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Protection against photooxidative injury of tobacco leaves by 2-alkenal reductase: detoxication of lipid peroxide-derived reactive carbonyls

(2005) PLANT PHYSIOLOGY. 139(4). p.1773-1783
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Abstract
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.
Keywords
OXIDOREDUCTASE, PRODUCT, INACTIVATION, ALDOSE REDUCTASE, METABOLISM, ALDEHYDE DEHYDROGENASE, ALDOSE/ALDEHYDE REDUCTASE, ARABIDOPSIS-THALIANA, OXIDIZING DRUG DIAMIDE, OXIDATIVE STRESS

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MLA
Mano, Jun’ichi, Enric Belles-Boix, Elena Babiychuk, et al. “Protection Against Photooxidative Injury of Tobacco Leaves by 2-alkenal Reductase: Detoxication of Lipid Peroxide-derived Reactive Carbonyls.” PLANT PHYSIOLOGY 139.4 (2005): 1773–1783. Print.
APA
Mano, Jun’ichi, Belles-Boix, E., Babiychuk, E., Inzé, D., Torii, Y., Hiraoka, E., Takimoto, K., et al. (2005). Protection against photooxidative injury of tobacco leaves by 2-alkenal reductase: detoxication of lipid peroxide-derived reactive carbonyls. PLANT PHYSIOLOGY, 139(4), 1773–1783.
Chicago author-date
Mano, Jun’ichi, Enric Belles-Boix, Elena Babiychuk, Dirk Inzé, Yoshimitsu Torii, Eiji Hiraoka, Koichi Takimoto, Luit Slooten, Kozi Asada, and Sergei Kushnir. 2005. “Protection Against Photooxidative Injury of Tobacco Leaves by 2-alkenal Reductase: Detoxication of Lipid Peroxide-derived Reactive Carbonyls.” Plant Physiology 139 (4): 1773–1783.
Chicago author-date (all authors)
Mano, Jun’ichi, Enric Belles-Boix, Elena Babiychuk, Dirk Inzé, Yoshimitsu Torii, Eiji Hiraoka, Koichi Takimoto, Luit Slooten, Kozi Asada, and Sergei Kushnir. 2005. “Protection Against Photooxidative Injury of Tobacco Leaves by 2-alkenal Reductase: Detoxication of Lipid Peroxide-derived Reactive Carbonyls.” Plant Physiology 139 (4): 1773–1783.
Vancouver
1.
Mano J, Belles-Boix E, Babiychuk E, Inzé D, Torii Y, Hiraoka E, et al. Protection against photooxidative injury of tobacco leaves by 2-alkenal reductase: detoxication of lipid peroxide-derived reactive carbonyls. PLANT PHYSIOLOGY. 2005;139(4):1773–83.
IEEE
[1]
J. Mano et al., “Protection against photooxidative injury of tobacco leaves by 2-alkenal reductase: detoxication of lipid peroxide-derived reactive carbonyls,” PLANT PHYSIOLOGY, vol. 139, no. 4, pp. 1773–1783, 2005.
@article{330909,
  abstract     = {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.},
  author       = {Mano, Jun'ichi and Belles-Boix, Enric and Babiychuk, Elena and Inzé, Dirk and Torii, Yoshimitsu and Hiraoka, Eiji and Takimoto, Koichi and Slooten, Luit and Asada, Kozi and Kushnir, Sergei},
  issn         = {0032-0889},
  journal      = {PLANT PHYSIOLOGY},
  keywords     = {OXIDOREDUCTASE,PRODUCT,INACTIVATION,ALDOSE REDUCTASE,METABOLISM,ALDEHYDE DEHYDROGENASE,ALDOSE/ALDEHYDE REDUCTASE,ARABIDOPSIS-THALIANA,OXIDIZING DRUG DIAMIDE,OXIDATIVE STRESS},
  language     = {eng},
  number       = {4},
  pages        = {1773--1783},
  title        = {Protection against photooxidative injury of tobacco leaves by 2-alkenal reductase: detoxication of lipid peroxide-derived reactive carbonyls},
  url          = {http://dx.doi.org/10.1104/pp.105.070391},
  volume       = {139},
  year         = {2005},
}

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