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阿西维辛与放线菌素的多酶靶向化疗

Multi-enzyme-targeted chemotherapy by acivicin and actinomycin.

作者信息

Weber G, Prajda N, Lui M S, Denton J E, Aoki T, Sebolt J, Zhen Y S, Burt M E, Faderan M A, Reardon M A

出版信息

Adv Enzyme Regul. 1982;20:75-96. doi: 10.1016/0065-2571(82)90009-7.

Abstract

On the basis of our observation of the increased specific activities of glutamine-utilizing enzymes in purine and pyrimidine metabolism in hepatoma 3924A, and because the concentration of glutamine is ten times lower in the hepatomas than in the liver, the biochemical pharmacology of the anti-glutamine agent, acivicin, was examined. (1) Acivicin competitively inhibited the activities of amidophosphoribosyl-transferase, CTP synthetase and carbamoyl-phosphate synthetase II from extracts of liver and hepatoma 3924A. (2) In addition to the competitive inhibition exerted by acivicin, evidence was obtained that this drug also irreversibly inactivated in vitro the glutamine-utilizing enzymes. It is particularly relevant for the selectivity of acivicin that the activity of aspartate carbamoyltransferase, an enzyme present in the same complex as carbamoyl-phosphate synthetase II, was not affected by the anti-glutamine agent. (3) Acivicin in vivo brought down the activities of glutamine-utilizing enzymes in a period of 10 min to 1 hr after injection. CTP synthetase activity declined to less than 10% of that observed in the uninjected rats. The decreases were not reversible by various in vitro methods, but in vivo the activities returned to normal range in 72 hr. (4) The activity of aspartate carbamoyltransferase, which exists as a multi-enzyme complex with synthetase II, was not altered by acivicin injection. Similar results were observed in transplantable sarcoma in the rat. (5) The acivicin-induced decrease in enzymic activities could not be restored by purification of the enzymes. (6) In vitro studies indicated that addition of acivicin to liver or hepatoma extracts or purified enzymes rapidly decreased enzymic activities; the activities could not be restored. These results are consistent with an interpretation that acivicin acts either as a tight-binding inhibitor or as an inactivator through alkylation of the enzymes of glutamine utilization. (7) Acivicin in combination with actinomycin provided a synergistic kill of hepatoma cells in tissue culture and also inhibited the growth of transplantable solid hepatoma 3924A in the rat. (8) The synergistic biological results of combination chemotherapy with acivicin and actinomycin can be accounted for by the action of acivicin in inhibiting GMP and CTP synthetases, resulting in a decrease in GTP and CTP content, and by the actinomycin-caused inhibition of RNA polymerase in selectively blocking the utilization of GTP and CTP.

摘要

基于我们对肝癌3924A中嘌呤和嘧啶代谢过程中谷氨酰胺利用酶比活性增加的观察,并且由于肝癌中谷氨酰胺的浓度比肝脏中低10倍,因此对谷氨酰胺拮抗剂阿西维辛的生化药理学进行了研究。(1)阿西维辛竞争性抑制肝脏和肝癌3924A提取物中的氨甲酰磷酸核糖基转移酶、CTP合成酶和氨甲酰磷酸合成酶II的活性。(2)除了阿西维辛产生的竞争性抑制作用外,还获得证据表明该药物在体外也能不可逆地使谷氨酰胺利用酶失活。对于阿西维辛的选择性而言,特别相关的是,与氨甲酰磷酸合成酶II存在于同一复合物中的天冬氨酸氨甲酰转移酶的活性不受谷氨酰胺拮抗剂的影响。(3)阿西维辛在体内注射后10分钟至1小时内降低了谷氨酰胺利用酶的活性。CTP合成酶活性降至未注射大鼠中观察到的活性的不到10%。通过各种体外方法,这些降低是不可逆的,但在体内,活性在72小时内恢复到正常范围。(4)与合成酶II以多酶复合物形式存在的天冬氨酸氨甲酰转移酶的活性,不受阿西维辛注射的影响。在大鼠可移植肉瘤中也观察到类似结果。(5)阿西维辛诱导的酶活性降低不能通过酶的纯化来恢复。(6)体外研究表明,向肝脏或肝癌提取物或纯化酶中添加阿西维辛会迅速降低酶活性;活性无法恢复。这些结果与一种解释一致,即阿西维辛要么作为紧密结合抑制剂起作用,要么通过对谷氨酰胺利用酶进行烷基化而作为失活剂起作用。(7)阿西维辛与放线菌素联合使用在组织培养中对肝癌细胞具有协同杀伤作用,并且也抑制大鼠中可移植实体肝癌3924A的生长。(8)阿西维辛与放线菌素联合化疗的协同生物学结果可以通过阿西维辛抑制GMP和CTP合成酶的作用来解释,导致GTP和CTP含量降低,以及通过放线菌素引起的RNA聚合酶抑制作用来解释,其选择性地阻断GTP和CTP的利用。

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