Stabilising cysteinyl thiol oxidation and nitrosation for proteomic analysis

Abstract

Oxidation and S-nitrosylation of cysteinyl thiols (Cys-SH) to sulfenic (Cys-SOH), sulfinic (Cys-SO2H), sulfonic acids (Cys-SO3H), disulphides and S-nitrosothiols are suggested as important post-translational modifications that can activate or deactivate the function of many proteins. Non-enzymatic post-translational modifications to cysteinyl thiols have been implicated in a wide variety of physiological and pathophysiological states but have been difficult to monitor in a physiological setting because of a lack of experimental tools. The purpose of this review is to bring together the approaches that have been developed for stably trapping cysteine either in its reduced or oxidised forms for enrichment and or subsequent mass spectrometric analysis. These tools are providing insight into potential targets for post-translational modifications to cysteine modification in vivo. This article is part of a Special Issue entitled: Special Issue: Posttranslational Protein modifications in biology and Medicine.

Keywords: 3-(2,4-dioxocyclohexyl)propyl; BSO; BST; Cys-SOH; DCP; DTNB; DTT; Dimedone; GSH; GSR; GSSG; Gel electrophoresis; Grx; HNE; IAA; IAM; ICAT; IEF; N-ethyl maleimide; NEM; NO; Nitrosothiol; PEG; ROS; SMase; SNO; Sulfenic acid; Trx; TrxR; biotin switch technique; buthionine sulfoximine; cysteine sulphenic acid; dithionitrobisbenzoic acid; dithiothreitol; glutaredoxin; glutathione; glutathione disulphide; glutathione reductase; hydroxynonenal; iodoacetamide; iodoacetic acid; isoelectric focussing; isotope-coded affinity tag; nitric oxide; nitrosothiol; polyethylene glycol; reactive oxygen species; sphingomyelinase; thioredoxin; thioredoxin reductase.