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- 저자 : J . D . Stoeckler ) (검색결과 3 건)
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최혜선,요하나 스토클러,Choi, Hye-Seon,Johanna, D. Stoeckler Korean Society for Biochemistry and Molecular Biol 1990 한국생화학회지 Vol.23 No.3
5-IR-1-P는 여러 종류의 세포에 강력한 독성을 보이는 5'-iodonucleoside에서 생성이 되어지는데 이 때 생성된 5-IR-1-P는 purine, pyrimidine 및 sugar phosphate의 대사에 관계하는 여러 효소의 활성을 억제시켰다. 목표가 되는 암세포로 가는 통로가 되어지는 적혈구에서 purine nucleoside phosphorylase(PNP)의 활성이 높으므로 5'-deoxy-5'-iodoinosine(5'-IIno) 존재하에 5-IR-1-P의 농도가 측정되었다. $560{\mu}M$의 5'-IIno는 $'500{\mu}M$의 5-IR-1-P를 생성한다. 5-IR-1-P의 세포내 농도는 1시간 안에 최대 수준에 도달하여 4시간 동안 변하지 않는다. 바깥에서 공급되는 5'-IIno를 제거하면 5-IR-1-P의 세포내 농도는 $'500{\mu}M$에서 $'300{\mu}M$으로 감소한다. 이미 세포속으로 들어간 5'-IIno만이 존재할 때 5-IR-1-P의 세포내 농도는 점차적으로 감소한다. 이 사실은 5'-IIno이 계속 공급되지 않으면 5-IR-1-P가 빨리 다른 물질로 대사되거나 파괴되는 것을 의미한다. 5'-deoxy-5'-iodoadenosine (5'-IAdo) and 5'-deoxy-5'-iodoinosine (5'-IIno) were highly cytotoxic to several cell lines in vitro. These studies indicated that the pentose l-phosphate generated from the 5'-iodonucleosides is responsible for the cytotoxicity. The synthesized and purified 5-iodoribose 1-phosphate (5-IR-1-P) inhibited several enzymes which are related to purine, pyrimidine and sugar phosphate metabolism. Intracellular concentrations of 5-IR-1-P were measured in human erythrocytes through which are in transit to a target site. 560 uM of 5'-IIno generated 500 uM 5-IR-1-P in human erythrocytes. Intracellular concentrations of 5-IR-1-P reached plateau levels in less than 1 hr which remained unchanged for 4 hr. Following removal of extracellular 5'-IIno, the intracellular concentrations of 5-IR-1-P decreased from 500 uM to 300 uM. Intracellular concentration of 5-IR-1-P declined progressively during the subsequent incubation, indicating that rapidly continuing degradation of 5-IR-1-P occurred in the absence of further synthesis of 5-IR-1-P from 5'-IIno.
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5 ' - Deoxy - 5 ' - Iodoinosine 존재하에 사람 적혈구에서의 5 - Iodoribose 1 - phosphate 대사
최혜선,요하나 스토클러 ( Hye Seon Choi,Johanna D . Stoeckler ) 생화학분자생물학회 1990 BMB Reports Vol.23 No.3
5`-deoxy-5`-iodoadenosine (5`-IAdo) and 5`-deoxy-5`-iodoinosine (5`-IIno) were highly cytotoxic to several cell lines in vitro. These studies indicated that the pentose 1-phosphate generated from the 5`-iodonucleosides is responsible for the cytotoxicity. The synthesized and purified 5-iodoribose 1-phosphate (5-IR-1-P) inhibited several enzymes which are related to purine, pyrimidine and sugar phosphate metabolism. Intracellular concentrations of 5-IR-1-P were measured in human erythrocytes through which are in transit to a target site. 560 uM of 5`-IIno generated 500 uM 5-IR-1-P in human erythrocytes. Intracellular concentrations of 5-IR-1-P reached plateau levels in less than 1 hr which remained unchanged for 4 hr. Following removal of extracellular 5`-IIno, the intracellular concentrations of 5-IR-1-P decreased from 500 uM to 300 uM. Intracellular concentration of 5-IR-1-P declined progressively during the subsequent incubation, indicatng that rapidly continuing degradation of 5-IR-1-P occurred in the absence of further synthesis of 5-IR-1-P from 5`-IIno.
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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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