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Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Published on: June 21, 2021

Global approaches for protein thiol redox state detection.

Lisa R Knoke¹, Lars I Leichert¹

¹Ruhr University Bochum, Institute of Biochemistry and Pathobiochemistry, Microbial Biochemistry, Universitätsstrasse 150, 44780 Bochum, Germany.

Current Opinion in Chemical Biology

|October 5, 2023

Summary

Cysteine

Area of Science:

Biochemistry
Molecular Biology
Cellular Biology

Background:

The thiol group of cysteine is highly nucleophilic and versatile.
Cysteine residues are crucial for protein function, acting as active sites or forming disulfide bonds.
Cytosolic cysteines are usually reduced but susceptible to oxidative modifications.

Purpose of the Study:

To investigate the role of cysteine's oxidative post-translational modifications in redox regulation.
To understand how these modifications impact protein function and cellular metabolism.
To highlight the importance of studying these modifications in redox biology.

Main Methods:

Proteomic analysis of cysteine oxidative post-translational modifications.
Investigating the reversibility of these modifications in vivo.

Keywords:

Cysteine Proteomics Redox proteomics Thiol Thiol-based redox regulation

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Studying the thioredoxin and glutaredoxin systems involved in thiol redox regulation.

Main Results:

Oxidative modifications of cysteine are reversible in vivo.
These modifications are linked to localized high oxidant levels.
Thiol oxidation in regulatory proteins modulates cellular metabolism in response to oxidative stimuli.

Conclusions:

Cysteine's oxidative post-translational modifications are key to thiol-based redox regulation.
Understanding these modifications is essential for comprehending cellular responses to oxidative stress.
Proteomic studies are indispensable for advancing redox biology research.