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Updated: May 12, 2025

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
Published on: June 21, 2021
Cysteine-based redox sensors in the cardiovascular system: from identification to physiology and drug discovery
Joseph R Burgoyne1, Philip Eaton2
1The British Heart Foundation Centre of Excellence, The Rayne Institute, St Thomas' Hospital, King's College London, London, United Kingdom.
Abstract:
Cysteine residues are uniquely equipped to sense redox signals because of the reactivity of their thiol side chains, which can undergo oxidation to form various modifications. By sensing changes within the intracellular redox environment, reactive cysteine thiols add a distinct shape and a charge characteristic that can induce protein conformational changes, ultimately triggering specific effector responses that alter cellular and tissue function. Redox sensing is essential within the cardiovascular system, where it regulates both cardiac and vascular function and significantly influences disease progression. This review provides a brief introduction to cysteine thiol redox sensors, outlines methodologies for their detection, and explores their roles in the cardiovascular system. Also discussed are recent advancements in identifying cysteine-targeted therapies and a proposal for a redefined perspective on the role of redox biology within the cardiovascular system.
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