A simple isotopic labeling method to study cysteine oxidation in Alzheimer's disease: oxidized cysteine-selective dimethylation (OxcysDML)

Analytical and Bioanalytical Chemistry
Liqing Gu, Renã A S Robinson

Abstract

Cysteine is widely involved in redox signaling pathways through a number of reversible and irreversible modifications. Reversible modifications (e.g., S-glutathionylation, S-nitrosylation, disulfide bonds, and sulfenic acid) are used to protect proteins from oxidative attack and maintain cellular homeostasis, while irreversible oxidations (e.g., sulfinic acid and sulfonic acid) serve as hallmarks of oxidative stress. Proteomic analysis of cysteine-enriched peptides coupled with reduction of oxidized thiols can be used to measure the oxidation states of cysteine, which is helpful for elucidating the role that oxidative stress plays in biology and disease. As an extension of our previously reported cysDML method, we have developed oxidized cysteine-selective dimethylation (OxcysDML), to investigate the site-specific total oxidation of cysteine residues in biologically relevant samples. OxcysDML employs (1) blocking of free thiols by a cysteine-reactive reagent, (2) enrichment of peptides containing reversibly oxidized cysteine by a solid phase resin, and (3) isotopic labeling of peptide amino groups to quantify cysteine modifications arising from different biological conditions. On-resin enrichment and labeling minimizes sample h...Continue Reading

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Citations

Apr 21, 2020·Biochemical Society Transactions·Loes van Dam, Tobias B Dansen
Mar 3, 2020·Rapid Communications in Mass Spectrometry : RCM·Grace Kouakou AhuieKlaus Klarskov
May 28, 2020·Frontiers in Oncology·Boutaina DaherJacques Pouysségur
Sep 27, 2016·Proteomics. Clinical Applications·Liqing Gu, Renã A S Robinson

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