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MTA 유사체의 Purine Metabolism 에의 영향
최혜선,J . D . Stoecker ( Hye Seon Choi,J . D . Stoeckler ) 생화학분자생물학회 1992 BMB Reports Vol.25 No.1
5`-Deoxy-5`-methylthioadenosine (MTA) which is related to polyamine synthesis, is rapidly converted to 5-methylthioribose 1-phosphate (MTR-1-P) and adenine by the reaction of MTA phosphorylase (MTAPase) (Savarese et al., 1981). MTA analogs in which the ribose moiety was replaced have demonstrated to be cytotoxic (Savarese et al., 1984; Ferro et al., 1982). These results indicated that the common product, 5-modified sugar phosphate, exerted cytotoxic effect against several tumor cells. L5178Y mouse lymphoblastic leukemia cells were treated with 5`-modified adenosines, MTA, 5`-deoxy-5`-isobutylthioadenosine (SIBA), 5`-deoxy-5`-iodoadenosine (5`-IAdo) and 5`-deoxyadenosine (5`-dAdo). The phosphorolysis of 100 μM of 5`-modified nucleosides measured in intact L5178Y cells agreed well with the relative V_m of MTAPase from Sarcoma 180 cells determined by Savarese et al. (1983). 5`-IAdo showed extra inhibition of 5-phosphoribosyl 1-pyrophosphate (PRPP) synthesis at high concentration, but the inhibition by 5`-dAdo, MTA and SIBA could be due to adenine released from 5`-substituted adenosines. 5`-Modified adenosines caused greater inhibition of purine synthesis de novo than the same concentration of adenine as were generated from the 5`-substituted adenosines. No inhibition of purine salvage pathway was observed. 5`-IAdo was most cytotoxic and inhibited purine metabolism to the greatest extent in L5178Y cells. In the HL-60 human promyelocytic leukemia cells and HL-60, APRT-deficient mutant cells, the effects of 5`-IAdo on purine and pyrimidine metabolism were measured. 5`-IAdo had no significant effects on PRPP accumulation, purine synthesis de novo and purine salvage pathway.
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