Expression of functional sulfotransferases (SULT) 1A1, 1A3, 1B1, 1C2, 1E1, and 2A1 in common marmosets.

Cytosolic sulfotransferases (SULTs), which mediate the conjugation of drugs with 3'-phosphoadenosine-5'-phosphosulfate, have been characterized in humans and cynomolgus monkeys. However, SULTs remain to be evaluated in common marmosets, a species of non-human primate often employed in drug metabolism and pharmacokinetic studies of endogenous and exogenous compounds. In this study, marmoset SULT1A1, 1A3, 1B1, 1C2, 1E1, and 2A1 cDNAs were isolated and characterized, based on genome data. The deduced amino acid sequences of these marmoset SULT cDNAs had high identities (90-95%) with their human orthologs, except for marmoset SULT2A1, which was only 81% identical to human SULT2A1. The amino acid sequences of the orthologs of these six SULTs in marmosets, monkeys, and humans were closely clustered in a phylogenetic tree. The structures and genomic organizations of marmoset SULT genes were similar to those of their human orthologs. Among the five marmoset tissues analyzed, SULT mRNAs showed typical expression patterns. The most abundant SULT mRNAs were SULT1B1 in liver, small intestine, and kidney; SULT1E1 in lung; and SULT1A3 in brain. Recombinant marmoset SULT1A1, 1A3, 1B1, 1C2, 1E1, and 2A1 proteins expressed in bacterial cytosolic fractions mediated sulfate conjugations with 3'-phosphoadenosine-5'-phosphosulfate of the following typical human SULT substrates: dopamine, 1-naphthol, p-nitrophenol, estradiol, and dehydroepiandrosterone. Taken together, these wide-ranging results suggest functional and molecular similarities of SULTs among marmosets, monkeys, and humans.