dc.identifier.uri |
http://dx.doi.org/10.15488/48 |
|
dc.identifier.uri |
http://www.repo.uni-hannover.de/handle/123456789/66 |
|
dc.contributor.author |
Hildebrandt, Tatjana M.
|
|
dc.contributor.author |
Di Meo, Ivano
|
|
dc.contributor.author |
Zeviani, Massimo
|
|
dc.contributor.author |
Viscomi, Carlo
|
|
dc.contributor.author |
Braun, Hans-Peter
|
|
dc.date.accessioned |
2015-10-02T15:52:05Z |
|
dc.date.available |
2015-10-02T15:52:05Z |
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dc.date.issued |
2013 |
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dc.identifier.citation |
Hildebrandt, Tatjana M.; Di Meo, Ivano; Zeviani, Massimo; Viscomi, Carlo; Braun, Hans-Peter: Proteome adaptations in Ethe1-deficient mice indicate a role in lipid catabolism and cytoskeleton organization via post-translational protein modifications. In: Bioscience Report 33 (2013), Nr. 4, S. 575-584. DOI: http://dx.doi.org/10.1042/BSR20130051 |
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dc.description.abstract |
Hydrogen sulfide is a physiologically relevant signalling molecule. However, circulating levels of this highly biologically active substance have to be maintained within tightly controlled limits in order to avoid toxic side effects. In patients suffering from EE (ethylmalonic encephalopathy), a block in sulfide oxidation at the level of the SDO (sulfur dioxygenase) ETHE1 leads to severe dysfunctions in microcirculation and cellular energy metabolism. We used an Ethe1-deficient mouse model to investigate the effect of increased sulfide and persulfide concentrations on liver, kidney, muscle and brain proteomes. Major disturbances in post-translational protein modifications indicate that the mitochondrial sulfide oxidation pathway could have a crucial function during sulfide signalling most probably via the regulation of cysteine S-modifications. Our results confirm the involvement of sulfide in redox regulation and cytoskeleton dynamics. In addition, they suggest that sulfide signalling specifically regulates mitochondrial catabolism of FAs (fatty acids) and BCAAs (branched-chain amino acids). These findings are particularly relevant in the context of EE since they may explain major symptoms of the disease. |
eng |
dc.description.sponsorship |
DFG/HI 1471/1-1 |
|
dc.description.sponsorship |
Telethon grant/GPP10005 and AFM15927 |
|
dc.description.sponsorship |
Pierfranco and Luisa Mariani Foundation Italy |
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dc.language.iso |
eng |
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dc.publisher |
London : Portland Press LTD |
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dc.relation.ispartofseries |
Bioscience Report 33 (2013), Nr. 4 |
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dc.rights |
CC BY 3.0 Unported |
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dc.rights.uri |
http://creativecommons.org/licenses/by/3.0/ |
|
dc.subject |
branched-chain amino acid oxidation |
eng |
dc.subject |
ethylmalonic encephalopathy |
eng |
dc.subject |
hydrogen sulfide |
eng |
dc.subject |
mitochondria |
eng |
dc.subject |
redox regulation |
eng |
dc.subject |
sulfur dioxygenase |
eng |
dc.subject.ddc |
580 | Pflanzen (Botanik)
|
|
dc.title |
Proteome adaptations in Ethe1-deficient mice indicate a role in lipid catabolism and cytoskeleton organization via post-translational protein modifications |
eng |
dc.type |
Article |
|
dc.type |
Text |
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dc.relation.issn |
0144-8463 |
|
dc.relation.doi |
10.1042/BSR20130051 |
|
dc.bibliographicCitation.firstPage |
575 |
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dc.bibliographicCitation.lastPage |
584 |
|
dc.description.version |
publishedVersion |
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tib.accessRights |
frei zug�nglich |
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