1. Molecular and functional characterizations of a Kunitz-type serine protease inhibitor FcKuSPI of the shrimp Fenneropenaeus chinensis.
- Author
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Kong, Hee Jeong, Lee, Ye-Ji, Park, In-Suk, Lee, Won Woo, Kim, Young-Ok, Nam, Bo-Hye, Kim, Woo-Jin, Jung, Hyungtaek, Jeon, You-Jin, An, Cheul Min, and Lee, Sang-Jun
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SERINE proteinase inhibitors , *SHRIMPS , *PENAEUS chinensis , *IMMUNE response in fishes , *ANTISENSE DNA , *GENE libraries - Abstract
Abstract: Serine proteinase inhibitors play important and diverse roles in biological processes such as coagulation, defense mechanisms, and immune responses. Here, we identified and characterized a Kunitz-type proteinase inhibitor, designated FcKuSPI, of the BPTI/Kunitz family of serine proteinase inhibitors from the hemocyte cDNA library of the shrimp Fenneropenaeus chinensis. The deduced amino acid sequence of FcKuSPI comprises 80 residues with a putative signal peptide of 15 amino acids. The predicted molecular weight of the mature peptide is 7.66 kDa and its predicted isoelectric point is 8.84. FcKuSPI includes a Kunitz domain containing six conserved cysteine residues that are predicted to form three disulfide bonds. FcKuSPI shares 44–53% homology with BPTI/Kunitz family members from other species. FcKuSPI mRNA was expressed highly in the hemocytes and moderately in muscle in healthy shrimp. Recombinant FcKuSPI protein demonstrated anti-protease activity against trypsin and anticoagulant activity against citrated human plasma in a dose-dependent manner in in vitro assays. [Copyright &y& Elsevier]
- Published
- 2013
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