Redox balance plays an important role in the regulation of cellular physiology via orchestrated action of electron donors/acceptors, reactive oxygen and nitrogen species (RONS) and antioxidant defence mechanisms. Recently postulated hypothesis of "redox switches" via ROS-induced protein post-translational modifications (PTMs) acknowledge its importance in cellular signaling events. Importantly, impairment of redox homeostasis is a crucial factor in the development of numerous human pathologies including metabolic and cardiovascular diseases. However, the role of redox regulated modifications and PTM cross-talk is poorly investigated, mostly due to the analytical challenges in their high-throughput detection and quantification. Using state-of-the-art bioanalytical methods, a detailed investigation of different lipid and protein PTMs was performed using dynamic cardiomyocyte model of nitroxidative stress. Fluorescent microscopy revealed significant alterations in subcellular distribution of main cytoskeletal proteins – actin, vimentin and tubulin. Using in-depth proteomics approach over 35 different post-translational modifications were mapped and relatively quantified for cytoskeletal proteins. This allowed to identify “hot spots”, like the single cysteine residue of vimentin, which might play an important role in PTM cross-talk and thus take part in redox regulation.

1 p. OCC World Congress and Annual SFRR-E Conference 2017 Metabolic Stress and Redox Regulation Berlin, Germany 21-23 June 2017

Funding was provided by SAF2015-68590-R from MINEICO (Spain) /FEDER and EU project 675132 (MASSTRPLAN) H2020-MSCA-ITN-2015

Peer reviewed