Glycosaminoglycan chains from alpha(5)beta(1) integrin are involved in fibronectin-dependent cell migration

Detalhes bibliográficos
Autor(a) principal: Franco, Celia Regina Cavichiolo [UNIFESP]
Data de Publicação: 2009
Outros Autores: Trindade, Edvaldo da Silva [UNIFESP], Rocha, Hugo Alexandre de Oliveira [UNIFESP], Silveira, Rafael Bertoni da [UNIFESP], Paludo, Katia Sabrina, Chammas, Roger, Veiga, Silvio Sanches, Nader, Helena Bonciani [UNIFESP], Dietrich, Carl Peter [UNIFESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNIFESP
Texto Completo: https://dx.doi.org/10.1139/O09-047
https://repositorio.unifesp.br/handle/11600/31697
Resumo: alpha(5)beta(1) integrin from both wild-type CHO cells (CHO-K1) and deficient in proteoglycan biosynthesis (CHO-745) is post-translationally modified by glycosaminoglycan chains. We demonstrated this using [S-35]sulfate metabolic labeling of the cells, enzymatic degradation, immunoprecipitation reaction with monoclonal antibody, fluorescence microscopy, and flow cytometry. the alpha(5)beta(1) integrin heterodimer is a hybrid proteoglycan containing both chondroitin and heparan sulfate chains. Xyloside inhibition of sulfate incorporation into alpha(5)beta(1) integrin also supports that integrin is a proteoglycan. Also. cells grown with xyloside adhered on fibronectin with no alteration in alpha(5)beta(1) integrin expression. However, haptotactic motility on fibronectin declined in cells grown with xyloside or chlorate as compared with controls. Thus, alpha(5)beta(1) integrin is a proteoglycan and the glycosaminoglycan chains of the integrin influence cell motility on fibronectin. Similar glycosylation of alpha(5)beta(1) integrin was observed in other normal and malignant cells, suggesting that this modification is conserved and important in the function of this integrin. Therefore, these glycosaminoglycan chains of alpha(5)beta(1) integrin are involved in cellular migration on fibronectin.
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spelling Glycosaminoglycan chains from alpha(5)beta(1) integrin are involved in fibronectin-dependent cell migrationIntegrinGlycosaminoglycanMigration on fibronectinAdhesion on fibronectinProteoglycanalpha(5)beta(1) integrin from both wild-type CHO cells (CHO-K1) and deficient in proteoglycan biosynthesis (CHO-745) is post-translationally modified by glycosaminoglycan chains. We demonstrated this using [S-35]sulfate metabolic labeling of the cells, enzymatic degradation, immunoprecipitation reaction with monoclonal antibody, fluorescence microscopy, and flow cytometry. the alpha(5)beta(1) integrin heterodimer is a hybrid proteoglycan containing both chondroitin and heparan sulfate chains. Xyloside inhibition of sulfate incorporation into alpha(5)beta(1) integrin also supports that integrin is a proteoglycan. Also. cells grown with xyloside adhered on fibronectin with no alteration in alpha(5)beta(1) integrin expression. However, haptotactic motility on fibronectin declined in cells grown with xyloside or chlorate as compared with controls. Thus, alpha(5)beta(1) integrin is a proteoglycan and the glycosaminoglycan chains of the integrin influence cell motility on fibronectin. Similar glycosylation of alpha(5)beta(1) integrin was observed in other normal and malignant cells, suggesting that this modification is conserved and important in the function of this integrin. Therefore, these glycosaminoglycan chains of alpha(5)beta(1) integrin are involved in cellular migration on fibronectin.Universidade Federal de São Paulo, Dept Bioquim, BR-04044020 São Paulo, BrazilUniv Fed Parana, Dept Biol Celular, Curitiba, PR, BrazilUniv Fed Rio Grande do Norte, Dept Bioquim, BR-59072970 Natal, RN, BrazilUniv São Paulo, Fac Med, Expt Oncol Lab, São Paulo, BrazilUniversidade Federal de São Paulo, Dept Bioquim, BR-04044020 São Paulo, BrazilWeb of ScienceCanadian Science Publishing, Nrc Research PressUniversidade Federal de São Paulo (UNIFESP)Univ Fed ParanaUniv Fed Rio Grande do NorteUniversidade de São Paulo (USP)Franco, Celia Regina Cavichiolo [UNIFESP]Trindade, Edvaldo da Silva [UNIFESP]Rocha, Hugo Alexandre de Oliveira [UNIFESP]Silveira, Rafael Bertoni da [UNIFESP]Paludo, Katia SabrinaChammas, RogerVeiga, Silvio SanchesNader, Helena Bonciani [UNIFESP]Dietrich, Carl Peter [UNIFESP]2016-01-24T13:58:34Z2016-01-24T13:58:34Z2009-08-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion677-686https://dx.doi.org/10.1139/O09-047Biochemistry and Cell Biology-biochimie Et Biologie Cellulaire. Ottawa: Canadian Science Publishing, Nrc Research Press, v. 87, n. 4, p. 677-686, 2009.10.1139/O09-0470829-8211https://repositorio.unifesp.br/handle/11600/31697WOS:000269762100012engBiochemistry and Cell Biology-biochimie Et Biologie Cellulaireinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP2024-01-19T19:40:11Zoai:repositorio.unifesp.br/:11600/31697Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestbiblioteca.csp@unifesp.bropendoar:34652024-01-19T19:40:11Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false
