XB-ART-10575J Biol Chem. October 20, 2000; 275 (42): 33151-7.
Multiplicity, structures, and endocrine and exocrine natures of eel fucose-binding lectins.
Lectins, a group of proteins that bind to cell surface carbohydrates and play important roles in innate immunity, are widely used experimentally to distinguish cell types and to induce cell proliferation. Eel serum lectins have been useful as anti-H hemagglutinins and also in lectin histochemistry as fucose-binding lectins (fucolectins), but their structures have not been determined. Here we report the primary structures and the sites of synthesis of eel fucolectins. Eel serum fucolectins were separated by two-dimensional gel electrophoresis and sequenced. cDNA cloning, based on the amino acid sequence information, and Northern blot analysis indicated that 1) the fucose-binding lectins are secretory proteins and have unique structures among the lectins, exhibiting only weak similarities to frog pentraxin, horseshoe crab tachylectin-4, and fly fw protein; 2) there are at least seven closely related members; and 3) their messages are abundantly expressed in the liver and in significant levels in the gill and intestine. The lectin-producing hepatic cells were identified by immunostaining; in the gill, exocrine mucous cells were stained, suggesting that serum fucolectins derive from the liver. Using primary culture of eel hepatocytes, the message levels were shown to be increased by lipopolysaccharide, suggesting a role for fucolectins in host defense. SDS-polyacrylamide gel electrophoresis analysis showed that eel fucolectins have a SDS-resistant tetrameric structure consisting of two disulfide-linked dimers.
PubMed ID: 10924498
Article link: J Biol Chem.