Modification of tryptophan and tryptophan residues in proteins by reactive nitrogen species
Modification of tryptophan and tryptophan residues in proteins by reactive nitrogen species
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DOI：
10.1016/j.niox.2005.07.009
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发表时间：
2006-03-01
影响因子：
3.9
通讯作者：
Ikeda, K
中科院分区：
文献类型：
--
作者：
Yamakura, F;Ikeda, K
通过活性氮物质（RNS）与蛋白质中的酪氨酸残基之间的反应形成3-硝基酪氨酸已被广泛分析，并且其被广泛用作由RNS介导的病理生理和生理条件的生物标志物。相反，关于色氨酸硝化的研究报道很少。本文综述了RNS修饰色氨酸的研究进展，并指出了RNS修饰色氨酸在病理生理学和生理学方面的重要性。游离色氨酸可以通过与各种RNS反应而被修饰成几种硝化产物（1-、4-、5-、6-和7-）、I-AT-亚硝基产物和几种氧化产物，这取决于所用的条件。其中，1-N-亚硝基色氨酸和6-硝基色氨酸（6-NO（2）Trp）是与过氧亚硝酸根反应的丰富产物，而6-NO（2）Trp是与过氧化物酶/过氧化氢/亚硝酸根反应的最丰富产物。6-NO（2）Trp也被观察到是人Cu，Zn-超氧化物歧化酶和牛血清白蛋白中过氧亚硝酸根或髓过氧化物酶/过氧化氢/亚硝酸根与色氨酸残基反应以及过氧亚硝酸根与肌红蛋白和血红蛋白反应的最丰富的硝化产物。修饰后的Cu，Zn-SOD中还发现了几种氧化产物。然而，在与过氧亚硝酸盐或髓过氧化物酶/H2 O2/亚硝酸盐系统反应的蛋白质中没有观察到1-N-亚硝基色氨酸和1-N-硝基色氨酸。蛋白质中色氨酸残基的修饰可能发生在体内比酪氨酸残基更有限数量的位点，因为色氨酸残基通常更多地埋在蛋白质中并且不太频繁地存在于蛋白质中。然而，表面暴露的色氨酸残基倾向于参与与其他分子的相互作用，因此这些色氨酸残基的修饰可能导致调节蛋白质和酶与其他分子的特异性相互作用。(c)2005年爱思唯尔公司All rights reserved.
Formation of 3-nitrotyrosine by the reaction between reactive nitrogen species (RNS) and tyrosine residues in proteins has been analyzed extensively and it is used widely as a biomarker of pathophysiological and physiological conditions mediated by RNS. In contrast, few studies on the nitration of tryptophan have been reported. This review provides an overview of the studies on tryptophan modifications by RNS and points out the possible importance of its modification in pathophysiological and physiological conditions. Free tryptophan can be modified to several nitrated products (1-, 4-, 5-, 6-, and 7-), I-AT-nitroso product, and several oxidized products by reaction with various RNS, depending on the conditions used. Among them, 1-N-nitrosotryptophan and 6-nitrotryptophan (6-NO(2)Trp) have been found as the abundant products in the reaction with peroxynitrite, and 6-NO(2)Trp has been the most abundant product in the reaction with the peroxidase/hydrogen peroxide/nitrite systems. 6-NO(2)Trp has also been observed as the most abundant nitrated product of the reactions between peroxynitrite or myeloperoxidase/hydrogen peroxide/nitrite and tryptophan residues both in human Cu,Zn-superoxide dismutase and in bovine serum albumin, as well as the reaction of peroxynitrite with myoglobin and hemoglobin. Several oxidized products have also been identified in the modified Cu,Zn-SOD. However, no 1-N-nitrosotryptophan and 1-N-nitrotryptophan has been observed in the proteins reacted with peroxynitrite or the myeloperoxidase/H2O2/nitrite system. The modification of tryptophan residues in proteins may occur at a more limited number of sites in vivo than that of tyrosine residues, since tryptophan residues are more buried inside proteins and exist less frequently in proteins, generally. However, surface-exposed tryptophan residues tend to participate in the interaction with the other molecules, therefore the modification of those tryptophans may result in modulation of the specific interaction of proteins and enzymes with other molecules. (c) 2005 Elsevier Inc. All rights reserved.