alpha 6 beta 1-Integrin, a major cell surface carrier of beta 1-6-branched oligosaccharides, mediates migration of EJ-ras-transformed fibroblasts on laminin-1 independently of its glycosylation state

Detalhes bibliográficos
Autor(a) principal: Jasiulionis,Miriam Galvonas [UNIFESP]
Data de Publicação: 1996
Outros Autores: Chammas, Roger, Ventura, Armando M., Travassos, Luiz Rodolpho [UNIFESP], Brentani, Ricardo Renzo [UNIFESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNIFESP
Texto Completo: http://cancerres.aacrjournals.org/content/56/7/1682
http://repositorio.unifesp.br/handle/11600/43246
Resumo: EJ-ras oncogene-induced malignant transformation is characterized by a series of changes in cell surface carbohydrates and cell-cell and cell-matrix interactions, Here, we show that EJ-ras-transformed NIH-3T3 fibroblasts acquired a migratory phenotype on laminin-1 surfaces, Such a phenotype was accompanied by overexpression of: (a) functional alpha 6 beta 1, but not other laminin binding beta 1-integrins; and (b) glycoconjugates on the cell surface bearing large oligosaccharides recognized by leukoagglutinin from Phaseolus vulgar is (L-PHA). The internal pool of pre-beta 1-integrins was differently regulated in EJ-ras-transformed cells compared with non-transfected fibroblasts. Conversion of pre-beta 1- into mature beta 1-integrins was faster in EJ-ras-transformed cells, a process associated with the overexpression of the alpha 6-chain, Overexpression of L-PHA-reactive oligosaccharides is dependent on the activity of N-acetylglucosaminyltransferase V, which is increased in transformed cells [J. W. Dennis et al., Science (Washington DC), 236: 582-585, 1987], We show that beta 1-integrins were the major carriers of L-PHA-reactive oligosaccharides on the cell surface, This glycosylation pattern, however, was not necessary for either the cell surface expression of beta 1-integrins or their functional activity in the migratory response to laminin-1, Moreover, EJ-ras-transformed fibroblasts aggregated spontaneously, These effects were not observed in c-jun-transfected fibroblasts, which were unable to migrate on laminin, did not overexpress either beta 1-integrins or L-PHA-reactive oligosaccharides, and did not self-aggregate.
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spelling alpha 6 beta 1-Integrin, a major cell surface carrier of beta 1-6-branched oligosaccharides, mediates migration of EJ-ras-transformed fibroblasts on laminin-1 independently of its glycosylation stateEJ-ras oncogene-induced malignant transformation is characterized by a series of changes in cell surface carbohydrates and cell-cell and cell-matrix interactions, Here, we show that EJ-ras-transformed NIH-3T3 fibroblasts acquired a migratory phenotype on laminin-1 surfaces, Such a phenotype was accompanied by overexpression of: (a) functional alpha 6 beta 1, but not other laminin binding beta 1-integrins; and (b) glycoconjugates on the cell surface bearing large oligosaccharides recognized by leukoagglutinin from Phaseolus vulgar is (L-PHA). The internal pool of pre-beta 1-integrins was differently regulated in EJ-ras-transformed cells compared with non-transfected fibroblasts. Conversion of pre-beta 1- into mature beta 1-integrins was faster in EJ-ras-transformed cells, a process associated with the overexpression of the alpha 6-chain, Overexpression of L-PHA-reactive oligosaccharides is dependent on the activity of N-acetylglucosaminyltransferase V, which is increased in transformed cells [J. W. Dennis et al., Science (Washington DC), 236: 582-585, 1987], We show that beta 1-integrins were the major carriers of L-PHA-reactive oligosaccharides on the cell surface, This glycosylation pattern, however, was not necessary for either the cell surface expression of beta 1-integrins or their functional activity in the migratory response to laminin-1, Moreover, EJ-ras-transformed fibroblasts aggregated spontaneously, These effects were not observed in c-jun-transfected fibroblasts, which were unable to migrate on laminin, did not overexpress either beta 1-integrins or L-PHA-reactive oligosaccharides, and did not self-aggregate.LUDWIG INST CANC RES,SAO PAULO,SP,BRAZILUNIV FED SAO PAULO,ESCOLA PAULISTA MED,DISCIPLINA BIOL CELULAR,SAO PAULO,SP,BRAZILUNIV FED SAO PAULO,ESCOLA PAULISTA MED,DISCIPLINA BIOL CELULAR,SAO PAULO,SP,BRAZILWeb of ScienceAmer Assoc Cancer ResearchLUDWIG INST CANC RESUniversidade Federal de São Paulo (UNIFESP)Jasiulionis,Miriam Galvonas [UNIFESP]Chammas, RogerVentura, Armando M.Travassos, Luiz Rodolpho [UNIFESP]Brentani, Ricardo Renzo [UNIFESP]2018-06-15T16:39:14Z2018-06-15T16:39:14Z1996-04-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion1682-1689http://cancerres.aacrjournals.org/content/56/7/1682Cancer Research. Philadelphia: Amer Assoc Cancer Research, v. 56, n. 7, p. 1682-1689, 1996.0008-5472http://repositorio.unifesp.br/handle/11600/43246WOS:A1996UC16700036engCancer Researchinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP2024-05-02T15:52:15Zoai:repositorio.unifesp.br/:11600/43246Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestbiblioteca.csp@unifesp.bropendoar:34652024-05-02T15:52:15Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false
