A sigma-class glutathione S-transferase from Solen grandis that responded to microorganism glycan and organic contaminants
Yang, Jialong1,3; Wei, Xiumei2; Xu, Jie2; Yang, Dinglong2; Liu, Xiangquan2; Yang, Jianmin2; Fang, Jinghui2; Hu, Xiaoke1
发表期刊FISH & SHELLFISH IMMUNOLOGY
ISSN1050-4648
2012-06-01
卷号32期号:6页码:1198-1204
关键词Soler Grandis Glutathione S-transferase (Gst) Innate Immunity Antioxidant Enzymes Real-time Pcr
产权排序[Yang, Jialong; Hu, Xiaoke] Chinese Acad Sci, Yantai Inst Coastal Zone Res, Yantai 264003, Peoples R China; [Wei, Xiumei; Xu, Jie; Yang, Dinglong; Liu, Xiangquan; Yang, Jianmin; Fang, Jinghui] Shandong Marine Fisheries Res Inst, Yantai 264006, Peoples R China; [Yang, Jialong] Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China
通讯作者Yang, JL (reprint author), Chinese Acad Sci, Yantai Inst Coastal Zone Res, 17 Chunhui Rd, Yantai 264003, Peoples R China.,jlyang@yic.ac.cn ; xkhu@yic.ac.cn
作者部门海岸带生物学与生物资源利用所重点实验室
英文摘要Glutathione S-transferases (GSTs) are a superfamily of antioxidant enzymes, which play crucial roles in detoxification and protection of tissues from oxidative damage caused by reactive oxygen species (ROS). In this study, a sigma-class GST was identified from razor clam Solen grandis (designated as SgGST-S1), and its expression patterns, both in tissues and toward microorganism glycan as well as organic contaminants stimulation, were then characterized. The full-length cDNA of SgGST-S1 was of 1291 bp, containing a 5' untranslated region (UTR) of 27 bp, and a 3' UTR of 619 bp with a poly (A) tail. The open reading frame (ORF) was of 645 bp, encoding a polypeptide of 214 amino acids with the predicted molecular weight of 24.8 kDa, which shared 47% identity with GST from Ruditapes philippinarum. The analysis of conserved domain and phylogenetic relationship strongly suggested that SgGST-S1 was a member of sigma-class GST. The mRNA of SgGST-S1 was constitutively expressed in all tested tissues of healthy razor clam, including mantle, gill, gonad, hemocytes, muscle, and hepatopancreas, and it was highly expressed in hepatopancreas. The mRNA expression of SgGST-S1 in hemocytes was significantly up-regulated (P < 0.01) after razor clam was stimulated by peptidoglycan (PGN) or beta-1, 3-glucan, but not LPS. In addition, the SgGST-S1 transcript level was also significantly (P < 0.01) induced by exposure of benzo[a]pyrene (B[a]P) or Polybrominated Diphenyl Ethers (PBDE). All the results indicated that SgGSTS1 might serve as an antioxidant enzyme involving in the detoxification cause by both microorganism glycan and organic contaminants. (C) 2012 Elsevier Ltd. All rights reserved.; Glutathione S-transferases (GSTs) are a superfamily of antioxidant enzymes, which play crucial roles in detoxification and protection of tissues from oxidative damage caused by reactive oxygen species (ROS). In this study, a sigma-class GST was identified from razor clam Solen grandis (designated as SgGST-S1), and its expression patterns, both in tissues and toward microorganism glycan as well as organic contaminants stimulation, were then characterized. The full-length cDNA of SgGST-S1 was of 1291 bp, containing a 5' untranslated region (UTR) of 27 bp, and a 3' UTR of 619 bp with a poly (A) tail. The open reading frame (ORF) was of 645 bp, encoding a polypeptide of 214 amino acids with the predicted molecular weight of 24.8 kDa, which shared 47% identity with GST from Ruditapes philippinarum. The analysis of conserved domain and phylogenetic relationship strongly suggested that SgGST-S1 was a member of sigma-class GST. The mRNA of SgGST-S1 was constitutively expressed in all tested tissues of healthy razor clam, including mantle, gill, gonad, hemocytes, muscle, and hepatopancreas, and it was highly expressed in hepatopancreas. The mRNA expression of SgGST-S1 in hemocytes was significantly up-regulated (P < 0.01) after razor clam was stimulated by peptidoglycan (PGN) or beta-1, 3-glucan, but not LPS. In addition, the SgGST-S1 transcript level was also significantly (P < 0.01) induced by exposure of benzo[a]pyrene (B[a]P) or Polybrominated Diphenyl Ethers (PBDE). All the results indicated that SgGSTS1 might serve as an antioxidant enzyme involving in the detoxification cause by both microorganism glycan and organic contaminants. (C) 2012 Elsevier Ltd. All rights reserved.
文章类型Article
资助机构Program of Agriculture Thoroughbred Project, Shandong province, China; Chinese Academy of Sciences
收录类别SCI
语种英语
关键词[WOS]MESSENGER-RNA EXPRESSION ; DIPHENYL ETHER PBDE ; FRESH-WATER MUSSEL ; MOLECULAR-CLONING ; OXIDATIVE STRESS ; GENE-EXPRESSION ; ANTIOXIDANT ; SELENIUM ; CHINA ; PEROXIDASE
研究领域[WOS]Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
WOS记录号WOS:000304511800032
引用统计
被引频次:23[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.yic.ac.cn/handle/133337/6086
专题海岸带生物学与生物资源利用重点实验室_海岸带生物学与生物资源保护实验室
海岸带生物学与生物资源利用重点实验室_海岸带生物资源高效利用研究与发展中心
作者单位1.Chinese Acad Sci, Yantai Inst Coastal Zone Res, Yantai 264003, Peoples R China
2.Shandong Marine Fisheries Res Inst, Yantai 264006, Peoples R China
3.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China
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Yang, Jialong,Wei, Xiumei,Xu, Jie,et al. A sigma-class glutathione S-transferase from Solen grandis that responded to microorganism glycan and organic contaminants[J]. FISH & SHELLFISH IMMUNOLOGY,2012,32(6):1198-1204.
APA Yang, Jialong.,Wei, Xiumei.,Xu, Jie.,Yang, Dinglong.,Liu, Xiangquan.,...&Hu, Xiaoke.(2012).A sigma-class glutathione S-transferase from Solen grandis that responded to microorganism glycan and organic contaminants.FISH & SHELLFISH IMMUNOLOGY,32(6),1198-1204.
MLA Yang, Jialong,et al."A sigma-class glutathione S-transferase from Solen grandis that responded to microorganism glycan and organic contaminants".FISH & SHELLFISH IMMUNOLOGY 32.6(2012):1198-1204.
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