方法检测蛋白谷胱甘肽化

Robyn L. Poerschke, Kristofer S. Fritz, Christopher C. Franklin
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引用次数: 3

摘要

谷胱甘肽酰化是一种翻译后修饰,可在谷胱甘肽和蛋白质半胱氨酸残基的巯基之间形成混合二硫。蛋白质的谷胱甘肽化通过非酶机制发生,包括硫醇/二硫交换和酶介导的反应。蛋白质谷胱甘肽化在氧化或亚硝化应激反应中被观察到,并且是氧化还原依赖的,在还原条件下容易可逆。这些发现表明谷胱甘肽化在介导氧化还原敏感信号传导中起重要作用。实际上,谷胱甘肽化可以通过改变活性、蛋白-蛋白相互作用和配体结合来影响蛋白质功能。谷胱甘肽化还可以防止半胱氨酸残基发生不可逆的氧化修饰。因此,确定一个给定的蛋白质成为谷胱甘肽化的能力可以提供洞察其氧化还原调节和在决定细胞对氧化和亚硝化应激反应的假定作用。描述了免疫印迹法和质谱法测定蛋白谷胱甘肽化的方法。咕咕叫。Protoc。Toxicol 57:6.17.1-6.17.18。©2013 by John Wiley &儿子,Inc。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Methods to Detect Protein Glutathionylation

Glutathionylation is a posttranslational modification that results in the formation of a mixed disulfide between glutathione and the thiol group of a protein cysteine residue. Glutathionylation of proteins occurs via both nonenzymatic mechanisms involving thiol/disulfide exchange and enzyme-mediated reactions. Protein glutathionylation is observed in response to oxidative or nitrosative stress and is redox-dependent, being readily reversible under reducing conditions. Such findings suggest that glutathionylation plays an important role in mediating redox-sensitive signaling. Indeed, glutathionylation can affect protein function by altering activity, protein-protein interactions, and ligand binding. Glutathionylation may also serve to prevent cysteine residues from undergoing irreversible oxidative modification. Thus, determining the ability of a given protein to become glutathionylated can provide insight into its redox regulation and putative role in dictating cellular response to oxidative and nitrosative stress. Methods to measure protein glutathionylation using immunoblotting and mass spectrometry are described. Curr. Protoc. Toxicol. 57:6.17.1-6.17.18. © 2013 by John Wiley & Sons, Inc.

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