Two domains of rat galectin-4 bind to distinct structures of the intercellular borders of colorectal epithelia.

Galectin-4 (G4) is a member of a family of soluble galactoside-binding lectins found in various mammalian tissues. To determine the function of this protein in colorectal tissue, we separately produced the N- and C-terminal carbohydrate binding domains (CBD) of rat G4 as a recombinant glutathione S-transferase (GST) fusion protein (G4-N and G4-C) and examined the tissue binding site(s) of each CBD by light and electron microscopy (LM and EM). At the LM level, both fusion proteins stained the intercellular borders of the surface-lining epithelial cells of colorectal mucosa. At the EM level, two proteins recognized spatially close but distinct subcellular structures. G4-N stained electron-lucent flocculent substances freely located in the intercellular spaces, whereas G4-C bound to the lateral cell membranes demarcating the intercellular spaces. These findings suggest that colorectal G4 may be involved in crosslinking the lateral cell membranes of the surface-lining epithelial cells, thereby reinforcing epithelial integrity against mechanical stress exerted by the bowel lumen. (J Histochem Cytochem 47:75-82, 1999)