Molecular characterization and expression analysis of Cathepsin B and L cysteine proteases from rock bream (Oplegnathus fasciatus)
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Title
- Molecular characterization and expression analysis of Cathepsin B and L cysteine proteases from rock bream (Oplegnathus fasciatus)
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Author(s)
- Whang, Ilson; De Zoysa, Mahanama; Nikapitiya, Chamilani; Lee, Youngdeuk; Kim, Yucheol; Lee, Sukkyoung; Oh, Chulhong; Jung, Sung-Ju; Oh, Myung-Joo; Choi, Cheol Young; Yeo, Sang-Yeob; Kim, Bong-Seok; Kim, Se-Jae; Lee, Jehee
- KIOST Author(s)
- Oh, Chul Hong(오철홍)
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Alternative Author(s)
- 오철홍
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Publication Year
- 2011-03
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Abstract
- Cathepsins are lysosomal cysteine proteases of the papain family that play an important role in intracellular protein degradation and turn over within the lysosomal system. In the present study, full-length sequences of cathepsin B (RbCathepsin B) and L (RbCathepsin L) were identified after transcriptome sequencing of rock bream Oplegnathus fasciatus mixed tissue cDNA. Cathepsin B was composed of 330 amino acid residues with 36 kDa predicted molecular mass. RbCathepsin L contained 336 amino acid residues encoding for a 38 kDa predicted molecular mass protein. The sequencing analysis results showed that both cathepsin B and L contain the characteristic papain family cysteine protease signature and active sites for the eukaryotic thiol proteases of cysteine, asparagine and histidine. In addition, RbCathepsin L contained EF hand Ca2+ binding and cathepsin propeptide inhibitor domains. The rock bream cathepsin B and L showed the highest amino acid identity of 90 and 95% to Lutjanus argentimaculatus cathepsin B and Lates calcarifer cathepsin L, respectively. By phylogenetic analysis, cathepsin B and L exhibited a high degree of evolutionary relationship to respective cathepsin family members of the papain superfamily. Quantitative real-time RT-PCR analysis results confirmed that the expression of cathepsin B and L genes was constitutive in all examined tissues isolated from un-induced rock bream. Moreover, activation of RbCathepsin B and L mRNA was observed in both lipopolysaccharide (LPS) and Edwardsiella tarda challenged liver and blood cells, indicating a role of immune response in rock bream. (C) 2010 Elsevier Ltd. All rights reserved.
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ISSN
- 1050-4648
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URI
- https://sciwatch.kiost.ac.kr/handle/2020.kiost/3911
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DOI
- 10.1016/j.fsi.2010.12.022
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Bibliographic Citation
- FISH & SHELLFISH IMMUNOLOGY, v.30, no.3, pp.763 - 772, 2011
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Publisher
- ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
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Subject
- TURBOT SCOPHTHALMUS-MAXIMUS; EDWARDSIELLA-TARDA GHOSTS; GENE-EXPRESSION; PARALICHTHYS-OLIVACEUS; SEQUENCE ALIGNMENT; IDENTIFICATION; PROTEIN; ENZYME; VIRUS; CELLS
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Keywords
- Cathepsin; Lysosomal cysteine proteases; Papain superfamily; Rock bream; Oplegnathus fasciatus
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Type
- Article
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Language
- English
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Document Type
- Article
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