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- Title
Molecular cloning and characterization of cathepsin F from olive flounder Paralichthys olivaceus.
- Authors
Kim, Young-Ok; Park, Eun-Mi; Nam, Bo-Hye; Kong, Hee Jeong; Kim, Woo-Jin; Lee, Sang-Jun; Choi, Tae-Jin
- Abstract
A cysteine protease of the papain family was identified by dbEST-database search of olive flounder. A 2,084 kb full-length cDNA encoding a predicted polypeptide of 475 amino acids was sequenced. The flounder cathepsin F exhibits a domain structure typical for papain-like cysteine proteases, a 17 amino acid N-terminal hydrophobic signal sequence followed by an extraordinarily long propeptide of 244 amino acids and the domain of the mature protease comprising 213 amino acids. The mature region contains all features characteristic of a papain-like cysteune protease, including the highly conserved cysteine, histidine and asparagine residues of the 'catalytic triad'. The cathepsin F protein showed 46-58% amino acid sequence identity with other known cathepsin F sequences. An in vivo expression study showed that cathepsin F mRNA was expressed predominantly in brain, liver, eye and heart, and moderately in other tissues. The accumulation of cathepsin F mRNA in immune related-tissues determined by RT-PCR showed the increase after bacterial challenge. In addition, its expression was detected early stage of development. This expression pattern suggests that flounder cathepsin F has been implicated in the defense, immune, growth and reproduction regulation.
- Publication
FASEB Journal, 2008, Vol 22, p199
- ISSN
0892-6638
- Publication type
Article
- DOI
10.1096/fasebj.22.2_supplement.199