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Identification of a cathepsin D potentially involved in H2A cleavage from scallop Chlamys farreri

文献类型：期刊论文

作者Li, Chenghua1; Zhang, Huan2; Li, Ling2; Song, Linsheng2
刊名MOLECULAR BIOLOGY REPORTS
出版日期2010-03-01
卷号37期号:3页码:1451-1460
ISSN号0301-4851
关键词Chlamys Farrei Cathepsin d Tissue Expression Innate Immunity
通讯作者Li, CH, Chinese Acad Sci, Yantai Inst Coastal Zone Res Sustainable Dev, 26 Yinhai Rd, Yantai 264003, Peoples R China
产权排序[Li, Chenghua] Chinese Acad Sci, Yantai Inst Coastal Zone Res Sustainable Dev, Yantai 264003, Peoples R China; [Zhang, Huan; Li, Ling; Song, Linsheng] Chinese Acad Sci, Key Lab Expt Marine Biol, Inst Oceanol, Qingdao 266071, Peoples R China
文献子类Article
英文摘要We report here a cDNA and its deduced amino acid sequence encoding a cathepsin D-like, aspartic protease from Chlamys farreri (denoted as CfCD) by expressed sequence tag and rapid amplification of cDNA ends techniques. The cDNA of CfCD consisted of 1,810 nucleotides with a canonical polyadenylation signal sequence AATAAA and a polyA tail, encoding a short signal peptide of 18 amino acids, a pro-enzyme peptide of 29 amino acid residues, and a mature enzyme of 349 residues. The deduced amino acid sequence of CfCD was significant homology to CDs from human, fish and invertebrates. Two conserved catalytic motifs (VFDTGSSNLWV and AIADTGTSLLVG) and two potential N-glycosylation sites were also identified in the deduced amino acid sequence of CfCD. All this characteristics indicated CfCD should be a member of CDs family. The mRNA spatial expression of CfCD in mantle, gonad, gill, hemocytes, hepatopancreas and adductor muscle was examined by quantitative real-time PCR. mRNA transcripts of CfCD could be detected in all tissues with the highest expression level in hepatopancreas. After 8 h Vibrio anguillarum challenge, the expression level of CfCD changed significantly in all examined tissues except mantle (P = 0.183) and hemocytes (P = 0.069). The information generated in the present study would be helpful for future studies aiming at investigating the detailed functions of cathepsin D from marine invertebrates.; We report here a cDNA and its deduced amino acid sequence encoding a cathepsin D-like, aspartic protease from Chlamys farreri (denoted as CfCD) by expressed sequence tag and rapid amplification of cDNA ends techniques. The cDNA of CfCD consisted of 1,810 nucleotides with a canonical polyadenylation signal sequence AATAAA and a polyA tail, encoding a short signal peptide of 18 amino acids, a pro-enzyme peptide of 29 amino acid residues, and a mature enzyme of 349 residues. The deduced amino acid sequence of CfCD was significant homology to CDs from human, fish and invertebrates. Two conserved catalytic motifs (VFDTGSSNLWV and AIADTGTSLLVG) and two potential N-glycosylation sites were also identified in the deduced amino acid sequence of CfCD. All this characteristics indicated CfCD should be a member of CDs family. The mRNA spatial expression of CfCD in mantle, gonad, gill, hemocytes, hepatopancreas and adductor muscle was examined by quantitative real-time PCR. mRNA transcripts of CfCD could be detected in all tissues with the highest expression level in hepatopancreas. After 8 h Vibrio anguillarum challenge, the expression level of CfCD changed significantly in all examined tissues except mantle (P = 0.183) and hemocytes (P = 0.069). The information generated in the present study would be helpful for future studies aiming at investigating the detailed functions of cathepsin D from marine invertebrates.
学科主题Biochemistry & Molecular Biology
URL标识查看原文
WOS关键词DEGRADATION ; LYSOSOMES ; ENZYME
WOS研究方向Biochemistry & Molecular Biology
语种英语
WOS记录号WOS:000274212500039
资助机构Chinese Academy of Sciences [AK0911DB-097-3]; Key Laboratory of Applied Marine Biology
公开日期2011-07-14
源URL[http://ir.yic.ac.cn/handle/133337/3758]  
专题烟台海岸带研究所_海岸带生物学与生物资源利用所重点实验室
作者单位1.Chinese Acad Sci, Yantai Inst Coastal Zone Res Sustainable Dev, Yantai 264003, Peoples R China
2.Chinese Acad Sci, Key Lab Expt Marine Biol, Inst Oceanol, Qingdao 266071, Peoples R China
推荐引用方式
GB/T 7714		 Li, Chenghua,Zhang, Huan,Li, Ling,et al. Identification of a cathepsin D potentially involved in H2A cleavage from scallop Chlamys farreri[J]. MOLECULAR BIOLOGY REPORTS,2010,37(3):1451-1460.
APA Li, Chenghua,Zhang, Huan,Li, Ling,&Song, Linsheng.(2010).Identification of a cathepsin D potentially involved in H2A cleavage from scallop Chlamys farreri.MOLECULAR BIOLOGY REPORTS,37(3),1451-1460.
MLA Li, Chenghua,et al."Identification of a cathepsin D potentially involved in H2A cleavage from scallop Chlamys farreri".MOLECULAR BIOLOGY REPORTS 37.3(2010):1451-1460.

入库方式： OAI收割

来源：烟台海岸带研究所

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