Cloning and expression of a novel serine protease from Japanese flounder, Paralichthys olivaceus

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• 作者：Jee Youn Hwang ; Ikuo Hirono ; Takashi Aoki
• 关键词：Japanese flounder ; Serine protease ; In situ hybridization ; Granulocytes ; Neutrophil
• 刊名：Developmental and Comparative Immunology
• 出版年：2007
• 出版时间：2007
• 年：2007
• 卷：31
• 期：6
• 页码：587-595
• 全文大小：610 K

文摘

Two different cDNA clones of Japanese flounder (types I-1 and I-2) with lengths of 1096 and 1572 bp, respectively, were found to encode the same serine protease consisting of 244 identical amino acid residues with three putative N-glycosylation sites, an 18-amino acid signal peptide and a 2-amino acid activation peptide. The amino acid sequence of the Japanese flounder serine protease shares 39–44 % identity to known hematopoietic serine proteases. Genomic analysis showed that two different clones were alternatively spliced from the same gene. A phylogenetic tree analysis showed that the Japanese flounder serine protease clustered with a hypothetical fugu protein and this cluster belonged to the neutrophil serine protease family cluster, which includes myeloblastin, N-elastase, and azurocidin. Expression of the Japanese flounder serine protease gene was observed to be up-regulated in head kidney cells after infection with Hirame rhabdovirus and LPS induction. In situ hybridization indicated that cells expressing Japanese flounder serine protease are different from CD8⁺ and immunoglobulin⁺ cells.