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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October 2011
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Conference Article|
September 21 2011
Redox signalling via the cellular thiolstat
Claus Jacob
Claus Jacob
1
1Division of Bioorganic Chemistry, School of Pharmacy, Saarland University, Campus, D-66123 Saarbrücken, Germany
1email c.jacob@mx.uni-saarland.de
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Publisher: Portland Press Ltd
Received:
June 15 2011
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2011 Biochemical Society
2011
Biochem Soc Trans (2011) 39 (5): 1247–1253.
Article history
Received:
June 15 2011
Citation
Claus Jacob; Redox signalling via the cellular thiolstat. Biochem Soc Trans 1 October 2011; 39 (5): 1247–1253. doi: https://doi.org/10.1042/BST0391247
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