Molecular characterization and expression analysis of Cathepsin B and L cysteine proteases from rock bream (Oplegnathus fasciatus) SCIE SCOPUS

Cited 43 time in WEB OF SCIENCE Cited 43 time in Scopus
Title
Molecular characterization and expression analysis of Cathepsin B and L cysteine proteases from rock bream (Oplegnathus fasciatus)
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)
Publication Year
2011-03
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.
ISSN
1050-4648
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/3911
DOI
10.1016/j.fsi.2010.12.022
Bibliographic Citation
FISH & SHELLFISH IMMUNOLOGY, v.30, no.3, pp.763 - 772, 2011
Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
Subject
TURBOT SCOPHTHALMUS-MAXIMUS; EDWARDSIELLA-TARDA GHOSTS; GENE-EXPRESSION; PARALICHTHYS-OLIVACEUS; SEQUENCE ALIGNMENT; IDENTIFICATION; PROTEIN; ENZYME; VIRUS; CELLS
Keywords
Cathepsin; Lysosomal cysteine proteases; Papain superfamily; Rock bream; Oplegnathus fasciatus
Type
Article
Language
English
Document Type
Article
Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
Related Researcher
Research Interests

Recombinant protein,Marine microorganisms,Functional proteins,재조합단백질,해양미생물,기능성단백질

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