Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 39, Issue -, Pages 1247-1253Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST0391247
Keywords
cysteine; oxidative stress; redox signalling; S-thiolation; thiolstat
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Funding
- University of Saarland
- Ministry of Economics and Science of Saarland
- Deutsche Forschungsgemeinschaft (DFG) [JA1741/2-1]
- European Community [215009]
- Corena Interreg IVa Programme
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Research conducted during the last two decades has provided evidence for the existence of an extensive intracellular redox signalling, control and feedback network based on different cysteine-containing proteins and enzymes. Together, these proteins enable the living cell to sense and respond towards external and internal redox changes in a measured, gradual, appropriate and mostly reversible manner. The (bio)chemical basis of this regulatory 'thiolstat' is provided by the complex redox chemistry of the amino acid cysteine, which occurs in vivo in various sulfur chemotypes and is able to participate in different redox processes. Although our knowledge of the biological redox behaviour of sulfur (i.e. cysteine or methionine) is expanding, numerous questions still remain. Future research will need to focus on the individual proteins involved in this redox system, their particular properties and specific roles in cellular defence and survival. Once it is more fully understood, the cellular thiolstat and its individual components are likely to form prominent targets for drug design.
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