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

doi:10.1007/s11033-009-9534-2

IOCAS-IR > 实验海洋生物学重点实验室

	Identification of a cathepsin D potentially involved in H2A cleavage from scallop Chlamys farreri
	Li, Chenghua 1; Zhang, Huan 2; Li, Ling 2; Song, Linsheng 2
	2010-03-01
发表期刊	MOLECULAR BIOLOGY REPORTS
卷号	37 期号:3 页码:1451-1460
文章类型	Article
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.
关键词	Chlamys Farrei Cathepsin d Tissue Expression Innate Immunity
DOI	10.1007/s11033-009-9534-2
收录类别	SCI
语种	英语
WOS记录号	WOS:000274212500039
引用统计	被引频次：6[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/337002/32818
专题	实验海洋生物学重点实验室
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.

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