Reduction of protein disulfide bonds in an oxidizing environment - The disulfide bridge of cholera toxin A-subunit is reduced in the endoplasmic reticulum
Reduction of protein disulfide bonds in an oxidizing environment - The disulfide bridge of cholera toxin A-subunit is reduced in the endoplasmic reticulum
复制标题
DOI：
10.1016/s0014-5793(96)01447-0
复制
发表时间：
1997-01-20
期刊：
影响因子：
3.5
通讯作者：
Soling, HD
中科院分区：
文献类型：
--
作者：
Majoul, I;Ferrari, D;Soling, HD
逆行转运至内质网 (ER) 后，霍乱毒素 (CTX-A) 的 A 亚基通过二硫键还原部分裂解为 CTX-A1 和 CTX-AZ [Majoul 等人，(1996) J. Cell Biol. [133, 777-789]，尽管 ER fa 中的氧化还原态或二硫键形成，我们在此表明 CTS-II 的二硫键在 GSH/GSSG 比例为 1 至 3 时已在体外裂解，蛋白质二硫键异构酶 (PDT) 仅发挥较小的加速作用，各种混合二硫键中间体 (CTX-A1-S-S-CTX-A1; PDI-S-S-A2；PDI-S-S-A1)在CTX-A还原过程中出现，这些结果表明在ER中蛋白质二硫键形成和蛋白质二硫键还原可以同时发生。
Following retrograde transport to the endoplasmic reticulum (ER) the A-subunit of cholera toxin (CTX-A) is partially cleaved into CTX-A1 and CTX-AZ by reduction of a disulfide bridge [Majoul et al, (1996) J. Cell Biol. 133, 777-789], although the redox state in the ER fa, ors disulfide formation, We show here that the disulfide bridge of CTS-II is cleaved in vitro already at GSH/GSSG ratios between 1 and 3, Protein disulfide isomerase (PDT) exerts only a minor accelerating effect, Various mixed disulfide intermediates (CTX-A1-S-S-CTX-A1; PDI-S-S-A2; PDI-S-S-A1) appear during CTX-A reduction, These results indicate that in the ER protein disulfide formation and protein disulfide reduction can take place simultaneously.