cDNA Cloning of a Mannose-Binding Lectin-Associated Serine Protease(MASP) Gene from Hagfish(Eptatretus burgeri)(Immunology)
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概要
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Hagfish, agnathan cyclostome, is the most primitive extant vertebrate and its complement (C) system seems to be a primordial system in comparison with a well-developed C system in gnathostome vertebrates. From a phylogenic perspective of defense mechanisms, we have isolated complement C3 from the serum of hagfish (Eptatretus burgeri). In this study, we first attempted to identify a hagfish Bf or C2 as a C3 convertase by RT-PCR using degenerative primers designed on the basis of the conserved amino acid stretches among the several kinds of serine proteases. Contrary to our expectation, homology search of cloned RT-PCR product suggested that there was a partial cDNA encoding the homologue of neither Bf nor C2 but a mannose-binding lectin-associated serine protease (MASP). Analyses of a full-length cDNA clone isolated from a hagfish liver cDNA library by using the partial cDNA as a probe indicated that this cDNA encoded hagfish MASP 1. This evidence strongly suggests that the hagfish defends itself against pathogens at least by the complement system composed of lectin pathway.
- 社団法人日本動物学会の論文
- 2005-08-25
著者
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Fujii Tamotsu
Department Of Health Sciences Faculty Of Human Culture And Science Prefectural University Of Hiroshi
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Fujii Tamotsu
Department Of Health Science Faculty Of Human Life And Environmental Science Hiroshima Women's
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Takamune Kazufumi
Department Of Biological Science Faculty Of Science Kumamoto University
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Song Liqiu
Department Of Health Sciences Faculty Of Human Culture And Science Prefectural University Of Hiroshi
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SUGAWARA Yoshiaki
Department of Health Science, Prefectural University of Hiroshima
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Takamune Kazufumi
Department Of Materials And Life Science Graduate School Of Science And Technology Kumamoto Universi
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Sugawara Yoshiaki
Department Of Health Sciences Faculty Of Human Culture And Science Prefectural University Of Hiroshi
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Sugawara Yoshiaki
Department Of Health Science Faculty Of Human Life And Environmental Science Hiroshima Women's
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