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  Dynamic rerouting of the carbohydrate flux is key to counteracting oxidative stress

Ralser, M., Wamelink, M. M., Kowald, A., Gerisch, B., Heeren, G., Struys, E. A., et al. (2007). Dynamic rerouting of the carbohydrate flux is key to counteracting oxidative stress. Journal of Biology, 6(4), 10-10. doi:10.1186/jbiol61.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-82DC-F Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-82DD-D
Genre: Journal Article
Alternative Title : J Biol

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 Creators:
Ralser, Markus1, Author              
Wamelink, Mirjam M., Author
Kowald, Axel2, Author              
Gerisch, Birgit3, Author              
Heeren, Gino, Author
Struys, Eduard A., Author
Klipp, Edda2, Author              
Jakobs, Cornelis, Author
Breitenbach, Michael, Author
Lehrach, Hans1, Author              
Krobitsch, Sylvia4, Author              
Affiliations:
1Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433550              
2Independent Junior Research Groups (OWL), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433554              
3Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433558              
4Neurodegenerative Disorders (Sylvia Krobitsch), Independent Junior Research Groups (OWL), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479661              

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 Abstract: Background Eukaryotic cells have evolved various response mechanisms to counteract the deleterious consequences of oxidative stress. Among these processes, metabolic alterations seem to play an important role. Results We recently discovered that yeast cells with reduced activity of the key glycolytic enzyme triosephosphate isomerase exhibit an increased resistance to the thiol-oxidizing reagent diamide. Here we show that this phenotype is conserved in Caenorhabditis elegans and that the underlying mechanism is based on a redirection of the metabolic flux from glycolysis to the pentose phosphate pathway, altering the redox equilibrium of the cytoplasmic NADP(H) pool. Remarkably, another key glycolytic enzyme, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), is known to be inactivated in response to various oxidant treatments, and we show that this provokes a similar redirection of the metabolic flux. Conclusion The naturally occurring inactivation of GAPDH functions as a metabolic switch for rerouting the carbohydrate flux to counteract oxidative stress. As a consequence, altering the homoeostasis of cytoplasmic metabolites is a fundamental mechanism for balancing the redox state of eukaryotic cells under stress conditions.

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Language(s): eng - English
 Dates: 2007
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 336973
DOI: 10.1186/jbiol61
URI: http://jbiol.com/content/pdf/jbiol61.pdf
 Degree: -

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Title: Journal of Biology
  Alternative Title : J Biol
Source Genre: Journal
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Pages: - Volume / Issue: 6 (4) Sequence Number: - Start / End Page: 10 - 10 Identifier: ISSN: 1475-4924