Glycan-Binding Profile and Cell Adhesion Activity of American Bullfrog (Rana catesbeiana) Oocyte Galectin-1

The glycan-binding profile of a beta-galactoside-binding 15 kDa lectin (Galectin-1) purified from the oocytes of the American bullfrog, Rana catesbeiana, was studied using 61 pyridyl-aminated oligosaccharides by frontal affinity chromatography. Human blood type-A-hexasaccharide (GalNAc alpha 1-3(Fuc alpha 1-2)Gal beta 1-4GlcNAc beta 1-4Gal beta 1-4Glc) was found to exhibit the strongest ligand binding to the galectin while Forssman antigen (GalNAc alpha 1-3GalNAc beta 1-3Gal alpha 1-4Gal beta 1-4Glc) and type-A-tetrasaccharide (GalNAc alpha 1-3(Fuc alpha 1-2)Gal beta 1-4GlcNAc beta 1-4Glc) were also extensively recognized. The kinetics of affinity of galectin-1 to type-A oligosaccharide was analysed by surface plasmon resonance using neoglycoprotein with type-A oligosaccharides. R. catesbeiana oocyte galectin adhered to human rhabdomyosarcoma cells dose dependently and the activity was specifically cancelled by the neoglycoprotein. It was concluded that galectin-1 from R. catesbeiana oocytes possesses different and rare glycan-binding properties from typical members in galectin family.