IOCAS-IR  > 海洋生物技术研发中心
Three clip domain serine proteases (cSPs) and one clip domain serine protease homologue (cSPH) identified from haemocytes and eyestalk cDNA libraries of swimming crab Portunus trituberculatus
Li, Qianqian1,2; Cui, Zhaoxia1; Liu, Yuan1; Wang, Shuangyan1,2; Song, Chengwen1,2; Cui, ZX (reprint author), Chinese Acad Sci, Inst Oceanol, EMBL, 7 Nanhai Rd, Qingdao 266071, Peoples R China.
2012-04-01
发表期刊FISH & SHELLFISH IMMUNOLOGY
ISSN1050-4648
卷号32期号:4页码:565-571
文章类型Article
摘要Four genes including three clip domain serine proteases (PtcSP1, PtcSP2 and PtcSP3) and one clip domain serine protease homologue (PtcSPH) of the swimming crab Portunus trituberculatus (Decapoda: Brachyura: Portunidae) were characterized based on analysis of expressed sequence tags from haemocytes and eyestalk cDNA libraries. The relative four peptidases, which share high structural similarity to the clip-SPs of other arthropod species, appeared to possess a clip domain at the N-terminus and an enzymatically active serine protease domain at the C-terminus except PtcSPH for its second catalytic residue Asp. (D) replaced by Ala (A). Alignment among the four full-sequences showed that PtcSP2 and PtcSP3 had the highest identical score (58%) while the similarity of other sequences was lower than 24%. The mRNA transcripts of PtcSPs and PtcSPH could be detected widely in all the examined tissues with remarkable different expression levels. The temporal expressions of PtcSPs and PtcSPH demonstrated different time-dependent expression pattern post Vibrio alginolyticus, Micrococcus luteus. and Pichia pastoris challenge. Especially, the expression of PtcSPH transcripts showed greater change against V. alginolyticus compared with the other two microorganisms. These findings suggest that PtcSPs and PtcSPH play different roles in the antibacterial defence mechanism of P. trituberculatus crab. (C) 2012 Elsevier Ltd. All rights reserved.
关键词Portunus Trituberculatus Clip Domain Serine Protease Serine Protease Homologue Mrna Expression Profile
学科领域Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
DOI10.1016/j.fsi.2012.01.006
URL查看原文
收录类别SCI
语种英语
WOS记录号WOS:000301827100007
引用统计
被引频次:15[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/337002/12401
专题海洋生物技术研发中心
实验海洋生物学重点实验室
通讯作者Cui, ZX (reprint author), Chinese Acad Sci, Inst Oceanol, EMBL, 7 Nanhai Rd, Qingdao 266071, Peoples R China.
作者单位1.Chinese Acad Sci, Inst Oceanol, EMBL, Qingdao 266071, Peoples R China
2.Chinese Acad Sci, Grad Univ, Beijing 100039, Peoples R China
第一作者单位中国科学院海洋研究所
推荐引用方式
GB/T 7714
Li, Qianqian,Cui, Zhaoxia,Liu, Yuan,et al. Three clip domain serine proteases (cSPs) and one clip domain serine protease homologue (cSPH) identified from haemocytes and eyestalk cDNA libraries of swimming crab Portunus trituberculatus[J]. FISH & SHELLFISH IMMUNOLOGY,2012,32(4):565-571.
APA Li, Qianqian,Cui, Zhaoxia,Liu, Yuan,Wang, Shuangyan,Song, Chengwen,&Cui, ZX .(2012).Three clip domain serine proteases (cSPs) and one clip domain serine protease homologue (cSPH) identified from haemocytes and eyestalk cDNA libraries of swimming crab Portunus trituberculatus.FISH & SHELLFISH IMMUNOLOGY,32(4),565-571.
MLA Li, Qianqian,et al."Three clip domain serine proteases (cSPs) and one clip domain serine protease homologue (cSPH) identified from haemocytes and eyestalk cDNA libraries of swimming crab Portunus trituberculatus".FISH & SHELLFISH IMMUNOLOGY 32.4(2012):565-571.
条目包含的文件
文件名称/大小 文献类型 版本类型 开放类型 使用许可
Three clip domain se(1863KB) 限制开放使用许可浏览
个性服务
推荐该条目
保存到收藏夹
查看访问统计
导出为Endnote文件
谷歌学术
谷歌学术中相似的文章
[Li, Qianqian]的文章
[Cui, Zhaoxia]的文章
[Liu, Yuan]的文章
百度学术
百度学术中相似的文章
[Li, Qianqian]的文章
[Cui, Zhaoxia]的文章
[Liu, Yuan]的文章
必应学术
必应学术中相似的文章
[Li, Qianqian]的文章
[Cui, Zhaoxia]的文章
[Liu, Yuan]的文章
相关权益政策
暂无数据
收藏/分享
文件名: Three clip domain serine proteases (cSPs) and one clip domain serine protease homologue (cSPH) identified from haemocytes and eyestalk cDNA libraries of swimming crab Portunus trituberculatus.pdf
格式: Adobe PDF
此文件暂不支持浏览
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。