Structure and distribution of N-linked oligosaccharide chains on various domains of mouse tumour laminin.

Asparagine-linked oligosaccharides were liberated from laminin and some of its fragments by hydrazinolysis, and after purification characterized by exoglycosidase digestions. This demonstrated the presence of nine forms of complex oligosaccharide chains, which differed in antennary and oligolactosamine structure, and of small amounts of high-mannose-type oligosaccharides. Additional variations were found with regard to substitutions by terminal alpha-galactose and sialic acid residues. Each of the various laminin fragments showed a unique but less complex repertoire of carbohydrate structures. These fragments also differed in mass, carbohydrate content, localization within the laminin molecule and functional activities such as cell-binding (fragments 1 and 6) and heparin- and collagen-binding (fragments 3 and 4). Fragment 7 with a particularly high carbohydrate content (72%) also showed the highest complexity of tri- and tetra-antennary structures. Further differences between the fragments were detected with human antibodies against the Gal alpha 1-3Gal epitope, which was expressed in either a high-affinity or a low-affinity form. Such differences in carbohydrate structure of topologically distinct laminin domains may have implications for their functions and in the regulation of post-translational modification events.