Analysis of the expression and antioxidative property of a peroxiredoxin 6 from Scophthalmus maximus

doi:10.1016/j.fsi.2010.04.008

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	Analysis of the expression and antioxidative property of a peroxiredoxin 6 from Scophthalmus maximus
	Zheng, Wen-jiang 1,2; Hu, Yong-hua 1; Zhang, Min 1; Sun, Li 1
	2010-08-01
发表期刊	FISH & SHELLFISH IMMUNOLOGY
ISSN	1050-4648
卷号	29 期号:2 页码:305-311
文章类型	Article
摘要	Peroxiredoxins (Prxs) are a group of antioxidant proteins that protect cells from oxidative damage caused by various peroxides. To date, six different isoforms of peroxiredoxin (Prx1 to Prx6) have been identified, of which, Prx6 belongs to the 1-Cys Prx subfamily. Although Prx6 of several fish species have been reported at sequence level, there are very few documented studies on the potential function of fish Prx6. In this report, we describe the identification and analysis of a Prx6 homologue, SmPrx6, from turbot Scophthalmus maximus. The full length cDNA of SmPrx6 contains a 5'- untranslated region (UTR) of 60 bp, an open reading frame of 666 bp, and a 3'-UTR of 244 bp. The deduced amino acid sequence of SmPrx6 shares 81-87% overall identities with known fish Prx6. In silico analysis identified in SmPrx6 a conserved Prx6 catalytic motif, PVCTTE, and the catalytic triads putatively involved in peroxidase and phospholipase A2 activities. Expression of SmPrx6 was detected in most fish organs, with the highest expression levels found in blood and heart and the lowest level in spleen. Experimental challenges with bacterial pathogens and poly(I:C) upregulated SmPrx6 expression in liver and spleen in a manner that is dependent on the challenging agent and the tissue type. Treatment of cultured primary hepatocytes with H(2)O(2) enhanced SmPrx6 expression in a dose-dependent manner. Recombinant SmPrx6 expressed in and purified from Escherichia coli exhibited thiol-dependent antioxidant activity and could protect cultured hepatocytes from H(2)O(2)-induced oxidative damage. Taken together, these results indicate that SmPrx6 is a Prx6 homologue with antioxidative property and is likely to be involved in both cellular maintenance and protective response during host immune defense against bacterial infection. (C) 2010 Elsevier Ltd. All rights reserved.; Peroxiredoxins (Prxs) are a group of antioxidant proteins that protect cells from oxidative damage caused by various peroxides. To date, six different isoforms of peroxiredoxin (Prx1 to Prx6) have been identified, of which, Prx6 belongs to the 1-Cys Prx subfamily. Although Prx6 of several fish species have been reported at sequence level, there are very few documented studies on the potential function of fish Prx6. In this report, we describe the identification and analysis of a Prx6 homologue, SmPrx6, from turbot Scophthalmus maximus. The full length cDNA of SmPrx6 contains a 5'- untranslated region (UTR) of 60 bp, an open reading frame of 666 bp, and a 3'-UTR of 244 bp. The deduced amino acid sequence of SmPrx6 shares 81-87% overall identities with known fish Prx6. In silico analysis identified in SmPrx6 a conserved Prx6 catalytic motif, PVCTTE, and the catalytic triads putatively involved in peroxidase and phospholipase A2 activities. Expression of SmPrx6 was detected in most fish organs, with the highest expression levels found in blood and heart and the lowest level in spleen. Experimental challenges with bacterial pathogens and poly(I:C) upregulated SmPrx6 expression in liver and spleen in a manner that is dependent on the challenging agent and the tissue type. Treatment of cultured primary hepatocytes with H2O2 enhanced SmPrx6 expression in a dose-dependent manner. Recombinant SmPrx6 expressed in and purified from Escherichia coli exhibited thiol-dependent antioxidant activity and could protect cultured hepatocytes from H2O2-induced oxidative damage. Taken together, these results indicate that SmPrx6 is a Prx6 homologue with antioxidative property and is likely to be involved in both cellular maintenance and protective response during host immune defense against bacterial infection. (C) 2010 Elsevier Ltd. All rights reserved.
关键词	Peroxiredoxin Scophthalmus Maximus Antioxidant Oxidative Stress Reactive Oxygen Species
学科领域	Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
DOI	10.1016/j.fsi.2010.04.008
URL	查看原文
收录类别	SCI
语种	英语
WOS记录号	WOS:000279388900017
引用统计	被引频次：39[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://ir.qdio.ac.cn/handle/337002/5790
专题	实验海洋生物学重点实验室
作者单位	1.Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China
第一作者单位	中国科学院海洋研究所
推荐引用方式 GB/T 7714	Zheng, Wen-jiang,Hu, Yong-hua,Zhang, Min,et al. Analysis of the expression and antioxidative property of a peroxiredoxin 6 from Scophthalmus maximus[J]. FISH & SHELLFISH IMMUNOLOGY,2010,29(2):305-311.
APA	Zheng, Wen-jiang,Hu, Yong-hua,Zhang, Min,&Sun, Li.(2010).Analysis of the expression and antioxidative property of a peroxiredoxin 6 from Scophthalmus maximus.FISH & SHELLFISH IMMUNOLOGY,29(2),305-311.
MLA	Zheng, Wen-jiang,et al."Analysis of the expression and antioxidative property of a peroxiredoxin 6 from Scophthalmus maximus".FISH & SHELLFISH IMMUNOLOGY 29.2(2010):305-311.

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