Abstract
2-Chloroadenosine (ClAdo) has been considered not to be phosphorylated by human cells. We cultured a human B cell line WI-L2 with this adenosine analog and found that human cells are able to phosphorylate ClAdo. The human cells were indeed killed by the drug. Since adenosine kinase negative variant of WI-L2 cells phosphorylated ClAdo at a slower rate than the parenteral cells, and the former were less sensitive than the latter to ClAdo, adenosine kinase was considered to participate in the phosphorylation and cytotoxicity. However, ClAdo was phosphorylated, although to minor extent, by adenosine kinase negative cells, while they were not able to phosphorylate MMPR, suggesting that other enzyme(s), in addition to adenosine kinase, also participate in the phosphorylation. We determined the rate of the production of hypoxanthine using HGPRT-negative WI-L2. When ClAdo was added to the medium, the human cells synthesized hypoxanthine more rapidly than control cultures containing no ClAdo. We found that ClAdo, at low concentrations, increased the level of IMP within the cells, and, at higher concentrations, decreased the level of ATP. These data suggest that ClAdo, by consuming ATP, increases the production of IMP and then hypoxanthine. There are numbers of reactions within the body that consume ATP, and acceleration of some of those reactions may be associated with the mechanisms of human hyperuricemia.
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Yamanaka, H., Nobori, T., Kamatani, N. et al. 2-COROADENOSINE IS PHOSPHORYLATED AND INCREASES THE PRODUCTION OF HYPOXANTHINE IN HUMAN CELLLS: 234. Pediatr Res 19, 782 (1985). https://doi.org/10.1203/00006450-198507000-00254
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DOI: https://doi.org/10.1203/00006450-198507000-00254