在一氧化氮/超氧化物系统中，硫氧还蛋白的S-亚硝基化激活凋亡信号调节激酶1。
S-nitrosation of thioredoxin in the nitrogen monoxide/superoxide system activates apoptosis signal-regulating kinase 1.
作者信息
Yasinska Inna M, Kozhukhar Anna V, Sumbayev Vadim V
机构信息
Department of Biochemistry, Mechnikov Odessa National University, Per. Shampansky 2, Odessa 65058, Ukraine.
出版信息
Arch Biochem Biophys. 2004 Aug 15;428(2):198-203. doi: 10.1016/j.abb.2004.06.004.
In the present study, we have investigated S-nitrosation of reactive thioredoxin (Trx) thiol groups in nitric oxide/superoxide system. We have found that Trx thiol groups are the targets for S-nitrosation by N2O3-like species generated in the system containing xanthine/xanthine oxidase (superoxide producing system) and DEA/NO-the *NO donating compound, however, they have shown low sensitivity to the *NO derived from DEA/NO. N2O3-dependent S-nitrosation of Trx at approximately 2-fold of NO excess compared to the superoxide amount resulted in dissociation and activation of apoptosis signal regulating kinase 1 (ASK1). However, approximately 4-fold of NO excess compared to a superoxide production preserved the level of dissociated ASK1 but decreased its activity due to the enzyme S-nitrosation.
在本研究中，我们研究了一氧化氮/超氧化物系统中活性硫氧还蛋白（Trx）巯基的S-亚硝基化作用。我们发现，Trx巯基是由含有黄嘌呤/黄嘌呤氧化酶的系统（超氧化物产生系统）和DEA/NO（一种NO供体化合物）生成的类似N2O3的物质进行S-亚硝基化的靶标，然而，它们对DEA/NO衍生的*NO表现出低敏感性。与超氧化物量相比，在NO过量约2倍时，N2O3依赖性的Trx S-亚硝基化导致凋亡信号调节激酶1（ASK1）的解离和激活。然而，与超氧化物产生量相比，NO过量约4倍时，虽然解离的ASK1水平得以维持，但由于该酶的S-亚硝基化，其活性降低。
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