Multiplicity, structures, and endocrine and exocrine natures of eel fucose-binding lectins.

作者: Shinji Honda , Masahide Kashiwagi , Kentaro Miyamoto , Yoshio Takei , Shigehisa Hirose

DOI: 10.1074/JBC.M002337200

关键词:

摘要: Lectins, a group of proteins that bind to cell surface carbohydrates and play important roles in innate immunity, are widely used experimentally distinguish types induce proliferation. Eel serum lectins have been useful as anti-H hemagglutinins also lectin histochemistry fucose-binding (fucolectins), but their structures not determined. Here we report the primary sites synthesis eel fucolectins. fucolectins were separated by two-dimensional gel electrophoresis sequenced. cDNA cloning, based on amino acid sequence information, Northern blot analysis indicated 1) secretory unique among lectins, exhibiting only weak similarities frog pentraxin, horseshoe crab tachylectin-4, fly fw protein; 2) there at least seven closely related members; 3) messages abundantly expressed liver significant levels gill intestine. The lectin-producing hepatic cells identified immunostaining; gill, exocrine mucous stained, suggesting derive from liver. Using culture hepatocytes, message shown be increased lipopolysaccharide, role for host defense. SDS-polyacrylamide showed SDS-resistant tetrameric structure consisting two disulfide-linked dimers.

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