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

Detalhes bibliográficos
Autor(a) principal: Chammas, Roger
Data de Publicação: 1993
Outros Autores: Veiga, Silvio Sanches [UNIFESP], Travassos, Luiz Rodolpho [UNIFESP], Brentani, Ricardo Renzo [UNIFESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNIFESP
Texto Completo: https://dx.doi.org/10.1073/pnas.90.5.1795
https://repositorio.unifesp.br/handle/11600/25307
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.
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spelling Functionally distinct roles for glycosylation of alpha and beta integrin chains in cell-matrix interactionsLaminin 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.LUDWIG INST CANC RES,RUA PROF ANTONIO PRUDENTE 109-4,BR-01509 São Paulo,BRAZILESCOLA PAULISTA MED SCH,DISCIPLINA BIOL CELULAR,BR-04023 São Paulo,BRAZILESCOLA PAULISTA MED SCH,DISCIPLINA BIOL CELULAR,BR-04023 São Paulo,BRAZILWeb of ScienceNatl Acad SciencesLUDWIG INST CANC RESUniversidade Federal de São Paulo (UNIFESP)Chammas, RogerVeiga, Silvio Sanches [UNIFESP]Travassos, Luiz Rodolpho [UNIFESP]Brentani, Ricardo Renzo [UNIFESP]2016-01-24T11:40:11Z2016-01-24T11:40:11Z1993-03-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion1795-1799https://dx.doi.org/10.1073/pnas.90.5.1795Proceedings of the National Academy of Sciences of the United States of America. Washington: Natl Acad Sciences, v. 90, n. 5, p. 1795-1799, 1993.10.1073/pnas.90.5.17950027-8424https://repositorio.unifesp.br/handle/11600/25307WOS:A1993KP97900035engProceedings of the National Academy of Sciences of the United States of Americainfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP2024-01-19T21:10:09Zoai:repositorio.unifesp.br/:11600/25307Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestbiblioteca.csp@unifesp.bropendoar:34652024-01-19T21:10:09Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false
dc.title.none.fl_str_mv Functionally distinct roles for glycosylation of alpha and beta integrin chains in cell-matrix interactions
title Functionally distinct roles for glycosylation of alpha and beta integrin chains in cell-matrix interactions
spellingShingle Functionally distinct roles for glycosylation of alpha and beta integrin chains in cell-matrix interactions
Chammas, Roger
title_short Functionally distinct roles for glycosylation of alpha and beta integrin chains in cell-matrix interactions
title_full Functionally distinct roles for glycosylation of alpha and beta integrin chains in cell-matrix interactions
title_fullStr Functionally distinct roles for glycosylation of alpha and beta integrin chains in cell-matrix interactions
title_full_unstemmed Functionally distinct roles for glycosylation of alpha and beta integrin chains in cell-matrix interactions
title_sort Functionally distinct roles for glycosylation of alpha and beta integrin chains in cell-matrix interactions
author Chammas, Roger
author_facet Chammas, Roger
Veiga, Silvio Sanches [UNIFESP]
Travassos, Luiz Rodolpho [UNIFESP]
Brentani, Ricardo Renzo [UNIFESP]
author_role author
author2 Veiga, Silvio Sanches [UNIFESP]
Travassos, Luiz Rodolpho [UNIFESP]
Brentani, Ricardo Renzo [UNIFESP]
author2_role author
author
author
dc.contributor.none.fl_str_mv LUDWIG INST CANC RES
Universidade Federal de São Paulo (UNIFESP)
dc.contributor.author.fl_str_mv Chammas, Roger
Veiga, Silvio Sanches [UNIFESP]
Travassos, Luiz Rodolpho [UNIFESP]
Brentani, Ricardo Renzo [UNIFESP]
description 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.
publishDate 1993
dc.date.none.fl_str_mv 1993-03-01
2016-01-24T11:40:11Z
2016-01-24T11:40:11Z
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv https://dx.doi.org/10.1073/pnas.90.5.1795
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.
10.1073/pnas.90.5.1795
0027-8424
https://repositorio.unifesp.br/handle/11600/25307
WOS:A1993KP97900035
url https://dx.doi.org/10.1073/pnas.90.5.1795
https://repositorio.unifesp.br/handle/11600/25307
identifier_str_mv 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.
10.1073/pnas.90.5.1795
0027-8424
WOS:A1993KP97900035
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Proceedings of the National Academy of Sciences of the United States of America
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 1795-1799
dc.publisher.none.fl_str_mv Natl Acad Sciences
publisher.none.fl_str_mv Natl Acad Sciences
dc.source.none.fl_str_mv reponame:Repositório Institucional da UNIFESP
instname:Universidade Federal de São Paulo (UNIFESP)
instacron:UNIFESP
instname_str Universidade Federal de São Paulo (UNIFESP)
instacron_str UNIFESP
institution UNIFESP
reponame_str Repositório Institucional da UNIFESP
collection Repositório Institucional da UNIFESP
repository.name.fl_str_mv Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)
repository.mail.fl_str_mv biblioteca.csp@unifesp.br
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