کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8499562 | 1553627 | 2014 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Molecular cloning and characterization of cathepsin L from freshwater mussel, Cristaria plicata
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
علوم آبزیان
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Molecular cloning and characterization of cathepsin L from freshwater mussel, Cristaria plicata Molecular cloning and characterization of cathepsin L from freshwater mussel, Cristaria plicata](/preview/png/8499562.png)
چکیده انگلیسی
Cathepsin L is one of the crucial enzyme superfamilies and involved in the immune responses. The Cathepsin L cDNA and genome of Cristaria plicataï¼CpCLï¼ was cloned from the hemocytes using degenerate primers by the rapid amplification of cDNA ends (RACE) PCR. The genomic DNA was 9353Â bp long and had a total of six introns and seven exons. The full-length cDNA of CpCL was 1144Â bp, the cDNA contained a 5â² untranslated region (UTR) of 34 nucleotides, the 3â² UTR of 108Â bp with a canonical polyadenylation signal sequence AATAAA and a polyA tail, and an open reading frame (ORF) of 1002Â bp, encoding 333 amino acid residues with 37.65Â 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, and 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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Fish & Shellfish Immunology - Volume 40, Issue 2, October 2014, Pages 446-454
Journal: Fish & Shellfish Immunology - Volume 40, Issue 2, October 2014, Pages 446-454
نویسندگان
Xiaojuan Hu, Xiangping Hu, Baoqing Hu, Chungen Wen, Yanhai Xie, Dan Wu, Zhiying Tao, Aihua Li, Qian Gao,