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测量线粒体蛋白硫醇氧化还原状态。

Measuring mitochondrial protein thiol redox state.

作者信息

Requejo Raquel, Chouchani Edward T, Hurd Thomas R, Menger Katja E, Hampton Mark B, Murphy Michael P

机构信息

Medical Research Council Mitochondrial Biology Unit, Wellcome Trust/MRC Building, Cambridge, UK.

出版信息

Methods Enzymol. 2010;474:123-47. doi: 10.1016/S0076-6879(10)74008-8. Epub 2010 Jun 20.

DOI:10.1016/S0076-6879(10)74008-8
PMID:20609908
Abstract

Protein thiols are an important component of mammalian intramitochondrial antioxidant defenses owing to their selective interaction with reactive oxygen and nitrogen species (ROS and RNS). Reversible modifications of protein thiols resulting from these interactions are also an important aspect of redox signal transduction. Therefore, to assess how mitochondria respond to oxidative stress and act as nodes in redox signaling pathways, it is important to measure general changes to protein thiol redox states and also to identify the specific mitochondrial thiol proteins involved. Here we outline some of the approaches that can be used to accomplish these goals and thereby infer the multiple roles of mammalian mitochondrial protein thiols in antioxidant defense and redox signaling.

摘要

蛋白质硫醇是哺乳动物线粒体内抗氧化防御的重要组成部分,因为它们能与活性氧和氮物种(ROS和RNS)发生选择性相互作用。这些相互作用导致的蛋白质硫醇的可逆修饰也是氧化还原信号转导的一个重要方面。因此,为了评估线粒体如何应对氧化应激并作为氧化还原信号通路中的节点发挥作用,测量蛋白质硫醇氧化还原状态的总体变化以及识别所涉及的特定线粒体硫醇蛋白非常重要。在这里,我们概述了一些可用于实现这些目标的方法,从而推断哺乳动物线粒体蛋白质硫醇在抗氧化防御和氧化还原信号转导中的多种作用。

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