Open AccessCharacterization of cellular oxidative stress response by stoichiometric redox proteomics
Author(s) -
Tong Zhang,
Matthew J. Gaffrey,
Xiaolu Li,
Weijun Qian
Publication year - 2021
Publication title -
american journal of physiology. cell physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.432
H-Index - 181
eISSN - 1522-1563
pISSN - 0363-6143
DOI - 10.1152/ajpcell.00040.2020
Subject(s) - proteomics , redox , chemistry , proteome , oxidative stress , cysteine , thiol , s nitrosylation , nitrosylation , posttranslational modification , oxidative phosphorylation , biochemistry , quantitative proteomics , biophysics , biology , enzyme , organic chemistry , nitric oxide , gene
The thiol redox proteome refers to all proteins whose cysteine thiols are subjected to various redox-dependent posttranslational modifications (PTMs) including S- glutathionylation (SSG), S- nitrosylation (SNO), S- sulfenylation (SOH), and S- sulfhydration (SSH). These modifications can impact various aspects of protein function such as activity, binding, conformation, localization, and interactions with other molecules. To identify novel redox proteins in signaling and regulation, it is highly desirable to have robust redox proteomics methods that can provide global, site-specific, and stoichiometric quantification of redox PTMs. Mass spectrometry (MS)-based redox proteomics has emerged as the primary platform for broad characterization of thiol PTMs in cells and tissues. Herein, we review recent advances in MS-based redox proteomics approaches for quantitative profiling of redox PTMs at physiological or oxidative stress conditions and highlight some recent applications. Considering the relative maturity of available methods, emphasis will be on two types of modifications: 1 ) total oxidation (i.e., all reversible thiol modifications), the level of which represents the overall redox state, and 2 ) S- glutathionylation, a major form of reversible thiol oxidation. We also discuss the significance of stoichiometric measurements of thiol PTMs as well as future perspectives toward a better understanding of cellular redox regulatory networks in cells and tissues.