Day Nicholas J, Gaffrey Matthew J, Qian Wei-Jun
Pacific Northwest National Laboratory, Biological Sciences Division, Richland, WA 99352, USA.
Antioxidants (Basel). 2021 Mar 23;10(3):499. doi: 10.3390/antiox10030499.
Post-translational modifications regulate the structure and function of proteins that can result in changes to the activity of different pathways. These include modifications altering the redox state of thiol groups on protein cysteine residues, which are sensitive to oxidative environments. While mass spectrometry has advanced the identification of protein thiol modifications and expanded our knowledge of redox-sensitive pathways, the quantitative aspect of this technique is critical for the field of redox proteomics. In this review, we describe how mass spectrometry-based redox proteomics has enabled researchers to accurately quantify the stoichiometry of reversible oxidative modifications on specific cysteine residues of proteins. We will describe advancements in the methodology that allow for the absolute quantitation of thiol modifications, as well as recent reports that have implemented this approach. We will also highlight the significance and application of such measurements and why they are informative for the field of redox biology.
翻译后修饰调节蛋白质的结构和功能，这可能导致不同信号通路的活性发生变化。这些修饰包括改变蛋白质半胱氨酸残基上硫醇基团氧化还原状态的修饰，这些残基对氧化环境敏感。虽然质谱技术推动了蛋白质硫醇修饰的鉴定，并扩展了我们对氧化还原敏感信号通路的认识，但该技术的定量方面对氧化还原蛋白质组学领域至关重要。在本综述中，我们描述了基于质谱的氧化还原蛋白质组学如何使研究人员能够准确量化蛋白质特定半胱氨酸残基上可逆氧化修饰的化学计量。我们将描述该方法的进展，这些进展允许对硫醇修饰进行绝对定量，以及最近实施该方法的报告。我们还将强调此类测量的意义和应用，以及它们为何对氧化还原生物学领域具有参考价值。
