Redox proteomics: from bench to bedside

Area of Science:

• Proteomics
• Biochemistry
• Molecular Biology

Background:

• Protein posttranslational modifications (PTMs) are essential for protein function.
• Oxidative posttranslational modifications (oxPTMs) specifically involve changes due to reactive oxygen and nitrogen species.
• Cysteine residues are key targets for reversible oxPTMs, playing a regulatory role.

Purpose of the Study:

• To provide a comprehensive investigation of oxPTMs, with a focus on cysteine oxidation.
• To highlight the significance of redox proteomics in understanding cellular processes.
• To discuss the available techniques for studying oxPTMs.

Main Methods:

• Utilizing diverse technical approaches for comprehensive investigation of oxPTMs.
• Employing gel-based and non-gel-based separation techniques.
• Combining separation with advanced detection, identification, and quantification methods.

Main Results:

• Cysteine oxidation is a significant type of oxPTM, often occurring at functional protein sites.
• Oxidative stress, mediated by ROS and RNS, influences protein function through oxPTMs.
• Reversible cysteine oxidations suggest a potential protein regulatory mechanism.

Conclusions:

• Redox proteomics is critical for mapping oxidative damage and protein modulation.
• Identifying and localizing oxPTMs is vital for understanding redox regulation in health and disease.
• Studying oxPTMs aids in developing strategies for preventing and treating oxidative stress-related diseases.