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Recombinant Galectin-1 Recognizes Mucin and Epithelial Cell Surface Glycocalyces of Gastrointestinal Tract
Kojiro Wasanoa and Yasuhiro Hirakawaaa Department of Anatomy and Cell Biology, Faculty of Medicine, Kyushu University, Fukuoka, Japan
Correspondence to: Kojiro Wasano, Dept. of Anatomy and Cell Biology, Faculty of Medicine, Kyushu Univ., Fukuoka 812, Japan.
Rat gastrointestinal (GI) tract is rich source of galectins, a family of mammalian galactoside-binding lectins. To determine which tissue component is the relevant glycoconjugate ligand for the galectins, we produced recombinant galectin-1 and surveyed its binding sites on tissue sections of rat GI tract. Mucin and epithelial surface glycocalyces of both gastric and intestinal mucosa were intensely stained. This finding raises the possibility that some GI tract galectins known to be secreted by the epithelia may recognize these glycoconjugates and crosslink them into a macromolecular mass. This galectin-ligand complex may play a role in protecting the epithelial surface against luminal contents such as gastric acid, digestive enzymes, and foreign organisms. (J Histochem Cytochem 45:275-283, 1997)
Key Words: galectins, rat, gastrointestinal tract, recombinant protein, glycoconjugates, mucosal defense, mucin, glycocalyx
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