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KMID : 0380220070400040532
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Journal of Biochemistry and Molecular Biology
2007 Volume.40 No. 4 p.532 ~ p.538
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Identification of a Functionally Relevant Signal Peptide of Mouse Ficolin A
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Kwon Sang-Hoon
Kim Min-Soo
Kim Dong-Bum
Lee Keun-Wook
Choi Soo-Young
Park Jin-Seu
Kim Yeon-Hyang
Lee Young-Hee
Kwon Hyung-Joo
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Abstract
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Mouse ficolin A is a plasma protein with lectin activity, and plays a role in host defense by binding carbohydrates, especially GlcNAc, on microorganisms. The ficolin A subunit consists of an N-terminal signal peptide, a collagen-like domain, and a C-terminal fibrinogen-like domain. In this study, we show that ficolin A can be synthesized and oligomerized in a cell and secreted into culture medium. We also identify a functionally relevant signal peptide of ficolin A by using MS/MS analysis to determine the N-terminal sequence of secreted ficolin A. When the signal peptide of mouse ficolin A was fused with enhanced green fluorescent protein (EGFP), EGFP was released into HEK 293 cell medium, suggesting that the signal peptide can efficiently direct ficolin A secretion. Moreover, our results suggest that the signal peptide of ficolin A has potential application for the production of useful secretory proteins.
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KEYWORD
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EGFP, Ficolin A, Fusion protein, Secretion, Signal peptide
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