Binding specificity of a baby hamster kidney lectin for H type I and II chains, polylactosamine glycans, and appropriately glycosylated forms of laminin and fibronectin.

摘要: Abstract The carbohydrate binding specificity of Mr = 30,000 lectin (CBP30) from baby hamster kidney (BHK) cells has been studied by inhibition the radiolabeled to asialofetuin-Sepharose using model oligosaccharides and glycopeptides. CBP30 binds type I or II Gal beta(1----3(4))GlcNAc chains but not Gal(beta 1----3)GalNAc. inhibitory potency straight chain polylactosamine structures complex-type branched glycans is increased in proportion number 1----3(4)) units present. Fucosylation sialylation terminal galactose residues further substitution (alpha 1----3)-linked N-acetylgalactosamine does affect whereas penultimate N-acetylglucosamine residue drastically reduces binding. Thus, blood group A, H structures, shows high affinity Lex, Lea, Leb bind poorly. murine Engelbreth-Holm-Swarm (EHS) tumor laminin human amniotic fluid fibronectin plasma fibronectin. Binding involves as well tri- tetraantennary present EHS absent Proteolytic fragments (E1X/Nd, P1, E8, E3) CBP30, only fragment E8 supports attachment spreading BHK cells. cell adhesion was disturbed CBP30-specific antibodies, at relatively concentrations (45 micrograms/ml) inhibited partially on laminin.