Peer-Reviewed Journal Details
Mandatory Fields
McDonagh, B
2017
July
Frontiers in physiology
Detection of ROS Induced Proteomic Signatures by Mass Spectrometry
Published
Altmetric: 10WOS: 6 ()
Optional Fields
TYROSINE-PHOSPHATASE 1B PROTEIN S-NITROSYLATION SULFENIC ACID FORMATION ACTIVE-SITE CYSTEINE OXIDATIVE STRESS REDOX REGULATION IN-VIVO NITRIC-OXIDE DISEASE CARBONYLATION
8
Reversible and irreversible post-translational modifications ( PTMs) induced by endogenously generated reactive oxygen species (ROS) in regulatory enzymes and proteins plays an essential role in cellular signaling. Almost all cellular processes including metabolism, transcription, translation and degradation have been identified as containing redox regulated proteins. Specific redox modifications of key amino acids generated by ROS offers a dynamic and versatile means to rapidly alter the activity or functional structure of proteins in response to biochemical, environmental, genetic and pathological perturbations. How the proteome responds to these stimuli is of critical importance in oxidant physiology, as it can regulate the cell stress response by reversible and irreversible PTMs, affecting protein activity and protein-protein interactions. Due to the highly labile nature of many ROS species, applying redox proteomics can provide a signature footprint of the ROS species generated. Ideally redox proteomic approaches would allow; (1) the identification of the specific PTM, (2) identification of the amino acid residue that is modified and (3) the percentage of the protein containing the PTM. New developments in MS offer the opportunity of a more sensitive targeted proteomic approach and retrospective data analysis. Subsequent bioinformatics analysis can provide an insight into the biochemical and physiological pathways or cell signaling cascades that are affected by ROS generation. This mini-review will detail current redox proteomic approaches to identify and quantify ROS induced PTMs and the subsequent effects on cellular signaling.
1664-042X
10.3389/fphys.2017.00470
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