dc.title.none.fl_str_mv alpha 6 beta 1-Integrin, a major cell surface carrier of beta 1-6-branched oligosaccharides, mediates migration of EJ-ras-transformed fibroblasts on laminin-1 independently of its glycosylation state
title alpha 6 beta 1-Integrin, a major cell surface carrier of beta 1-6-branched oligosaccharides, mediates migration of EJ-ras-transformed fibroblasts on laminin-1 independently of its glycosylation state
spellingShingle alpha 6 beta 1-Integrin, a major cell surface carrier of beta 1-6-branched oligosaccharides, mediates migration of EJ-ras-transformed fibroblasts on laminin-1 independently of its glycosylation state
Jasiulionis,Miriam Galvonas [UNIFESP]
title_short alpha 6 beta 1-Integrin, a major cell surface carrier of beta 1-6-branched oligosaccharides, mediates migration of EJ-ras-transformed fibroblasts on laminin-1 independently of its glycosylation state
title_full alpha 6 beta 1-Integrin, a major cell surface carrier of beta 1-6-branched oligosaccharides, mediates migration of EJ-ras-transformed fibroblasts on laminin-1 independently of its glycosylation state
title_fullStr alpha 6 beta 1-Integrin, a major cell surface carrier of beta 1-6-branched oligosaccharides, mediates migration of EJ-ras-transformed fibroblasts on laminin-1 independently of its glycosylation state
title_full_unstemmed alpha 6 beta 1-Integrin, a major cell surface carrier of beta 1-6-branched oligosaccharides, mediates migration of EJ-ras-transformed fibroblasts on laminin-1 independently of its glycosylation state
title_sort alpha 6 beta 1-Integrin, a major cell surface carrier of beta 1-6-branched oligosaccharides, mediates migration of EJ-ras-transformed fibroblasts on laminin-1 independently of its glycosylation state
author Jasiulionis,Miriam Galvonas [UNIFESP]
author_facet Jasiulionis,Miriam Galvonas [UNIFESP]
Chammas, Roger
Ventura, Armando M.
Travassos, Luiz Rodolpho [UNIFESP]
Brentani, Ricardo Renzo [UNIFESP]
author_role author
author2 Chammas, Roger
Ventura, Armando M.
Travassos, Luiz Rodolpho [UNIFESP]
Brentani, Ricardo Renzo [UNIFESP]
author2_role author
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 Jasiulionis,Miriam Galvonas [UNIFESP]
Chammas, Roger
Ventura, Armando M.
Travassos, Luiz Rodolpho [UNIFESP]
Brentani, Ricardo Renzo [UNIFESP]
description EJ-ras oncogene-induced malignant transformation is characterized by a series of changes in cell surface carbohydrates and cell-cell and cell-matrix interactions, Here, we show that EJ-ras-transformed NIH-3T3 fibroblasts acquired a migratory phenotype on laminin-1 surfaces, Such a phenotype was accompanied by overexpression of: (a) functional alpha 6 beta 1, but not other laminin binding beta 1-integrins; and (b) glycoconjugates on the cell surface bearing large oligosaccharides recognized by leukoagglutinin from Phaseolus vulgar is (L-PHA). The internal pool of pre-beta 1-integrins was differently regulated in EJ-ras-transformed cells compared with non-transfected fibroblasts. Conversion of pre-beta 1- into mature beta 1-integrins was faster in EJ-ras-transformed cells, a process associated with the overexpression of the alpha 6-chain, Overexpression of L-PHA-reactive oligosaccharides is dependent on the activity of N-acetylglucosaminyltransferase V, which is increased in transformed cells [J. W. Dennis et al., Science (Washington DC), 236: 582-585, 1987], We show that beta 1-integrins were the major carriers of L-PHA-reactive oligosaccharides on the cell surface, This glycosylation pattern, however, was not necessary for either the cell surface expression of beta 1-integrins or their functional activity in the migratory response to laminin-1, Moreover, EJ-ras-transformed fibroblasts aggregated spontaneously, These effects were not observed in c-jun-transfected fibroblasts, which were unable to migrate on laminin, did not overexpress either beta 1-integrins or L-PHA-reactive oligosaccharides, and did not self-aggregate.
publishDate 1996
dc.date.none.fl_str_mv 1996-04-01
2018-06-15T16:39:14Z
2018-06-15T16:39:14Z
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 http://cancerres.aacrjournals.org/content/56/7/1682
Cancer Research. Philadelphia: Amer Assoc Cancer Research, v. 56, n. 7, p. 1682-1689, 1996.
0008-5472
http://repositorio.unifesp.br/handle/11600/43246
WOS:A1996UC16700036
url http://cancerres.aacrjournals.org/content/56/7/1682
http://repositorio.unifesp.br/handle/11600/43246
identifier_str_mv Cancer Research. Philadelphia: Amer Assoc Cancer Research, v. 56, n. 7, p. 1682-1689, 1996.
0008-5472
WOS:A1996UC16700036
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Cancer Research
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 1682-1689
dc.publisher.none.fl_str_mv Amer Assoc Cancer Research
publisher.none.fl_str_mv Amer Assoc Cancer Research
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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