Proteome-wide analysis of cysteine oxidation reveals metabolic sensitivity to redox stress

摘要: Reactive oxygen species (ROS) are increasingly recognised as important signalling molecules through oxidation of protein cysteine residues. Comprehensive identification redox-regulated proteins and pathways is crucial to understand ROS-mediated events. Here, we present stable isotope labelling with iodoacetamide (SICyLIA), a mass spectrometry-based workflow assess proteome-scale oxidation. SICyLIA does not require enrichment steps achieves unbiased proteome-wide sensitivity. Applying diverse cellular models primary tissues provides detailed insights into thiol proteomes. Our results demonstrate that acute chronic oxidative stress causes distinct metabolic proteins, indicating plays key role in the adaptation redox stress. Analysis mouse kidneys identifies circulating biofluids, which can affect whole-body physiology. Obtaining accurate peptide profiles from complex organs using holds promise for future analysis patient-derived samples study human pathologies.