Abstract
Sulfonation, as mediated by the cytosolic sulfotransferases (SULTs), represents an important mechanism in vivo for the detoxification/metabolism of drugs and other xenobiotics, as well as endogenous neurotransmitters and hormones. Madin-Darby canine kidney (MDCK) cells have been widely used as a model system for investigating the excretion/detoxification mechanism of kidney. In this study, a cDNA encoding a novel canine SULT was cloned from MDCK cells using reverse transcription-polymerase chain reaction (RT-PCR) technique. Nucleotide sequence revealed that the newly cloned canine SULT cDNA has an open reading frame encompassing 912 nucleotides and encoding a 303-amino acid polypeptide. Analysis of the deduced amino acid sequence showed that the novel canine SULT is highly homologous to human SULT1C4, with 82.8% amino acid identity. Recombinant canine SULT1C4, expressed and purified using the pGEX-4T-1 GST gene fusion system, exhibited strong phenol-sulfonating activities toward 1- or 2-naphthol and o-bromophenol among a variety of xenobiotic compounds tested as substrates. These data indicated that the newly identified canine SULT1C4 may function in kidney for the detoxification of xenobiotic compounds.
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