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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.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.relation.projectID | info:eu-repo/grantAgreement/MICINN//MAT2009-14440-C02-01/ES/Dinamica De Las Proteinas De La Matriz En La Interfase Celula-Material/ | |
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. https://doi.org/10.1371/journal.pone.0019610 | es_ES |
dc.description.accrualMethod | S | 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 | European Regional Development Fund | |
dc.contributor.funder | Generalitat Valenciana | |
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