| pubmed-article:16299173 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16299173 | lifeskim:mentions | umls-concept:C0175677 | lld:lifeskim |
| pubmed-article:16299173 | lifeskim:mentions | umls-concept:C0040329 | lld:lifeskim |
| pubmed-article:16299173 | lifeskim:mentions | umls-concept:C0242724 | lld:lifeskim |
| pubmed-article:16299173 | lifeskim:mentions | umls-concept:C0023779 | lld:lifeskim |
| pubmed-article:16299173 | lifeskim:mentions | umls-concept:C0030016 | lld:lifeskim |
| pubmed-article:16299173 | lifeskim:mentions | umls-concept:C1545588 | lld:lifeskim |
| pubmed-article:16299173 | lifeskim:mentions | umls-concept:C0598281 | lld:lifeskim |
| pubmed-article:16299173 | lifeskim:mentions | umls-concept:C0205332 | lld:lifeskim |
| pubmed-article:16299173 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:16299173 | pubmed:dateCreated | 2005-12-12 | lld:pubmed |
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| pubmed-article:16299173 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16299173 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16299173 | pubmed:abstractText | Degradation of lipid peroxides leads to the formation of cytotoxic 2-alkenals and oxenes (collectively designated reactive carbonyls). The novel NADPH-dependent oxidoreductase 2-alkenal reductase (AER; EC 1.3.1.74) from Arabidopsis (Arabidopsis thaliana), which is encoded by the gene At5g16970, catalyzes the reduction of the alpha,beta-unsaturated bond of reactive carbonyls, and hence is presumed to function in antioxidative defense in plants. Here we show that Arabidopsis AER (At-AER) has a broad substrate spectrum to biologically relevant reactive carbonyls. Besides 2-alkenals, the enzyme recognized as substrates the lipid peroxide-derived oxenes 9-oxo-octadeca-(10E),(12Z)-dienoic acid and 13-oxo-octadeca-(9E),(11Z)-dienoic acid, as well as the potent genotoxin 4-oxo-(2E)-nonenal, altogether suggesting AER has a key role in the detoxification of reactive carbonyls. To validate this conclusion by in vivo studies, transgenic tobacco (Nicotiana tabacum) plants that had 100- to 250-fold higher AER activity levels than control plants were generated. The engineered plants exhibited significantly less damage from either (1) the exogenously administered 4-hydroxy-(2E)-nonenal, (2) treatment with methyl viologen plus light, or (3) intense light. We further show that the At-AER protein fused with the Aequorea victoria green fluorescent protein localizes in cytosol and the nucleus in Bright-Yellow 2 cells. These results indicate that reactive carbonyls mediate photooxidative injury in leaf cells, and At-AER in the cytosol protects the cells by reducing the alpha,beta-unsaturated bond of the photoproduced reactive carbonyls. | lld:pubmed |
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| pubmed-article:16299173 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16299173 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16299173 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16299173 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16299173 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16299173 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:16299173 | pubmed:issn | 0032-0889 | lld:pubmed |
| pubmed-article:16299173 | pubmed:author | pubmed-author:InzéDirkD | lld:pubmed |
| pubmed-article:16299173 | pubmed:author | pubmed-author:BabiychukElen... | lld:pubmed |
| pubmed-article:16299173 | pubmed:author | pubmed-author:KushnirSergei... | lld:pubmed |
| pubmed-article:16299173 | pubmed:author | pubmed-author:Belles-BoixEn... | lld:pubmed |
| pubmed-article:16299173 | pubmed:author | pubmed-author:SlootenLuitL | lld:pubmed |
| pubmed-article:16299173 | pubmed:author | pubmed-author:TakimotoKoich... | lld:pubmed |
| pubmed-article:16299173 | pubmed:author | pubmed-author:AsadaKoziK | lld:pubmed |
| pubmed-article:16299173 | pubmed:author | pubmed-author:ManoJun'ichiJ | lld:pubmed |
| pubmed-article:16299173 | pubmed:author | pubmed-author:ToriiYoshimit... | lld:pubmed |
| pubmed-article:16299173 | pubmed:author | pubmed-author:HiraokaEijiE | lld:pubmed |
| pubmed-article:16299173 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16299173 | pubmed:volume | 139 | lld:pubmed |
| pubmed-article:16299173 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16299173 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16299173 | pubmed:pagination | 1773-83 | lld:pubmed |
| pubmed-article:16299173 | pubmed:dateRevised | 2010-9-21 | lld:pubmed |
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| pubmed-article:16299173 | pubmed:meshHeading | pubmed-meshheading:16299173... | lld:pubmed |
| pubmed-article:16299173 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16299173 | pubmed:articleTitle | Protection against photooxidative injury of tobacco leaves by 2-alkenal reductase. Detoxication of lipid peroxide-derived reactive carbonyls. | lld:pubmed |
| pubmed-article:16299173 | pubmed:affiliation | Science Research Center , Yamaguchi University, Yoshida 1677-1, Yamaguchi 753-8515, Japan. mano@yamaguchi-u.ac.jp | lld:pubmed |
| pubmed-article:16299173 | pubmed:publicationType | Journal Article | lld:pubmed |
| entrez-gene:831560 | entrezgene:pubmed | pubmed-article:16299173 | lld:entrezgene |
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