Functionally distinct roles for glycosylation of alpha and beta integrin chains in cell-matrix interactions
| dc.contributor.author | Chammas, Roger | |
| dc.contributor.author | Veiga, Silvio Sanches [UNIFESP] | |
| dc.contributor.author | Travassos, Luiz Rodolpho [UNIFESP] | |
| dc.contributor.author | Brentani, Ricardo Renzo [UNIFESP] | |
| dc.contributor.institution | LUDWIG INST CANC RES | |
| dc.contributor.institution | Universidade Federal de São Paulo (UNIFESP) | |
| dc.date.accessioned | 2016-01-24T11:40:11Z | |
| dc.date.available | 2016-01-24T11:40:11Z | |
| dc.date.issued | 1993-03-01 | |
| dc.description.abstract | 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. | en |
| dc.description.affiliation | LUDWIG INST CANC RES,RUA PROF ANTONIO PRUDENTE 109-4,BR-01509 São Paulo,BRAZIL | |
| dc.description.affiliation | ESCOLA PAULISTA MED SCH,DISCIPLINA BIOL CELULAR,BR-04023 São Paulo,BRAZIL | |
| dc.description.affiliationUnifesp | ESCOLA PAULISTA MED SCH,DISCIPLINA BIOL CELULAR,BR-04023 São Paulo,BRAZIL | |
| dc.description.source | Web of Science | |
| dc.format.extent | 1795-1799 | |
| dc.identifier | https://dx.doi.org/10.1073/pnas.90.5.1795 | |
| dc.identifier.citation | 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. | |
| dc.identifier.doi | 10.1073/pnas.90.5.1795 | |
| dc.identifier.issn | 0027-8424 | |
| dc.identifier.uri | https://repositorio.unifesp.br/handle/11600/25307 | |
| dc.identifier.wos | WOS:A1993KP97900035 | |
| dc.language.iso | eng | |
| dc.publisher | Natl Acad Sciences | |
| dc.relation.ispartof | Proceedings of the National Academy of Sciences of the United States of America | |
| dc.rights | info:eu-repo/semantics/openAccess | |
| dc.title | Functionally distinct roles for glycosylation of alpha and beta integrin chains in cell-matrix interactions | en |
| dc.type | info:eu-repo/semantics/article |