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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Identification of a Functionally Relevant Signal Peptide of Mouse Ficolin A

  • Kwon, Sang-Hoon (Department of Microbiology, College of Medicine, Hallym University) ;
  • Kim, Min-Soo (Department of Microbiology, College of Medicine, Hallym University) ;
  • Kim, Dong-Bum (Center for Medical Science Research, College of Medicine, Hallym University) ;
  • Lee, Keun-Wook (Center for Medical Science Research, College of Medicine, Hallym University) ;
  • Choi, Soo-Young (Department of Biomedical Science, Hallym University) ;
  • Park, Jin-Seu (Department of Biomedical Science, Hallym University) ;
  • Kim, Yeon-Hyang (Department of Biomedical Science, Hallym University) ;
  • Lee, Young-Hee (Department of Biochemistry, College of Natural Sciences, Chungbuk National University) ;
  • Kwon, Hyung-Joo (Department of Microbiology, College of Medicine, Hallym University)
  • Published : 2007.07.31
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Abstract

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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References

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