The cDNA cloning and mRNA expression of heat shock protein 70 gene in the haemocytes of bay scallop (Argopecten irradians, Lamarck 1819) responding to bacteria challenge and naphthalin stress
文献类型：期刊论文
| 作者 | Song, Linsheng1,3; Wu, Longtao1; Ni, Duojiao1; Chang, Yaqing2; Xu, Wei1; Xing, Kezhi3 |
| 刊名 | FISH & SHELLFISH IMMUNOLOGY
 |
| 出版日期 | 2006-10-01 |
| 卷号 | 21期号:4页码:335-345 |
| 关键词 | Bay Scallop Argopecten Irradians Expressed Sequence Tag Heat Shock Protein 70 Cdna Cloning Mrna Expression Bacteria Challenge Naphthalin Stress Immunity Response |
| ISSN号 | 1050-4648 |
| DOI | 10.1016/j.fsi.2005.12.011 |
| 文献子类 | Article |
| 英文摘要 | Heat shock protein 70 (HSP70) is an important member of the heat shock protein superfamily, and it plays a key role in the process of protecting cells, facilitating the folding of nascent peptides and responding to stress. The cDNA of bay scallop Argopecten irradians HSP70 (designated AIHSP70) was cloned by the techniques of homological cloning and rapid amplification of cDNA end (RACE). The full length of AIHSP70 cDNA was 2651 bp in length, having a 5' untranslated region (UTR) of 96 bp, a 3' UTR of 575 bp, and an open reading frame (ORF) of 1980 bp encoding a polypeptide of 659 amino acids with an estimated molecular mass of 71.80 kDa and an estimated isoelectric point of 5.26. BLAST analysis revealed that the AIHSP70 gene shared high identity with other known HSP70 genes. Three classical HSP signature motifs were detected in AIHSP70 by InterPro, analysis. 3-D structural prediction of AIHSP70 showed that its N terminal ATPase activity domain and,C terminal substrate-binding domain shared high similarity with that in human heat shock protein 70. The results indicated that the AIHSP70 was a member of the heat shock protein 70 family. A semi-quantitive RT-PCR method was used to analyse the expression of AIHSP70 gene after the treatment of naphthalin which is one kind of polycyclic aromatic hydrocarbon (PAH) and the challenge of bacteria. mRNA expression of AIHSP70 in scallop was up-regulated significantly after the stimulation of naphthalin and increased with increasing naphthalin concentration. A clearly time-dependent expression pattern of AIHSP70 was observed after the scallops were infected by Vibrio anguillarum, and the mRNA expression reached a maximum level at 8 h and lasted to 16 h, and then dropped progressively. The results indicated that AIHSP70 could play an important role in mediating the environmental stress and immune response in scallop. (c) 2006 Elsevier Ltd. All rights reserved.; Heat shock protein 70 (HSP70) is an important member of the heat shock protein superfamily, and it plays a key role in the process of protecting cells, facilitating the folding of nascent peptides and responding to stress. The cDNA of bay scallop Argopecten irradians HSP70 (designated AIHSP70) was cloned by the techniques of homological cloning and rapid amplification of cDNA end (RACE). The full length of AIHSP70 cDNA was 2651 bp in length, having a 5' untranslated region (UTR) of 96 bp, a 3' UTR of 575 bp, and an open reading frame (ORF) of 1980 bp encoding a polypeptide of 659 amino acids with an estimated molecular mass of 71.80 kDa and an estimated isoelectric point of 5.26. BLAST analysis revealed that the AIHSP70 gene shared high identity with other known HSP70 genes. Three classical HSP signature motifs were detected in AIHSP70 by InterPro, analysis. 3-D structural prediction of AIHSP70 showed that its N terminal ATPase activity domain and,C terminal substrate-binding domain shared high similarity with that in human heat shock protein 70. The results indicated that the AIHSP70 was a member of the heat shock protein 70 family. A semi-quantitive RT-PCR method was used to analyse the expression of AIHSP70 gene after the treatment of naphthalin which is one kind of polycyclic aromatic hydrocarbon (PAH) and the challenge of bacteria. mRNA expression of AIHSP70 in scallop was up-regulated significantly after the stimulation of naphthalin and increased with increasing naphthalin concentration. A clearly time-dependent expression pattern of AIHSP70 was observed after the scallops were infected by Vibrio anguillarum, and the mRNA expression reached a maximum level at 8 h and lasted to 16 h, and then dropped progressively. The results indicated that AIHSP70 could play an important role in mediating the environmental stress and immune response in scallop. (c) 2006 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:000240061600001 |
| 公开日期 | 2010-12-24 |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/5923]  |
| 专题 | 海洋研究所_实验海洋生物学重点实验室 |
| 作者单位 | 1.Acad Sinica, Inst Oceanol, Qingdao 266071, Peoples R China 2.Dalian Fisheries Coll, Dalian 116023, Peoples R China 3.Tianjin Agr Coll, Tianjin 300381, Peoples R China |
| 推荐引用方式 GB/T 7714 | Song, Linsheng,Wu, Longtao,Ni, Duojiao,et al. The cDNA cloning and mRNA expression of heat shock protein 70 gene in the haemocytes of bay scallop (Argopecten irradians, Lamarck 1819) responding to bacteria challenge and naphthalin stress[J]. FISH & SHELLFISH IMMUNOLOGY,2006,21(4):335-345. |
| APA | Song, Linsheng,Wu, Longtao,Ni, Duojiao,Chang, Yaqing,Xu, Wei,&Xing, Kezhi.(2006).The cDNA cloning and mRNA expression of heat shock protein 70 gene in the haemocytes of bay scallop (Argopecten irradians, Lamarck 1819) responding to bacteria challenge and naphthalin stress.FISH & SHELLFISH IMMUNOLOGY,21(4),335-345. |
| MLA | Song, Linsheng,et al."The cDNA cloning and mRNA expression of heat shock protein 70 gene in the haemocytes of bay scallop (Argopecten irradians, Lamarck 1819) responding to bacteria challenge and naphthalin stress".FISH & SHELLFISH IMMUNOLOGY 21.4(2006):335-345. |
入库方式： OAI收割
来源：海洋研究所
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