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Altered glycosylation of β 1 integrins associated with reduced adhesiveness to fibronectin and laminin
Author(s) -
Kawano Takehiro,
Takasaki Seiichi,
Tao TienWen,
Kobata Akira
Publication year - 1993
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910530118
Subject(s) - integrin , laminin , fibronectin , mutant , wheat germ agglutinin , cell adhesion , glycoprotein , cd49c , glycosylation , microbiology and biotechnology , cell adhesion molecule , chemistry , biochemistry , biology , collagen receptor , cell , lectin , gene
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.