Molecular cloning, characterization and expression of a serine protease with clip-domain homologue from scallop Chlamys farreri
文献类型：期刊论文
| 作者 | Zhu, Ling; Song, Linsheng; Zhao, Jiangmin; Xu, Wei; Chang, Yaqing |
| 刊名 | FISH & SHELLFISH IMMUNOLOGY
 |
| 出版日期 | 2007-05-01 |
| 卷号 | 22期号:5页码:556-566 |
| 关键词 | Serine Protease Clip Domain Chlamys Farreri Tissue Distribution Mrna Expression Injury Healing Immune Response |
| ISSN号 | 1050-4648 |
| DOI | 10.1016/j.fsi.2006.08.002 |
| 文献子类 | Article |
| 英文摘要 | Serine proteases play critical roles in a variety of invertebrate immune defense responses, including hemolymph coagulation, antimicrobial peptide synthesis, and melanization. The first mollusk serine protease with clip-domain (designated CFSP1) cDNA was obtained from the scallop Chlamys farreri challenged with Vibrio anguillarum by randomly sequencing a whole tissue cDNA library and rapid amplification of cDNA ends (RACE). The full-length cDNA of the C. farreri serine protease was 1211 bp, consisting of a 5-terminal untranslated region (UTR) of 72 bp, a 3'-terminal UTR of 77 bp with a canonical polyadenylation signal sequence AATAAA and a poly (A) tail, and an open reading frame of 1062 bp. The CFSP1 cDNA encoded a polypeptide of 354 amino acids with a putative signal peptide of 19 amino acids and a mature protein of 335 amino acids. The deduced amino acid sequence of CFSP1 contained an amino-terminal clip domain, a low complexity region, and a carboxyl-terminal serine protease domain. CFSP1 mRNA was mainly expressed constitutively in the hemocytes and was up-regulated and increased 2.9- and 1.9-fold at 16 h after injury and injection of bacteria. (c) 2006 Elsevier Ltd. All rights reserved.; Serine proteases play critical roles in a variety of invertebrate immune defense responses, including hemolymph coagulation, antimicrobial peptide synthesis, and melanization. The first mollusk serine protease with clip-domain (designated CFSP1) cDNA was obtained from the scallop Chlamys farreri challenged with Vibrio anguillarum by randomly sequencing a whole tissue cDNA library and rapid amplification of cDNA ends (RACE). The full-length cDNA of the C. farreri serine protease was 1211 bp, consisting of a 5-terminal untranslated region (UTR) of 72 bp, a 3'-terminal UTR of 77 bp with a canonical polyadenylation signal sequence AATAAA and a poly (A) tail, and an open reading frame of 1062 bp. The CFSP1 cDNA encoded a polypeptide of 354 amino acids with a putative signal peptide of 19 amino acids and a mature protein of 335 amino acids. The deduced amino acid sequence of CFSP1 contained an amino-terminal clip domain, a low complexity region, and a carboxyl-terminal serine protease domain. CFSP1 mRNA was mainly expressed constitutively in the hemocytes and was up-regulated and increased 2.9- and 1.9-fold at 16 h after injury and injection of bacteria. (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:000245208300011 |
| 公开日期 | 2010-12-24 |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/5781]  |
| 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, Qingdao 266071, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China 3.Dalian Fisheries Coll, Dalian 116023, Peoples R China |
| 推荐引用方式 GB/T 7714 | Zhu, Ling,Song, Linsheng,Zhao, Jiangmin,et al. Molecular cloning, characterization and expression of a serine protease with clip-domain homologue from scallop Chlamys farreri[J]. FISH & SHELLFISH IMMUNOLOGY,2007,22(5):556-566. |
| APA | Zhu, Ling,Song, Linsheng,Zhao, Jiangmin,Xu, Wei,&Chang, Yaqing.(2007).Molecular cloning, characterization and expression of a serine protease with clip-domain homologue from scallop Chlamys farreri.FISH & SHELLFISH IMMUNOLOGY,22(5),556-566. |
| MLA | Zhu, Ling,et al."Molecular cloning, characterization and expression of a serine protease with clip-domain homologue from scallop Chlamys farreri".FISH & SHELLFISH IMMUNOLOGY 22.5(2007):556-566. |
入库方式： OAI收割
来源：海洋研究所
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