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
Autor(a) principal: | |
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Data de Publicação: | 1996 |
Outros Autores: | , , , |
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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Repositório Institucional da UNIFESP |
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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 |
_version_ |
1814268362465738752 |