Journal
CHEMICAL RESEARCH IN TOXICOLOGY
Volume 19, Issue 7, Pages 894-898Publisher
AMER CHEMICAL SOC
DOI: 10.1021/tx060076u
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Funding
- NIDDK NIH HHS [P30 DK056350, DK 56350] Funding Source: Medline
- NIEHS NIH HHS [R01 ES010845, R01 ES010845-05, ES010845] Funding Source: Medline
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Several methyltransferases have been shown to catalyze the oxidative methylation of inorganic arsenic (iAs) in mammalian species. However, the relative contributions of these enzymes to the overall capacity of cells to methylate iAs have not been characterized. Arsenic (+3 oxidation state) methyltransferase (AS3MT) that is expressed in rat and human hepatocytes catalyzes the conversion of iAs, yielding methylated metabolites that contain arsenic in +3 or +5 oxidation states. This study used short hairpin RNA (shRNA) to knock down AS3MT expression in human hepatocellular carcinoma (HepG2) cells. In a stable clonal HepG2/A cell line, AS3MT mRNA and protein levels were reduced by 83 and 88%, respectively. In comparison, the capacity to methylate iAs decreased only by 70%. These data suggest that AS3MT is the major enzyme in this pathway, although an AS3MT-independent process may contribute to iAs methylation in human hepatic cells.
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