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
	2009-05-01
发表期刊	FISH & SHELLFISH IMMUNOLOGY
ISSN	1050-4648
卷号	26 期号:5 页码:716-723
文章类型	Article
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.
关键词	Thioredoxin Eriocheir Sinensis Gene Cloning Innate Immunity Mrna Expression Antioxidant Capacity
学科领域	Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
DOI	10.1016/j.fsi.2009.02.024
URL	查看原文
收录类别	SCI
语种	英语
WOS记录号	WOS:000266659400006
引用统计	被引频次：43[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/337002/2990
专题	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
第一作者单位	实验海洋生物学重点实验室
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.

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