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Altered glycosylation of β 1 integrins associated with reduced adhesiveness to fibronectin and laminin

1993; Wiley; Volume: 53; Issue: 1 Linguagem: Inglês

10.1002/ijc.2910530118

1097-0215

Takehiro Kawano, S. Takasaki, T. Tao, Akira Kobata,

Monoclonal and Polyclonal Antibodies Research

Abstract The carbohydrate structures of the β 1 integrins obtained from a mouse metastatic melanoma 816 FI and its weakly metastatic wheat‐germ agglutinin‐resistant mutant Wa4‐bI were studied comparatively. The results indicated that the integrins from both cells contain high mannose‐type and bi‐, tri‐ and tetra‐antennary complex‐type sugar chains. No significant difference was found in the outer chain branching between both integrins, but sialylation of the sugar chains of the mutant's integrin was markedly decreased and almost all the outer chain moieties of tri‐ and tetra‐antennary oligosaccharides of the mutant's integrin were fucosylated, resulting in the formation of X‐antigenic determinants, GalβI → 4 (Fucα → 3) GlcNAc. In contrast, the integrin from parental cell contained no X‐antigenic determinant. These structural differences found in the integrin are thought to account for the reduction in the metastatic potential of the mutant which also shows reduced adhesion to fibronectin and laminin as compared with the parental cell.