biotransformation reactions in eight finfish species

Kinetics of hepatic phase I and II biotransformation reactions in eight finfish species

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

Steroid catabolism in marine and freshwater fish

Contact Info

Product

Resources

About