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Functionally distinct roles for glycosylation of alpha and beta integrin chains in cell-matrix interactions.

Laminin interaction with gp120/140, a B16-F10 laminin-binding protein immunologically related to alpha 6 beta 1 integrin, has been shown to be dependent on oligosaccharides from both ligand and receptor. Lectin analysis of gp120/140 led to the conclusion that this integrin is a sialoglycoprotein bearing mainly complex antennary structures. By means of exoglycosidase treatment, it was possible to identify alpha-galactosyl residues on the integrin alpha chain as the laminin-binding determinants. These residues are involved in cell adhesion to laminin. On the other hand, beta-chain complex antennary structures, whose synthesis could be inhibited by swainsonine, were associated with cell spreading rather than cell adhesion. Thus, it was possible to modulate integrin-mediated cell adhesion and spreading through changes in the glycosylation state of integrin alpha and beta chains.[1]

References

  1. Functionally distinct roles for glycosylation of alpha and beta integrin chains in cell-matrix interactions. Chammas, R., Veiga, S.S., Travassos, L.R., Brentani, R.R. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
 
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