A thioredoxin with antioxidant activity identified from Eriocheir sinensis

doi:10.1016/j.fsi.2009.02.024

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	A thioredoxin with antioxidant activity identified from Eriocheir sinensis
	Mu, Changkao 1,2; Zhao, Jianmin 1; Wang, Lingling 1; Song, Linsheng 1; Song, Xiaoyan 3; Zhang, Huan 1,2; Qiu, Limei 1; Gai, Yunchao 1,2; Cui, Zhaoxia 1
刊名	FISH & SHELLFISH IMMUNOLOGY
	2009-05-01
卷号	26 期号:5 页码:716-723
关键词	Thioredoxin Eriocheir Sinensis Gene Cloning Innate Immunity Mrna Expression Antioxidant Capacity
ISSN号	1050-4648
DOI	10.1016/j.fsi.2009.02.024
文献子类	Article
英文摘要	Thioredoxin, with a redox-active disulfide/dithiol in the active site, is the major ubiquitous disulfide reductase responsible for maintaining proteins in their reduced state. In the present study, the cDNA encoding thioredoxin-1 (designated EsTrx1) was cloned from Chinese mitten crab Eriocheir sinensis by using rapid amplification of cDNA ends (RACE) approaches. The full-length cDNA of EsTrx1 was of 641 bp, containing a 51 untranslated region (UTR) of 17 bp, a 3' UTR of 306 bp with a poly (A) tail, and an open reading frame (ORF) of 318 bp encoding a polypeptide of 105 amino acids. The high similarity of EsTrx1 with Trx1s from other animals indicated that EsTrx1 should be a new member of the Trx1 sub-family. Quantitative real-time PCR analysis revealed the presence of EsTrx1 transcripts in gill, gonad, hepato-pancreas, muscle, heart and haemocytes. The expression of EsTrx1 mRNA in haemocytes was up-regulated after Listonella anguillarum challenge, reached the maximum level at 6 h post-stimulation, and then dropped back to the original level gradually. In order to elucidate its biological functions, EsTrx1 was recombined and expressed in E. coli BL21 (DE3). The rEsTrx1 was demonstrated to possess the expected redox activity in enzymatic analysis, and to be more potent than GSH in antioxidant capacity. These results together indicated that EsTrx1 could function as an important antioxidant in a physiological context, and perhaps is involved in the responses to bacterial challenge. (C) 2009 Elsevier Ltd. All rights reserved.; Thioredoxin, with a redox-active disulfide/dithiol in the active site, is the major ubiquitous disulfide reductase responsible for maintaining proteins in their reduced state. In the present study, the cDNA encoding thioredoxin-1 (designated EsTrx1) was cloned from Chinese mitten crab Eriocheir sinensis by using rapid amplification of cDNA ends (RACE) approaches. The full-length cDNA of EsTrx1 was of 641 bp, containing a 51 untranslated region (UTR) of 17 bp, a 3' UTR of 306 bp with a poly (A) tail, and an open reading frame (ORF) of 318 bp encoding a polypeptide of 105 amino acids. The high similarity of EsTrx1 with Trx1s from other animals indicated that EsTrx1 should be a new member of the Trx1 sub-family. Quantitative real-time PCR analysis revealed the presence of EsTrx1 transcripts in gill, gonad, hepato-pancreas, muscle, heart and haemocytes. The expression of EsTrx1 mRNA in haemocytes was up-regulated after Listonella anguillarum challenge, reached the maximum level at 6 h post-stimulation, and then dropped back to the original level gradually. In order to elucidate its biological functions, EsTrx1 was recombined and expressed in E. coli BL21 (DE3). The rEsTrx1 was demonstrated to possess the expected redox activity in enzymatic analysis, and to be more potent than GSH in antioxidant capacity. These results together indicated that EsTrx1 could function as an important antioxidant in a physiological context, and perhaps is involved in the responses to bacterial challenge. (C) 2009 Elsevier Ltd. All rights reserved.
学科主题	Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
URL标识	查看原文
语种	英语
WOS记录号	WOS:000266659400006
公开日期	2010-12-22
内容类型	期刊论文
源URL	[http://ir.qdio.ac.cn/handle/337002/2991]
专题	海洋研究所_实验海洋生物学重点实验室
作者单位	1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China 3.NW A&F Univ, Coll Anim Sci & Technol, Yangling 712100, Peoples R China
推荐引用方式 GB/T 7714	Mu, Changkao,Zhao, Jianmin,Wang, Lingling,et al. A thioredoxin with antioxidant activity identified from Eriocheir sinensis[J]. FISH & SHELLFISH IMMUNOLOGY,2009,26(5):716-723.
APA	Mu, Changkao.,Zhao, Jianmin.,Wang, Lingling.,Song, Linsheng.,Song, Xiaoyan.,...&Cui, Zhaoxia.(2009).A thioredoxin with antioxidant activity identified from Eriocheir sinensis.FISH & SHELLFISH IMMUNOLOGY,26(5),716-723.
MLA	Mu, Changkao,et al."A thioredoxin with antioxidant activity identified from Eriocheir sinensis".FISH & SHELLFISH IMMUNOLOGY 26.5(2009):716-723.