Sulfotransferase activities towards xenobiotics and estradiol in two marine fish species (Mullus barbatus and Lepidorhombus boscii): characterization and inhibition by endocrine disrupters

6 pages, 4 figures, 2 tables.-- PMID: 16806523 [PubMed].-- Printed version published Aug 12, 2006.
We have characterized hepatic phenol sulfotransferase (SULT) activities in two benthic fish species, Mullus barbatus and Lepidorhombus boscii, using p-nitrophenol, dopamine, 17β-estradiol, 4-nonylphenol, and 1-naphthol as substrates. High affinity sulfation of 17β-estradiol was observed in both species (Km = 28–75 nM), suggesting the presence of a specific estrogen sulfotransferase that catalyzes the formation of estradiol-3 sulfate. Among the tested compounds, 1-naphthol was the most effective substrate for sulfation, with Vmax/Km ratios several hundred-fold higher than the other substrates examined. Both species sulfated the tested compounds, but only M. barbatus was able to sulfate dopamine. We also tested the inhibitory effects of common marine pollutants with estrogenic (4-nonylphenol) and androgenic (tributyltin, triphenyltin) properties on p-nitrophenol and 17β-estradiol SULT activities. 4-Nonylphenol and triphenyltin inhibited sulfation of both substrates at micromolar concentrations in both species. However, tributyltin was only effective against SULTs from L. boscii, again at micromolar concentrations. The data indicate that M. barbatus and L. boscii are able to sulfate a range of xenobiotics and endogenous compounds, and inhibition of these activities by environmental pollutants may contribute to the known toxic effects of these compounds.
The study was partially financed by the Spanish Ministry of Science and Technology through the projects Ref. REN2002-01709/HID, and VEM2003-20068-C05-01. Rebeca Martin-Skilton acknowledges a predoctoral fellowship from the Spanish Government. Dr. Rémi Thibaut is greatly acknowledged for technical advice and support.