Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 39, Issue -, Pages 1260-1267Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST0391260
Keywords
alkylating agent; dibromobimane (DBB); glutaredoxin (Grx); mass spectrometry; thiol oxidation; thioredoxin (Trx)
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Funding
- Medical Research Council
- British Heart Foundation
- Leducq Foundation
- Department of Health via the National Institute of Health Research cBRC (Comprehensive Biomedical Research Centre)
- Wellcome Trust
- British Heart Foundation [PG/10/98/28655] Funding Source: researchfish
- Medical Research Council [G0700320, G0600785] Funding Source: researchfish
- MRC [G0600785, G0700320] Funding Source: UKRI
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Elevated protein oxidation is a widely reported hallmark of most major diseases. Historically, this 'oxidative stress' has been considered causatively detrimental, as the protein oxidation events were interpreted simply as damage. However, recent advances have changed this antiquated view; sensitive methodology for detecting and identifying proteins susceptible to oxidation has revealed a fundamental role for this modification in physiological cell signalling during health. Reversible protein oxidation that is dynamically coupled with cellular reducing systems allows oxidative protein modifications to regulate protein function, analogous to phosphoregulation. However, the relatively labile nature of many reversible protein oxidation states hampers the reliable detection and identification of modified proteins. Consequently, specialized methods to stabilize protein oxidation in combination with techniques to detect specific types of modification have been developed. Here, these techniques are discussed, and their sensitivity, selectivity and ability to reliably identify reversibly oxidized proteins are critically assessed.
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