The transport of oxidized glutathione from human erythrocytes.
The transport of oxidized glutathione from human erythrocytes.
复制标题
人红细胞氧化型谷胱甘肽的转运。
DOI：
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发表时间：
1969
影响因子：
4.8
通讯作者：
E. Beutler
中科院分区：
文献类型：
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作者：
S. Srivastava;E. Beutler
用H2 O2扩散或苯偶氮甲酸甲酯处理正常和葡萄糖-6-磷酸脱氢酶缺陷的人红细胞，使其还原型谷胱甘肽氧化。当正常细胞在不存在葡萄糖的情况下孵育时，或当葡萄糖-6-磷酸脱氢酶缺陷细胞在不存在或存在葡萄糖的情况下孵育时，由此形成的氧化型谷胱甘肽的一部分从红细胞中消失，并且可以从培养基中回收。GSSG的运动是严格单向的：当正常红细胞在含有高浓度添加的GSSG的培养基中孵育时，没有GSSG进入红细胞，因此培养基中GSSG与RBC中GSSG的比例约为600。发现GSSG从红细胞的转运速率在4小时内近似呈线性，甚至可以逆着浓度梯度进行。GSSG的运输几乎完全停止耗尽内源性高能量化合物，如ATP通过预孵育红细胞在无葡萄糖培养基中8小时或通过存在0.1 M氟化物在孵育介质中。GSSG从红细胞的转运率也被发现是显着的温度敏感性。GSSG从红细胞中的主动转运可以解释在葡萄糖-6-磷酸脱氢酶缺陷的红细胞中观察到的低水平的总谷胱甘肽和红细胞内谷胱甘肽的命运，其具有2至3天的正常半衰期。它可能作为一种防御机制，对抑制细胞内酶的高水平GSSG。
Abstract The reduced glutathione of normal and glucose-6-P dehydrogenase-deficient human erythrocytes was oxidized by subjecting the cells to H2O2 diffusion or to treatment with methyl phenylazoformate. A portion of the oxidized glutathione thus formed disappeared from the erythrocytes and could be recovered from the medium when the normal cells were incubated in the absence of glucose or when glucose-6-P dehydrogenase-deficient cells were incubated in the absence or the presence of glucose. The movement of GSSG was strictly unidirectional: no GSSG entered the red cell when the normal red cells were incubated in a medium containing a high concentration of added GSSG, so that the ratio of GSSG in the medium to GSSG in the RBC was approximately 600. The rate of GSSG transport from the red cells was found to be approximately linear over a period of 4 hours and could proceed even against a concentration gradient. The transport of GSSG was halted almost entirely by exhausting endogenous high energy compounds such as ATP by preliminary incubation of red cells in a glucose-free medium for 8 hours or by the presence of 0.1 m fluoride in the incubation medium. The rate of GSSG transport from red cells was also found to be markedly temperature-sensitive. Active transport of GSSG from red cells may explain the low levels of total glutathione observed in glucose-6-P dehydrogenase-deficient erythrocytes and the fate of intraerythrocytic glutathione, which has a normal half-life of 2 to 3 days. It may serve as a defense mechanism against inhibition of intracellular enzymes by high levels of GSSG.