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Journal Article

Pronounced alterations of cellular Metabolism and structure due to hyper- or hypo-osmosis

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Nolden,  Tobias
Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons50203

Himmelbauer,  Heinz
Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Citation

Mao, L., Hartl, D., Nolden, T., Koppelstätter, A., Klose, J., Himmelbauer, H., et al. (2008). Pronounced alterations of cellular Metabolism and structure due to hyper- or hypo-osmosis. Journal of Proteome Research, 7(9), 3968-3983. doi:10.1021/pr800245x.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-7F24-2
Abstract
Cell volume alteration represents an important factor contributing to the pathology of late-onset diseases. Previously, it was reported that protein biosynthesis and degradation are inversely (trans) regulated during cell volume regulation. Upon cell shrinkage, protein biosynthesis was up-regulated and protein degradation down-regulated. Cell swelling showed opposite regulation. Recent evidence suggests a decrease of protein biodegradation activity in many neurodegenerative diseases and even during aging; both also show prominent cell shrinkage. To clarify the effect of cell volume regulation on the overall protein turnover dynamics, we investigated mouse embryonic stem cells under hyper- and hypotonic osmotic conditions using a 2-D gel based proteomics approach. These conditions cause cell swelling and shrinkage, respectively. Our results demonstrate that the adaption to altered osmotic conditions and therefore cell volume alterations affects a broad spectrum of cellular pathways, including stress response, cytoskeleton remodeling and importantly, cellular metabolism and protein degradation. Interestingly, protein synthesis and degradation appears to be cis-regulated (same direction) on a global level. Our findings also support the hypothesis that protein alterations due to osmotic stress contribute to the pathology of neurodegenerative diseases due to a 60% expression overlap with proteins found altered in Alzheimer’s, Huntington’s, or Parkinson’s disease. Eighteen percent of the proteins altered are even shared with all three disorders.