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题名: Molecular cloning and characterization of cathepsin L from freshwater mussel, Cristaria plicata
作者: Hu, Xiaojuan1; Hu, Xiangping1; Hu, Baoqing1; Wen, Chungen1; Xie, Yanhai1; Wu, Dan1; Tao, Zhiying1; Li, Aihua2; Gao, Qian2
关键词: Cristaria plicata ; Cathepsin L ; Molecular clone ; Genome ; Expression
刊名: FISH & SHELLFISH IMMUNOLOGY
发表日期: 2014-10-01
DOI: 10.1016/j.fsi.2014.07.005
卷: 40, 期:2, 页:446-454
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology ; Life Sciences & Biomedicine
类目[WOS]: Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
研究领域[WOS]: Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
英文摘要: Cathepsin L is one of the crucial enzyme superfamilies and involved in the immune responses. The Cathepsin L cDNA and genome of Cristaria plicata (CpCL) was cloned from the hemocytes using degenerate primers by the rapid amplification of cDNA ends (RACE) PCR. The genomic DNA was 9353 bp long and had a total of six introns and seven exons. The full-length cDNA of CpCL was 1144 bp, the cDNA contained a 5' untranslated region (UTR) of 34 nucleotides, the 3' UTR of 108 bp with a canonical polyadenylation signal sequence AATAAA and a polyA tail, and an open reading frame (ORF) of 1002 bp, encoding 333 amino acid residues with 37.65 kDa predicted molecular weight. The theoretical isoelectric point was 8.61. The prepro-cathepsin L was consisted of a typical signal peptide (Met1-Gly20), a pro-region peptide (Leu21-Glu116) and a mature peptide (Tyr117-Val333). Many members of the papain family possessed of a proline residue at position 2 in the mature enzymem, this was also observed in CpCL. The preproprotein included an oxyanion hole (Gln 135), the active center formed by Cys141, His280 and Asn 300, the potential N-glycosylation site (Asn38, Asn 113 and Asn 272) and the conserved GCXGG motifs, which was characteristic of cathepsin, the conserved ERWNIN and GNFD motifs, which were characteristic for cathepsin L. Homology analysis revealed that the CpCL shared 49-87% identity to other known cathepsin L sequences. The phylogenetic tree showed that the CpCL clustered with the invertebrate cathepsin L cysteine proteases, and was closely related to the cathepsin L of Hyriopsis cumingii. The expression of CpCL mRNA was detected in hepatopancreas, hemocytes, mantle, gills and adductor muscle, Mid the higher expression level was in hepatopancreas. After A. hydrophila stimulation, the expression of the CpCL mRNA was up-regulated in hemocytes and hepatopancreas, and the expression level was significantly lower in gill than one after PBS challenge group. (C) 2014 Elsevier Ltd. All rights reserved.
关键词[WOS]: CYSTEINE PROTEASES ; GENE-EXPRESSION ; CAENORHABDITIS-ELEGANS ; FUNCTIONAL EXPRESSION ; SCHISTOSOMA-MANSONI ; FASCIOLA-HEPATICA ; PROTEINASES ; EMBRYOGENESIS ; OYSTER ; IDENTIFICATION
语种: 英语
WOS记录号: WOS:000343381100013
ISSN号: 1050-4648
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内容类型: 期刊论文
URI标识: http://ir.ihb.ac.cn/handle/342005/20332
Appears in Collections:鱼类生物学及渔业生物技术研究中心_期刊论文

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作者单位: 1.Nanchang Univ, Sch Life Sci & Food Engn, Inst Life Sci, Nanchang 330031, Peoples R China
2.Chinese Acad Sci, Inst Hydrobiol, State Key Lab Freshwater Ecol & Biotechnol, Wuhan 430072, Hubei Province, Peoples R China

Recommended Citation:
Hu, Xiaojuan; Hu, Xiangping; Hu, Baoqing; Wen, Chungen; Xie, Yanhai; Wu, Dan; Tao, Zhiying; Li, Aihua; Gao, Qian.Molecular cloning and characterization of cathepsin L from freshwater mussel, Cristaria plicata,FISH & SHELLFISH IMMUNOLOGY,2014,():
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