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

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dc.contributor.authorFranco, Celia Regina Cavichiolo [UNIFESP]
dc.contributor.authorTrindade, Edvaldo da Silva [UNIFESP]
dc.contributor.authorRocha, Hugo Alexandre de Oliveira [UNIFESP]
dc.contributor.authorSilveira, Rafael Bertoni da [UNIFESP]
dc.contributor.authorPaludo, Katia Sabrina
dc.contributor.authorChammas, Roger
dc.contributor.authorVeiga, Silvio Sanches
dc.contributor.authorNader, Helena Bonciani [UNIFESP]
dc.contributor.authorDietrich, Carl Peter [UNIFESP]
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniv Fed Parana
dc.contributor.institutionUniv Fed Rio Grande do Norte
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.date.accessioned2016-01-24T13:58:34Z
dc.date.available2016-01-24T13:58:34Z
dc.date.issued2009-08-01
dc.description.abstractalpha(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.en
dc.description.affiliationUniversidade Federal de São Paulo, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.description.affiliationUniv Fed Parana, Dept Biol Celular, Curitiba, PR, Brazil
dc.description.affiliationUniv Fed Rio Grande do Norte, Dept Bioquim, BR-59072970 Natal, RN, Brazil
dc.description.affiliationUniv São Paulo, Fac Med, Expt Oncol Lab, São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Bioquim, BR-04044020 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent677-686
dc.identifierhttps://dx.doi.org/10.1139/O09-047
dc.identifier.citationBiochemistry and Cell Biology-biochimie Et Biologie Cellulaire. Ottawa: Canadian Science Publishing, Nrc Research Press, v. 87, n. 4, p. 677-686, 2009.
dc.identifier.doi10.1139/O09-047
dc.identifier.issn0829-8211
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/31697
dc.identifier.wosWOS:000269762100012
dc.language.isoeng
dc.publisherCanadian Science Publishing, Nrc Research Press
dc.relation.ispartofBiochemistry and Cell Biology-biochimie Et Biologie Cellulaire
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectIntegrinen
dc.subjectGlycosaminoglycanen
dc.subjectMigration on fibronectinen
dc.subjectAdhesion on fibronectinen
dc.subjectProteoglycanen
dc.titleGlycosaminoglycan chains from alpha(5)beta(1) integrin are involved in fibronectin-dependent cell migrationen
dc.typeinfo:eu-repo/semantics/article
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