LAUSR

Redox proteomics is a field of proteomics which is concerned with the characterization of the oxidation state of proteins in order to gain information about their modulated structure, function, activity and involvement in different physiological pathways. Oxidative modifications of proteins have been shown to be implicated in normal physiological processes of cells, as well as in pathomechanisms leading to the development of cancer, diabetes, neurodegenerative diseases, and some rare hereditary metabolic diseases, like classic galactosemia. Reactive oxygen species (ROS) generate a variety of reversible and irreversible modifications of amino acid residue side chains, and within the protein backbone. These oxidative post-translational modifications (Ox-PTMs) can participate in the activation of signal transduction pathways, and mediate the toxicity of harmful oxidants. Thus, the application of advanced redox proteomics technologies is important for gaining insights into molecular mechanisms of diseases. Mass spectrometry (MS) based proteomics is one of the most powerful methods that can be used to give detailed qualitative and quantitative information on protein modifications and allows to characterize redox proteomes associated with diseases. The current review illustrates the role and biological consequences of Ox- PTMs under basal and oxidative stress (OS) conditions by focussing on protein carbonylation and S-glutathionylation, two abundant modifications with impact on cellular pathways that were intensively studied during the last decade.