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Molecular cloning, characterization and expression analysis of cathepsin O in silkworm Bombyx mori related to bacterial response

Cathepsins are the main members of the cysteine family and play important roles in immune response in vertebrates. The O of ( O) was cloned from the hemocytes by the rapid amplification of cDNA ends (RACE). The genomic DNA was 6131 bp long with a total of six exons and five introns. Its pre-mRNA was... Full description

Journal Title: Molecular Immunology August 2015, Vol.66(2), pp.409-417
Main Author: Zhang, Kui
Other Authors: Su, Jingjing , Chen, Siyuan , Yu, Shuang , Tan, Juan , Xu, Man , Liang, Hanghua , Zhao, Yuzu , Chao, Huijuan , Yang, Liqun , Cui, Hongjuan
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0161-5890 ; E-ISSN: 1872-9142 ; DOI: 10.1016/j.molimm.2015.04.008
Link: https://www.sciencedirect.com/science/article/pii/S0161589015003673
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recordid: elsevier_sdoi_10_1016_j_molimm_2015_04_008
title: Molecular cloning, characterization and expression analysis of cathepsin O in silkworm Bombyx mori related to bacterial response
format: Article
creator:
  • Zhang, Kui
  • Su, Jingjing
  • Chen, Siyuan
  • Yu, Shuang
  • Tan, Juan
  • Xu, Man
  • Liang, Hanghua
  • Zhao, Yuzu
  • Chao, Huijuan
  • Yang, Liqun
  • Cui, Hongjuan
subjects:
  • Silkworm
  • Molecular Cloning
  • Cathepsin O
  • 20-Ecdysone
  • Infection
  • Medicine
  • Biology
  • Chemistry
ispartof: Molecular Immunology, August 2015, Vol.66(2), pp.409-417
description: Cathepsins are the main members of the cysteine family and play important roles in immune response in vertebrates. The O of ( O) was cloned from the hemocytes by the rapid amplification of cDNA ends (RACE). The genomic DNA was 6131 bp long with a total of six exons and five introns. Its pre-mRNA was spliced to generate two spliceosomes. By comparisons with other reported cathepsins O, it was concluded that the identity between them ranged from 29 to 39%. Expression analysis indicated that O was specific-expressed in hemocytes, and highly expressed at the 4th molting and metamorphosis stages. Immunofluorescence assay and qRT-PCR showed that BmCathepsin O was expressed in granulocytes and plasmatocytes. Interestingly, O was significantly up-regulated after stimulated by 20-hydroxyecdysone (20-E) in vivo, which suggested that may be regulated by 20E. Moreover, activation of O was also observed in hemocytes challenged by , indicating its potential involvement in the innate immune system of silkworm, . In summary, our studies provide a new insight into the functional features of Cathepsin O.
language: eng
source:
identifier: ISSN: 0161-5890 ; E-ISSN: 1872-9142 ; DOI: 10.1016/j.molimm.2015.04.008
fulltext: fulltext
issn:
  • 0161-5890
  • 01615890
  • 1872-9142
  • 18729142
url: Link


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titleMolecular cloning, characterization and expression analysis of cathepsin O in silkworm Bombyx mori related to bacterial response
creatorZhang, Kui ; Su, Jingjing ; Chen, Siyuan ; Yu, Shuang ; Tan, Juan ; Xu, Man ; Liang, Hanghua ; Zhao, Yuzu ; Chao, Huijuan ; Yang, Liqun ; Cui, Hongjuan
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subjectSilkworm ; Molecular Cloning ; Cathepsin O ; 20-Ecdysone ; Infection ; Medicine ; Biology ; Chemistry
descriptionCathepsins are the main members of the cysteine family and play important roles in immune response in vertebrates. The O of ( O) was cloned from the hemocytes by the rapid amplification of cDNA ends (RACE). The genomic DNA was 6131 bp long with a total of six exons and five introns. Its pre-mRNA was spliced to generate two spliceosomes. By comparisons with other reported cathepsins O, it was concluded that the identity between them ranged from 29 to 39%. Expression analysis indicated that O was specific-expressed in hemocytes, and highly expressed at the 4th molting and metamorphosis stages. Immunofluorescence assay and qRT-PCR showed that BmCathepsin O was expressed in granulocytes and plasmatocytes. Interestingly, O was significantly up-regulated after stimulated by 20-hydroxyecdysone (20-E) in vivo, which suggested that may be regulated by 20E. Moreover, activation of O was also observed in hemocytes challenged by , indicating its potential involvement in the innate immune system of silkworm, . In summary, our studies provide a new insight into the functional features of Cathepsin O.
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