dc.title.none.fl_str_mv Glycosaminoglycan chains from alpha(5)beta(1) integrin are involved in fibronectin-dependent cell migration
title Glycosaminoglycan chains from alpha(5)beta(1) integrin are involved in fibronectin-dependent cell migration
spellingShingle Glycosaminoglycan chains from alpha(5)beta(1) integrin are involved in fibronectin-dependent cell migration
Franco, Celia Regina Cavichiolo [UNIFESP]
Integrin
Glycosaminoglycan
Migration on fibronectin
Adhesion on fibronectin
Proteoglycan
title_short Glycosaminoglycan chains from alpha(5)beta(1) integrin are involved in fibronectin-dependent cell migration
title_full Glycosaminoglycan chains from alpha(5)beta(1) integrin are involved in fibronectin-dependent cell migration
title_fullStr Glycosaminoglycan chains from alpha(5)beta(1) integrin are involved in fibronectin-dependent cell migration
title_full_unstemmed Glycosaminoglycan chains from alpha(5)beta(1) integrin are involved in fibronectin-dependent cell migration
title_sort Glycosaminoglycan chains from alpha(5)beta(1) integrin are involved in fibronectin-dependent cell migration
author Franco, Celia Regina Cavichiolo [UNIFESP]
author_facet Franco, Celia Regina Cavichiolo [UNIFESP]
Trindade, Edvaldo da Silva [UNIFESP]
Rocha, Hugo Alexandre de Oliveira [UNIFESP]
Silveira, Rafael Bertoni da [UNIFESP]
Paludo, Katia Sabrina
Chammas, Roger
Veiga, Silvio Sanches
Nader, Helena Bonciani [UNIFESP]
Dietrich, Carl Peter [UNIFESP]
author_role author
author2 Trindade, Edvaldo da Silva [UNIFESP]
Rocha, Hugo Alexandre de Oliveira [UNIFESP]
Silveira, Rafael Bertoni da [UNIFESP]
Paludo, Katia Sabrina
Chammas, Roger
Veiga, Silvio Sanches
Nader, Helena Bonciani [UNIFESP]
Dietrich, Carl Peter [UNIFESP]
author2_role author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Federal de São Paulo (UNIFESP)
Univ Fed Parana
Univ Fed Rio Grande do Norte
Universidade de São Paulo (USP)
dc.contributor.author.fl_str_mv Franco, Celia Regina Cavichiolo [UNIFESP]
Trindade, Edvaldo da Silva [UNIFESP]
Rocha, Hugo Alexandre de Oliveira [UNIFESP]
Silveira, Rafael Bertoni da [UNIFESP]
Paludo, Katia Sabrina
Chammas, Roger
Veiga, Silvio Sanches
Nader, Helena Bonciani [UNIFESP]
Dietrich, Carl Peter [UNIFESP]
dc.subject.por.fl_str_mv Integrin
Glycosaminoglycan
Migration on fibronectin
Adhesion on fibronectin
Proteoglycan
topic Integrin
Glycosaminoglycan
Migration on fibronectin
Adhesion on fibronectin
Proteoglycan
description alpha(5)beta(1) integrin from both wild-type CHO cells (CHO-K1) and deficient in proteoglycan biosynthesis (CHO-745) is post-translationally modified by glycosaminoglycan chains. We demonstrated this using [S-35]sulfate metabolic labeling of the cells, enzymatic degradation, immunoprecipitation reaction with monoclonal antibody, fluorescence microscopy, and flow cytometry. the alpha(5)beta(1) integrin heterodimer is a hybrid proteoglycan containing both chondroitin and heparan sulfate chains. Xyloside inhibition of sulfate incorporation into alpha(5)beta(1) integrin also supports that integrin is a proteoglycan. Also. cells grown with xyloside adhered on fibronectin with no alteration in alpha(5)beta(1) integrin expression. However, haptotactic motility on fibronectin declined in cells grown with xyloside or chlorate as compared with controls. Thus, alpha(5)beta(1) integrin is a proteoglycan and the glycosaminoglycan chains of the integrin influence cell motility on fibronectin. Similar glycosylation of alpha(5)beta(1) integrin was observed in other normal and malignant cells, suggesting that this modification is conserved and important in the function of this integrin. Therefore, these glycosaminoglycan chains of alpha(5)beta(1) integrin are involved in cellular migration on fibronectin.
publishDate 2009
dc.date.none.fl_str_mv 2009-08-01
2016-01-24T13:58:34Z
2016-01-24T13:58:34Z
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/10.1139/O09-047
Biochemistry and Cell Biology-biochimie Et Biologie Cellulaire. Ottawa: Canadian Science Publishing, Nrc Research Press, v. 87, n. 4, p. 677-686, 2009.
10.1139/O09-047
0829-8211
https://repositorio.unifesp.br/handle/11600/31697
WOS:000269762100012
url https://dx.doi.org/10.1139/O09-047
https://repositorio.unifesp.br/handle/11600/31697
identifier_str_mv Biochemistry and Cell Biology-biochimie Et Biologie Cellulaire. Ottawa: Canadian Science Publishing, Nrc Research Press, v. 87, n. 4, p. 677-686, 2009.
10.1139/O09-047
0829-8211
WOS:000269762100012
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Biochemistry and Cell Biology-biochimie Et Biologie Cellulaire
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 677-686
dc.publisher.none.fl_str_mv Canadian Science Publishing, Nrc Research Press
publisher.none.fl_str_mv Canadian Science Publishing, Nrc Research Press
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_ 1814268392743370752

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