| Identification of a cathepsin D potentially involved in H2A cleavage from scallop Chlamys farreri | |
| Li, Chenghua1; Zhang, Huan2; Li, Ling2; Song, Linsheng2 | |
| 发表期刊 | MOLECULAR BIOLOGY REPORTS
 |
| ISSN | 0301-4851 |
| 2010-03-01 | |
| 卷号 | 37期号:3页码:1451-1460 |
| 关键词 | Chlamys Farrei Cathepsin d Tissue Expression Innate Immunity |
| 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 |
| 通讯作者 | Li, CH, Chinese Acad Sci, Yantai Inst Coastal Zone Res Sustainable Dev, 26 Yinhai Rd, Yantai 264003, Peoples R China |
| 作者部门 | 生物资源实验室 |
| 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. |
| 文章类型 | Article |
| 资助机构 | Chinese Academy of Sciences [AK0911DB-097-3]; Key Laboratory of Applied Marine Biology |
| 收录类别 | SCI |
| 语种 | 英语 |
| 关键词[WOS] | DEGRADATION ; LYSOSOMES ; ENZYME |
| 研究领域[WOS] | Biochemistry & Molecular Biology |
| WOS记录号 | WOS:000274212500039 |
| 引用统计 | |
| 文献类型 | 期刊论文 |
| 条目标识符 | http://ir.yic.ac.cn/handle/133337/3757 |
| 专题 | 海岸带生物学与生物资源利用重点实验室_海岸带生物学与生物资源保护实验室 |
| 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. |
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