Redoxproteomisches

Redoxproteomics is a subdiscipline of proteomics that focuses on the study of the redox state of proteins within a cell or organism. This involves identifying and quantifying the reversible and irreversible modifications that occur to proteins due to reactive oxygen species (ROS) and reactive nitrogen species (RNS). These modifications, known as oxidoreductive modifications, can significantly alter protein structure, function, localization, and interactions.

The primary goal of redoxproteomics is to map the redox-sensitive cysteine residues within the proteome and to understand how these modifications impact cellular processes. Common oxidoreductive modifications include the formation of disulfide bonds, S-nitrosylation, S-glutathionylation, oxidation of methionine to methionine sulfoxide, and oxidation of tryptophan. These modifications are often transient and reversible, serving as signaling mechanisms, or they can be permanent, leading to protein inactivation or degradation.

Techniques employed in redoxproteomics typically involve enrichment strategies for modified peptides followed by mass spectrometry-based identification and quantification. Isotope-coded affinity tagging (ICAT) and other chemical labeling methods are often used to distinguish between oxidized and reduced cysteine residues. The dynamic nature of these modifications requires careful sample handling and experimental design to capture meaningful biological information.

Understanding the redox proteome is crucial for deciphering cellular signaling pathways, particularly those involving oxidative stress. Dysregulation of redox homeostasis is implicated in numerous diseases, including cancer, neurodegenerative disorders, cardiovascular diseases, and aging. Redoxproteomics provides a powerful tool for identifying biomarkers of oxidative damage and for developing targeted therapeutic strategies.