Coupling of vinculin to F-actin demands Syndecan-4 proteoglycan

Página do item simplificado
dc.citation.volume63
dc.contributor.authorCavalheiro, R. P. [UNIFESP]
dc.contributor.authorLima, M. A. [UNIFESP]
dc.contributor.authorJarrouge-Boucas, T. R. [UNIFESP]
dc.contributor.authorViana, G. M. [UNIFESP]
dc.contributor.authorLopes, C. C. [UNIFESP]
dc.contributor.authorCoulson-Thomas, V. J. [UNIFESP]
dc.contributor.authorDreyfuss, J. L. [UNIFESP]
dc.contributor.authorYates, E. A. [UNIFESP]
dc.contributor.authorTersariol, I. L. S. [UNIFESP]
dc.contributor.authorNader, H. B. [UNIFESP]
dc.coverageAmsterdam
dc.date.accessioned2020-09-01T13:21:30Z
dc.date.available2020-09-01T13:21:30Z
dc.date.issued2017
dc.description.abstractSyndecans are heparan sulfate proteoglycans characterized as transmembrane receptors that act cooperatively with the cell surface and extracellular matrix proteins. Syn4 knockdown was performed in orderto address its role in endothelial cells (EC) behavior. Normal EC and shRNA-Syn4-EC cells were studied comparatively using complementary confocal, super-resolution and non-linear microscopic techniques. Confocal and super-resolution microscopy revealed that Syn4 knockdown alters the level and arrangement of essential proteins for focal adhesion, evidenced by the decoupling of vinculin from F-actin filaments. Furthermore, Syn4 knockdown alters the actin network leading to filopodial protrusions connected by VE-cadherin rich junction. shRNA-Syn4-EC showed reduced adhesion and increased migration. Also, Syn4 silencing alters cell cycle as well as cell proliferation. Moreover, the ability of EC to form tube-like structures in matrigel is reduced when Syn4 is silenced. Together, the results suggest a mechanism in which Syndecan-4 acts as a central mediator that bridges fibronectin, integrin and intracellular components (actin and vinculin) and once silenced, the cytoskeleton protein network is disrupted. Ultimately, the results highlight Syn4 relevance for balanced cell behavior. (C) 2016 Elsevier B.V. All rights reserved.en
dc.description.affiliationUniv Fed Sao Paulo, Escola Paulista Med, Dept Bioquim, Disciplina Biol Mol, Sao Paulo, SP, Brazil
dc.description.affiliationUniv Liverpool, Inst Integrat Biol, Dept Biochem, Liverpool, Merseyside, England
dc.description.affiliationUniv Fed Sao Paulo, Inst Ciencias Ambientais Quim & Farmaceut, Diadema, SP, Brazil
dc.description.affiliationUniv Houston, Coll Optometry, TOSI, Houston, TX USA
dc.description.affiliationUniv Fed Sao Paulo, Grp Interdisciplinar Ciencias Exatas Saude, Sao Paulo, SP, Brazil
dc.description.affiliationUnifespUniv Fed Sao Paulo, Escola Paulista Med, Dept Bioquim, Disciplina Biol Mol, Sao Paulo, SP, Brazil
dc.description.affiliationUnifespUniv Fed Sao Paulo, Inst Ciencias Ambientais Quim & Farmaceut, Diadema, SP, Brazil
dc.description.affiliationUnifespUniv Fed Sao Paulo, Grp Interdisciplinar Ciencias Exatas Saude, Sao Paulo, SP, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipCAPES (Coordenagdo de Aperfeicoamento de Pessoal de Nivel Superior)
dc.description.sponsorshipCNPq (Conselho Nacional de Desenvolvimento Cientffico e Tecnologico)
dc.description.sponsorshipFAPESP (Fundacao de Amparo a Pesquisa do Estado de sao Paulo), Brazil
dc.description.sponsorshipIDFAPESP: 15/08782-3
dc.description.sponsorshipIDFAPESP: 15/03964-6
dc.format.extent23-37
dc.identifierhttp://dx.doi.org/10.1016/j.matbio.2016.12.006
dc.identifier.citationMatrix Biology. Amsterdam, v. 63, p. 23-37, 2017.
dc.identifier.doi10.1016/j.matbio.2016.12.006
dc.identifier.issn0945-053X
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/58309
dc.identifier.wosWOS:000413135300003
dc.language.isoeng
dc.publisherElsevier Science Bv
dc.relation.ispartofMatrix Biology
dc.rightsAcesso restrito
dc.subjectHeparan sulfateen
dc.subjectbeta 1 integrinen
dc.subjectFibronectinen
dc.subjectFocal adhesion proteinsen
dc.subjectSuper-resolution microscopyen
dc.subjectActin networken
dc.titleCoupling of vinculin to F-actin demands Syndecan-4 proteoglycanen
dc.typeArtigo
Arquivos
Coleções
EPM - Artigos
ICAQF - Artigos