Protein tyrosine nitration in cellular signal transduction pathways

被引：43

作者：

Yakovlev, Vasily A. ^{[1
]}

Mikkelsen, Ross B. ^{[1
]}

机构：

[1] Virginia Commonwealth Univ, Massey Canc Ctr, Dept Radiat Oncol, Richmond, VA 23284 USA

来源：

JOURNAL OF RECEPTORS AND SIGNAL TRANSDUCTION | 2010年 / 30卷 / 06期

基金：

美国国家卫生研究院;

关键词：

Nitric oxide; tyrosine nitration; peroxynitrite; superoxide; uncoupling; NITRIC-OXIDE SYNTHASE; MITOCHONDRIAL PERMEABILITY TRANSITION; GROWTH-FACTOR RECEPTOR; COLON-CANCER CELLS; S-NITROSYLATION; REACTIVE OXYGEN; IONIZING-RADIATION; PROTEOMIC ANALYSIS; OXIDATIVE STRESS; PHOSPHORYLASE-B;

D O I：

10.3109/10799893.2010.513991

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

How specificity and reversibility in tyrosine nitration are defined biologically in cellular systems is poorly understood. As more investigations identify proteins involved in cell regulatory pathways in which only a small fraction of that protein pool is modified by nitration to affect cell function, the mechanisms of biological specificity and reversal should come into focus. In this review experimental evidence has been summarized to suggest that tyrosine nitration is a highly selective modification and under certain physiological conditions fulfills the criteria of a physiologically relevant signal. It can be specific, reversible, occurs on a physiological time scale, and, depending on a target, can result in either activation or inhibition.

引用

页码：420 / 429

页数：10

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