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Molecular cloning, characterization and expression of a serine protease with clip-domain homologue from scallop Chlamys farreri
Zhu, Ling; Song, Linsheng; Zhao, Jiangmin; Xu, Wei; Chang, Yaqing
2007-05-01
发表期刊FISH & SHELLFISH IMMUNOLOGY
ISSN1050-4648
卷号22期号:5页码:556-566
文章类型Article
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.
关键词Serine Protease Clip Domain Chlamys Farreri Tissue Distribution Mrna Expression Injury Healing Immune Response
学科领域Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
DOI10.1016/j.fsi.2006.08.002
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收录类别SCI
语种英语
WOS记录号WOS:000245208300011
引用统计
被引频次:17[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/337002/5780
专题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
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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.
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