Recombinant Galectin-1 Recognizes Mucin and Epithelial Cell Surface Glycocalyces of Gastrointestinal Tract
Autor: | Yasuhiro Hirakawa, Kojiro Wasano |
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Rok vydání: | 1997 |
Předmět: |
0301 basic medicine
Histology Galectin 1 Glycoconjugate Biology Glycocalyx Polymerase Chain Reaction Epithelium 03 medical and health sciences Intestinal mucosa Lectins otorhinolaryngologic diseases Animals Rats Wistar Galectin chemistry.chemical_classification Gastrointestinal tract Binding Sites 030102 biochemistry & molecular biology Mucin Mucins Recombinant Proteins Extracellular Matrix Rats Cell biology Hemagglutinins 030104 developmental biology Biochemistry chemistry Galectin-1 Gastric acid Anatomy Poly A Digestive System |
Zdroj: | Journal of Histochemistry & Cytochemistry. 45:275-283 |
ISSN: | 1551-5044 0022-1554 |
DOI: | 10.1177/002215549704500212 |
Popis: | 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. |
Databáze: | OpenAIRE |
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