Biological selectivity and functional aspects of protein tyrosine nitration
Biological selectivity and functional aspects of protein tyrosine nitration
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DOI：
10.1016/s0006-291x(03)00814-3
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发表时间：
2003-06-06
影响因子：
3.1
通讯作者：
Ischiropoulos, H
中科院分区：
文献类型：
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作者：
Ischiropoulos, H
一氧化氮在生物系统中的形成导致了许多翻译后蛋白质修饰的发现，这些修饰可以调节蛋白质功能或潜在地用作一氧化氮信号传导的换能器。一氧化氮介导的蛋白质修饰的主要内容包括：一氧化氮-铁血红素结合、还原性半胱氨酸残基的S-亚硝基化以及酪氨酸和色氨酸残基的C-硝化。除了一氧化氮与血红素铁蛋白结合外，其他两种修饰似乎需要一氧化氮的二次反应和氮氧化物的形成。分析和免疫学方法的快速发展已经允许在体内定量S-亚硝基化和C-硝化的蛋白质，揭示了修饰的蛋白质的明显选择性和特异性。这篇评论主要集中在酪氨酸残基的硝化讨论参数，可能会在体内蛋白质硝化的选择性，和潜在的生物学意义和临床意义，这种一氧化氮介导的蛋白质修饰。(C)2003 Elsevier Science（美国）。All rights reserved.
The formation of nitric oxide in biological systems has led to the discovery of a number of post-translational protein modifications that could regulate protein function or potentially be utilized as transducers of nitric oxide signaling. Principal among the nitric oxide-mediated protein modifications are: the nitric oxide-iron heme binding, the S-nitrosylation of reduced cysteine residues, and the C-nitration of tyrosine and tryptophan residues. With the exception of the nitric oxide binding to heme iron proteins, the other two modifications appear to require secondary reactions of nitric oxide and the formation of nitrogen oxides. The rapid development of analytical and immunological methodologies has allowed for the quantification of S-nitrosylated and C-nitrated proteins in vivo revealing an apparent selectivity and specificity of the proteins modified. This review is primarily focused upon the nitration of tyrosine residues discussing parameters that may govern the in vivo selectivity of protein nitration, and the potential biological significance and clinical relevance of this nitric oxide-mediated protein modification. (C) 2003 Elsevier Science (USA). All rights reserved.