FUNCTIONALLY DISTINCT ROLES for GLYCOSYLATION of ALPHA-INTEGRIN and BETA-INTEGRIN CHAINS in CELL MATRIX INTERACTIONS

FUNCTIONALLY DISTINCT ROLES for GLYCOSYLATION of ALPHA-INTEGRIN and BETA-INTEGRIN CHAINS in CELL MATRIX INTERACTIONS

Autor Chammas, R. Google Scholar
Veiga, Silvio Sanches Autor UNIFESP Google Scholar
Travassos, Luiz Rodolpho Autor UNIFESP Google Scholar
Brentani, Ricardo Renzo Autor UNIFESP Google Scholar
Instituição LUDWIG INST CANC RES
Universidade Federal de São Paulo (UNIFESP)
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.
Idioma Inglês
Data de publicação 1993-03-01
Publicado em 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.
ISSN 0027-8424 (Sherpa/Romeo, fator de impacto)
Publicador Natl Acad Sciences
Extensão 1795-1799
Fonte http://dx.doi.org/10.1073/pnas.90.5.1795
Direito de acesso Acesso aberto Open Access
Tipo Artigo
Web of Science WOS:A1993KP97900035
Endereço permanente http://repositorio.unifesp.br/handle/11600/25307

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