The localization of lectin-binding sites on Schwann cell basal lamina

Abstract

Basal laminae were separated from Schwann cells of mouse sciatic nerves by Bonification, and the distributions of lectin-binding sites were demonstrated by electron microscopy using ferritin-conjugated lectins. Only three out of the 11 lectins examined were bound to the basal laminae of Schwann cells: they wereRicinus communis agglutinin-I (RCA-I),Canavalia ensiformis agglutinin (ConA) andTriticum vulgaris agglutinin (wheat germ agglutinin, WGA). It was notable that WGA was bound more densely to the cellular side than to the interstitial side, whereas in the case of RCA-I and ConA there were no differences in the binding density on the two sides of the basal lamina. These results indicate that there are sugar residues such as β-d-galactose, α-d-mannose, α-d-glucose and β(1–4) linkedN-acetyl-d-glucosamine in the Schwann cell basal laminae. The first three sugar residues are almost equally densely distributed on the cellular and interstitial sides of the basal laminae, whereas β(1–4) linkedN-acetyl-d-glucosamine is more densely distributed on the cellular than on the interstitial side. This result suggests that the basal lamina has a polarity in chemical composition between the cellular and interstitial sides. These findings are discussed in the context of the preferential attachment of regenerating axons to the cellular side of the Schwann cell basal laminae.