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Role of surface chemistry in protein remodeling at the cell-material interface

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Role of surface chemistry in protein remodeling at the cell-material interface

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dc.contributor.author Llopis Hernández, Virginia es_ES
dc.contributor.author Rico Tortosa, Patricia María es_ES
dc.contributor.author Ballester Beltrán, José es_ES
dc.contributor.author Moratal Pérez, David es_ES
dc.contributor.author Salmerón Sánchez, Manuel es_ES
dc.date.accessioned 2013-04-30T14:14:23Z
dc.date.available 2013-04-30T14:14:23Z
dc.date.issued 2011
dc.identifier.issn 1932-6203
dc.identifier.uri http://hdl.handle.net/10251/28360
dc.description.abstract Background: The cell-material interaction is a complex bi-directional and dynamic process that mimics to a certain extent the natural interactions of cells with the extracellular matrix. Cells tend to adhere and rearrange adsorbed extracellular matrix (ECM) proteins on the material surface in a fibril-like pattern. Afterwards, the ECM undergoes proteolytic degradation, which is a mechanism for the removal of the excess ECM usually approximated with remodeling. ECM remodeling is a dynamic process that consists of two opposite events: assembly and degradation. Methodology/Principal Findings: This work investigates matrix protein dynamics on mixed self-assembled monolayers (SAMs) of -OH and -CH3 terminated alkanethiols. SAMs assembled on gold are highly ordered organic surfaces able to provide different chemical functionalities and well-controlled surface properties. Fibronectin (FN) was adsorbed on the different surfaces and quantified in terms of the adsorbed surface density, distribution and conformation. Initial cell adhesion and signaling on FN-coated SAMs were characterized via the formation of focal adhesions, integrin expression and phosphorylation of FAKs. Afterwards, the reorganization and secretion of FN was assessed. Finally, matrix degradation was followed via the expression of matrix metalloproteinases MMP2 and MMP9 and correlated with Runx2 levels. We show that matrix degradation at the cell material interface depends on surface chemistry in MMP-dependent way. Conclusions/Significance: This work provides a broad overview of matrix remodeling at the cell-material interface, establishing correlations between surface chemistry, FN adsorption, cell adhesion and signaling, matrix reorganization and degradation. The reported findings improve our understanding of the role of surface chemistry as a key parameter in the design of new biomaterials. It demonstrates the ability of surface chemistry to direct proteolytic routes at the cell-material interface, which gains a distinct bioengineering interest as a new tool to trigger matrix degradation in different biomedical applications. © 2011 Llopis-Hernández et al. es_ES
dc.description.sponsorship The support of the Spanish Ministry of Science and Innovation through project MAT2009-14440-C02-01 is acknowledged. CIBER-BBN is an initiative funded by the VI National R&D&i Plan 2008-2011, Iniciativa Ingenio 2010, Consolider Program, CIBER Actions and financed by the Instituto de Salud Carlos III with assistance from the European Regional Development Fund. This work was supported by funds for research in the field of Regenerative Medicine through the collaboration agreement from the Conselleria de Sanidad (Generalitat Valenciana), and the Instituto de Salud Carlos III. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. en_EN
dc.language Inglés es_ES
dc.publisher Public Library of Science es_ES
dc.relation MICINN/MAT2009-14440-C02-01
dc.relation.ispartof PLoS ONE es_ES
dc.rights Reconocimiento (by) es_ES
dc.subject Fibronectin es_ES
dc.subject Focal adhesion kinase es_ES
dc.subject Gelatinase A es_ES
dc.subject Gelatinase B es_ES
dc.subject Integrin es_ES
dc.subject Scleroprotein es_ES
dc.subject Transcription factor RUNX2 es_ES
dc.subject Phosphotyrosine es_ES
dc.subject Adsorption es_ES
dc.subject Article es_ES
dc.subject Atomic force microscopy es_ES
dc.subject Biocompatibility es_ES
dc.subject Cell adhesion es_ES
dc.subject Cell interaction es_ES
dc.subject Controlled study es_ES
dc.subject Degradation es_ES
dc.subject Focal adhesion es_ES
dc.subject Human es_ES
dc.subject Molecular dynamics es_ES
dc.subject Nucleotide sequence es_ES
dc.subject Protein conformation es_ES
dc.subject Protein expression es_ES
dc.subject Protein function es_ES
dc.subject Protein localization es_ES
dc.subject Protein modification es_ES
dc.subject Protein phosphorylation es_ES
dc.subject Protein secretion es_ES
dc.subject Signal transduction es_ES
dc.subject Surface property es_ES
dc.subject Animal es_ES
dc.subject Cell es_ES
dc.subject Cell line es_ES
dc.subject Chemistry es_ES
dc.subject Extracellular matrix es_ES
dc.subject Gene expression regulation es_ES
dc.subject Metabolism es_ES
dc.subject Mouse es_ES
dc.subject Wettability es_ES
dc.subject Animals es_ES
dc.subject Cells es_ES
dc.subject Fibronectins es_ES
dc.subject Focal Adhesion Protein-Tyrosine Kinases es_ES
dc.subject Humans es_ES
dc.subject Mice es_ES
dc.subject Microscopy, Atomic Force es_ES
dc.subject.classification FISICA APLICADA es_ES
dc.subject.classification TECNOLOGIA ELECTRONICA es_ES
dc.subject.classification TERMODINAMICA APLICADA (UPV) es_ES
dc.title Role of surface chemistry in protein remodeling at the cell-material interface es_ES
dc.type Artículo es_ES
dc.identifier.doi 10.1371/journal.pone.0019610
dc.rights.accessRights Abierto es_ES
dc.contributor.affiliation Universitat Politècnica de València. Departamento de Ingeniería Electrónica - Departament d'Enginyeria Electrònica es_ES
dc.contributor.affiliation Universitat Politècnica de València. Departamento de Física Aplicada - Departament de Física Aplicada es_ES
dc.contributor.affiliation Universitat Politècnica de València. Centro de Biomateriales e Ingeniería Tisular - Centre de Biomaterials i Enginyeria Tissular es_ES
dc.description.bibliographicCitation Llopis Hernández, V.; Rico Tortosa, PM.; Ballester Beltrán, J.; Moratal Pérez, D.; Salmerón Sánchez, M. (2011). Role of surface chemistry in protein remodeling at the cell-material interface. PLoS ONE. 6(5):19610-19620. doi:10.1371/journal.pone.0019610 es_ES
dc.description.accrualMethod Senia es_ES
dc.relation.publisherversion http://www.plosone.org/article/info:doi/10.1371/journal.pone.0019610 es_ES
dc.description.upvformatpinicio 19610 es_ES
dc.description.upvformatpfin 19620 es_ES
dc.type.version info:eu-repo/semantics/publishedVersion es_ES
dc.description.volume 6 es_ES
dc.description.issue 5 es_ES
dc.relation.senia 210685
dc.identifier.pmid 21573010 en_EN
dc.identifier.pmcid PMC3090403 en_EN
dc.contributor.funder Ministerio de Ciencia e Innovación
dc.contributor.funder Instituto de Salud Carlos III
dc.contributor.funder Fondo Europeo de Desarrollo Regional
dc.contributor.funder Generalitat Valenciana


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