Functionally distinct roles for glycosylation of alpha and beta integrin chains in cell-matrix interactions
Data
1993-03-01
Autores
Veiga, Silvio Sanches 
Travassos, Luiz Rodolpho
Brentani, Ricardo Renzo
Tipo
Artigo
Título da Revista
ISSN da Revista
Título de Volume
Resumo
Laminin interaction with gp120/140, a B16-F10 laminin-binding protein immunologically related to alpha6beta1 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.
Descrição
Citação
Proceedings of the National Academy of Sciences of the United States of America. Washington: Natl Acad Sciences, v. 90, n. 5, p. 1795-1799, 1993.