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

<h4>Background</h4>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 materia...

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Autores principales:	Virginia Llopis-Hernández, Patricia Rico, José Ballester-Beltrán, David Moratal, Manuel Salmerón-Sánchez
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/8127d2c2768240c7a4638bfcf44bd76e
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spelling	oai:doaj.org-article:8127d2c2768240c7a4638bfcf44bd76e2021-11-18T06:54:18ZRole of surface chemistry in protein remodeling at the cell-material interface.1932-620310.1371/journal.pone.0019610https://doaj.org/article/8127d2c2768240c7a4638bfcf44bd76e2011-05-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21573010/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>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.<h4>Methodology/principal findings</h4>This work investigates matrix protein dynamics on mixed self-assembled monolayers (SAMs) of -OH and -CH(3) 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.<h4>Conclusions/significance</h4>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.Virginia Llopis-HernándezPatricia RicoJosé Ballester-BeltránDavid MoratalManuel Salmerón-SánchezPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 5, p e19610 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Virginia Llopis-Hernández Patricia Rico José Ballester-Beltrán David Moratal Manuel Salmerón-Sánchez Role of surface chemistry in protein remodeling at the cell-material interface.
description	<h4>Background</h4>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.<h4>Methodology/principal findings</h4>This work investigates matrix protein dynamics on mixed self-assembled monolayers (SAMs) of -OH and -CH(3) 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.<h4>Conclusions/significance</h4>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.
format	article
author	Virginia Llopis-Hernández Patricia Rico José Ballester-Beltrán David Moratal Manuel Salmerón-Sánchez
author_facet	Virginia Llopis-Hernández Patricia Rico José Ballester-Beltrán David Moratal Manuel Salmerón-Sánchez
author_sort	Virginia Llopis-Hernández
title	Role of surface chemistry in protein remodeling at the cell-material interface.
title_short	Role of surface chemistry in protein remodeling at the cell-material interface.
title_full	Role of surface chemistry in protein remodeling at the cell-material interface.
title_fullStr	Role of surface chemistry in protein remodeling at the cell-material interface.
title_full_unstemmed	Role of surface chemistry in protein remodeling at the cell-material interface.
title_sort	role of surface chemistry in protein remodeling at the cell-material interface.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/8127d2c2768240c7a4638bfcf44bd76e
work_keys_str_mv	AT virginiallopishernandez roleofsurfacechemistryinproteinremodelingatthecellmaterialinterface AT patriciarico roleofsurfacechemistryinproteinremodelingatthecellmaterialinterface AT joseballesterbeltran roleofsurfacechemistryinproteinremodelingatthecellmaterialinterface AT davidmoratal roleofsurfacechemistryinproteinremodelingatthecellmaterialinterface AT manuelsalmeronsanchez roleofsurfacechemistryinproteinremodelingatthecellmaterialinterface
_version_	1718424239629926400

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

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