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A thioredoxin with antioxidant activity identified from Eriocheir sinensis

文献类型:期刊论文

作者Mu, Changkao1,2; Zhao, Jianmin1; Wang, Lingling1; Song, Linsheng1; Song, Xiaoyan3; Zhang, Huan1,2; Qiu, Limei1; Gai, Yunchao1,2; Cui, Zhaoxia1
刊名FISH & SHELLFISH IMMUNOLOGY
出版日期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
DOI10.1016/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
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
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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.

入库方式: OAI收割

来源:海洋研究所

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