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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Sako, Miyuki Mizumura, Hikaru Oda, Toshio Kawabata, Shun-ichiro Shiga, Takafumi Shibata, Toshio Kobayashi, Yuki Maenaka, Katsumi Koshiba, Takumi |
| Description | Author Affiliation: Kobayashi Y ( From the Graduate School of Systems Life Sciences.); Shiga T ( From the Graduate School of Systems Life Sciences.); Shibata T ( Department of Biology, Faculty of Sciences, and Institute for Advanced Study, Kyushu University, Fukuoka 812-8581.); Sako M ( the Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, and.); Maenaka K ( the Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, and.); Koshiba T ( From the Graduate School of Systems Life Sciences, Department of Biology, Faculty of Sciences, and.); Mizumura H ( the LAL Research and Development Group, Seikagaku Corporation, Higashiyamato, Tokyo 207-0021, Japan.); Oda T ( the LAL Research and Development Group, Seikagaku Corporation, Higashiyamato, Tokyo 207-0021, Japan.); Kawabata S ( From the Graduate School of Systems Life Sciences, Department of Biology, Faculty of Sciences, and skawascb@kyudai.jp.) |
| Abstract | Factor C, a serine protease zymogen involved in innate immune responses in horseshoe crabs, is known to be autocatalytically activated on the surface of bacterial lipopolysaccharides, but the molecular mechanism of this activation remains unknown. In this study, we show that wild-type factor C expressed in HEK293S cells exhibits a lipopolysaccharide-induced activity equivalent to that of native factor C. Analysis of the N-terminal addition, deletion, or substitution mutants shows that the N-terminal Arg residue and the distance between the N terminus and the tripartite of lipopolysaccharide-binding site are essential factors for autocatalytic activation, and that the positive charge of the N terminus may interact with an acidic amino acid(s) of the molecule to convert the zymogen into an active form. Chemical cross-linking experiments indicate that the N terminus is required to form a complex of the factor C molecules in a sufficiently close vicinity to be chemically cross-linked on the surface of lipopolysaccharides. We propose a molecular mechanism of the autocatalytic activation of the protease zymogen on lipopolysaccharides functioning as a platform to induce specific protein-protein interaction between the factor C molecules. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 37 |
| Volume Number | 289 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2014-09-12 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Arthropod Proteins Metabolism Enzyme Precursors Genetics Horseshoe Crabs Enzymology Immunity, Innate Serine Proteases Amino Acid Sequence Animals Biosynthesis Gene Expression Regulation, Enzymologic Drug Effects HEK293 Cells Lipopolysaccharides Toxicity Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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