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. 1993 Mar 1;90(5):1795–1799. doi: 10.1073/pnas.90.5.1795

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

R Chammas 1, S S Veiga 1, L R Travassos 1, R R Brentani 1
PMCID: PMC45966  PMID: 8446593

Abstract

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.

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