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KMID : 0613820140240121291
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Journal of Life Science
2014 Volume.24 No. 12 p.1291 ~ p.1300
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Molecular Characterization and Expression Analysis of Peroxiredoxin 2 cDNA from Abalone (Haliotis discus hannai)
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Moon Ji-Young
Park Eun-Hee
Kong Hee-Jeong
Kim Young-Ok
Kim Dong-Gyun
An Cheul-Min
Nam Bo-Hye
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Abstract
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Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant enzymes that participate in a variety of biological processes, including H2O2-mediated signal transduction, molecular chaperoning, and mitochondrial function. In this study, we isolated and characterized a Prx 2 cDNA from abalone (Haliotis discus hannai). The abalone Prx 2 cDNA encoded a 199-amino acid polypeptide that belongs to a class of typical 2-Cys Prxs that contain peroxidatic and resolving cysteines. The deduced abalone Prx 2 protein showed strong homology (64-99%) with Prx 2 proteins from other species, including mollusk, fish, amphibians, and mammals, and it was most closely related to disk abalone (H. discus discus) Prx 2. Abalone Prx 2 mRNA was ubiquitously detected in tested tissues, and its expression was comparatively high in the mantle, gills, liver, foot, and digestive duct. The expression level of abalone Prx 2 mRNA was 106.7-fold, 51.9-fold, and 437.8-fold higher, respectively, in the gills, digestive duct, and liver than in the muscles. The expression level of abalone Prx 2 mRNA in the liver peaked at 6 hr postinfection with Vibrio parahemolyticus and decreased at 12 hr postinfection. The expression level of abalone Prx 2 mRNA in hemocytes was drastically increased at 1 hr postinfection with V. parahemolyticus. These results suggest that abalone Prx 2 is conserved through evolution and that it may play a role similar to that of its mammalian counterpart.
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KEYWORD
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Abalone, Haliotis discuss hannai, peroxiredoxin, reactive oxygen species, Vibrio parahemolyticus
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