pubmed-article:18221415 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18221415 | lifeskim:mentions | umls-concept:C2613152 | lld:lifeskim |
pubmed-article:18221415 | lifeskim:mentions | umls-concept:C0162610 | lld:lifeskim |
pubmed-article:18221415 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
pubmed-article:18221415 | lifeskim:mentions | umls-concept:C1292733 | lld:lifeskim |
pubmed-article:18221415 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:18221415 | pubmed:dateCreated | 2008-3-12 | lld:pubmed |
pubmed-article:18221415 | pubmed:abstractText | Studies of mutations affecting lifespan in Caenorhabditis elegans show that mitochondrial generation of reactive oxygen species (ROS) plays a major causative role in organismal aging. Here, we describe a novel mechanism for regulating mitochondrial ROS production and lifespan in C. elegans: progressive mitochondrial protein modification by the glycolysis-derived dicarbonyl metabolite methylglyoxal (MG). We demonstrate that the activity of glyoxalase-1, an enzyme detoxifying MG, is markedly reduced with age despite unchanged levels of glyoxalase-1 mRNA. The decrease in enzymatic activity promotes accumulation of MG-derived adducts and oxidative stress markers, which cause further inhibition of glyoxalase-1 expression. Over-expression of the C. elegans glyoxalase-1 orthologue CeGly decreases MG modifications of mitochondrial proteins and mitochondrial ROS production, and prolongs C. elegans lifespan. In contrast, knock-down of CeGly increases MG modifications of mitochondrial proteins and mitochondrial ROS production, and decreases C. elegans lifespan. | lld:pubmed |
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pubmed-article:18221415 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18221415 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18221415 | pubmed:language | eng | lld:pubmed |
pubmed-article:18221415 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18221415 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:18221415 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:18221415 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:18221415 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18221415 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18221415 | pubmed:month | Mar | lld:pubmed |
pubmed-article:18221415 | pubmed:issn | 1474-9726 | lld:pubmed |
pubmed-article:18221415 | pubmed:author | pubmed-author:BierhausAngel... | lld:pubmed |
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pubmed-article:18221415 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:18221415 | pubmed:volume | 7 | lld:pubmed |
pubmed-article:18221415 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18221415 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18221415 | pubmed:pagination | 260-9 | lld:pubmed |
pubmed-article:18221415 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:18221415 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18221415 | pubmed:articleTitle | Glyoxalase-1 prevents mitochondrial protein modification and enhances lifespan in Caenorhabditis elegans. | lld:pubmed |
pubmed-article:18221415 | pubmed:affiliation | Department of Medicine I and Clinical Chemistry, University of Heidelberg, Im Neuenheimer Feld 410, 69120 Heidelberg, Germany. | lld:pubmed |
pubmed-article:18221415 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:18221415 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:18221415 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
entrez-gene:175530 | entrezgene:pubmed | pubmed-article:18221415 | lld:entrezgene |
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