Monocyte migration driven by galectin-3 occurs through distinct mechanisms involving selective interactions with the extracellular matrix

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dc.contributor.authorPolli, Cláudia Danella
dc.contributor.authorToledo, Karina Alves de [UNESP]
dc.contributor.authorFranco, Luís Henrique
dc.contributor.authorMariano, Vânia Sammartino
dc.contributor.authorOliveira, Leandro Licursi de
dc.contributor.authorBernardes, Emerson Soares
dc.contributor.authorRoque-Barreira, Maria Cristina
dc.contributor.authorSilva, Gabriela Pereira da
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade Federal de Viçosa (UFV)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.date.accessioned2015-08-21T17:53:18Z
dc.date.available2015-08-21T17:53:18Z
dc.date.issued2013
dc.description.abstractMonocyte migration into tissues, an important event in inflammation, requires an intricate interplay between determinants on cell surfaces and extracellular matrix (ECM). Galectin-3 is able to modulate cell-ECM interactions and is an important mediator of inflammation. In this study, we sought to investigate whether interactions established between galectin-3 and ECM glycoproteins are involved in monocyte migration, given that the mechanisms by which monocytes move across the endothelium and through the extravascular tissue are poorly understood. Using the in vitro transwell system, we demonstrated that monocyte migration was potentiated in the presence of galectin-3 plus laminin or fibronectin, but not vitronectin, and was dependent on the carbohydrate recognition domain of the lectin. Only galectin-3-fibronectin combinations potentiated the migration of monocytederived macrophages. In binding assays, galectin-3 did not bind to fibronectin, whereas both the full-length and the truncated forms of the lectin, which retains carbohydrate binding ability, were able to bind to laminin. Our results show that monocytes migrate through distinct mechanisms and selective interactions with the extracellular matrix driven by galectin-3.We suggest that the lectin may bridge monocytes to laminin and may also activate these cells, resulting in the positive regulation of other adhesion molecules and cell adhesion to fibronectin.en
dc.description.affiliationDepartamento de Biologia Celular e Molecular e Bioagentes Patogênicos, FMRP/USP, Ribeirão Preto, SP, Brazil
dc.description.affiliationDepartamento de Biologia Geral, UFV, Viçosa, MG, Brazil
dc.description.affiliationDepartamento de Enfermagem Materno-Infantil e Saúde Pública, EERP/USP, 3900-14040-902 Ribeirão Preto, SP, Brazil
dc.description.affiliationUnespUniversidade Estadual Paulista Júlio de Mesquita Filho, Faculdade de Ciências e Letras de Assis, Assis, Avenida Dom Antonio, 2100, Parque Universitário, CEP 19806900, SP, Brasil
dc.description.affiliationUnespCiências Biológicas
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.format.extent1-9
dc.identifierhttp://www.hindawi.com/journals/isrn/2013/259256/
dc.identifier.citationISRN Inflammation, v. 2013, p. 1-9, 2013.
dc.identifier.doi10.1155/2013/259256
dc.identifier.fileISSN2090-8695-2013-2013-01-09.pdf
dc.identifier.issn2090-8695
dc.identifier.lattes5772565774304020
dc.identifier.orcid0000-0001-7212-6794
dc.identifier.urihttp://hdl.handle.net/11449/126842
dc.language.isoeng
dc.relation.ispartofISRN Inflammation
dc.rights.accessRightsAcesso aberto
dc.sourceCurrículo Lattes
dc.titleMonocyte migration driven by galectin-3 occurs through distinct mechanisms involving selective interactions with the extracellular matrixen
dc.typeArtigo
unesp.author.lattes5772565774304020
unesp.author.orcid0000-0001-7212-6794
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências e Letras, Assispt
unesp.departmentCiências Biológicas - FCLASpt

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