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Altered glycosylation of β1 integrins associated with reduced adhesiveness to fibronectin and laminin

✍ Scribed by Takehiro Kawano; Seiichi Takasaki; Tien-Wen Tao; Akira Kobata

Publisher
John Wiley and Sons
Year
1993
Tongue
French
Weight
650 KB
Volume
53
Category
Article
ISSN
0020-7136

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✦ Synopsis

The carbohydrate structures of the PI integrins obtained from a mouse metastatic melanoma 816 F I and its weakly metastatic wheat-germ agglutinin-resistant mutant Wa4-b I were studied comparatively. The results indicated that the integrins from both cells contain high mannose-type and bi-, triand 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, Gal6 i + 4 (Fucal + 3) GlcNAc. In 3To whom correspondence and reprint requests should be addressed.

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