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Arrangement of Type IV Collagen on NH2 and COOH Functionalized Surfaces

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Arrangement of Type IV Collagen on NH2 and COOH Functionalized Surfaces

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dc.contributor.author Miranda Coelho, Nuno es_ES
dc.contributor.author González García, Cristina es_ES
dc.contributor.author Salmerón Sánchez, Manuel es_ES
dc.contributor.author Altankov, George es_ES
dc.date.accessioned 2013-12-26T08:35:15Z
dc.date.issued 2011-07
dc.identifier.issn 0006-3592
dc.identifier.uri http://hdl.handle.net/10251/34674
dc.description.abstract Apart from the paradigm that cell-biomaterials interaction depends on the adsorption of soluble adhesive proteins we anticipate that upon distinct conditions also other, less soluble ECM proteins such as collagens, associate with the biomaterials interface with consequences for cellular response that might be of significant bioengineering interest. Using atomic force microscopy (AFM) we seek to follow the nanoscale behavior of adsorbed type IV collagen (Col IV)-a unique multifunctional matrix protein involved in the organization of basement membranes (BMs) including vascular ones. We have previously shown that substratum wettability significantly affects Col IV adsorption pattern, and in turn alters endothelial cells interaction. Here we introduce two new model surfaces based on self-assembled monolayers (SAMs), a positively charged -NH 2, and negatively charged -COOH surface, to learn more about their particular effect on Col IV behavior. AFM studies revealed distinct pattern of Col IV assembly onto the two SAMs resembling different aspects of network-like structure or aggregates (suggesting altered protein conformation). Moreover, the amount of adsorbed FITC-labeled Col IV was quantified and showed about twice more protein on NH 2 substrata. Human umbilical vein endothelial cells attached less efficiently to Col IV adsorbed on negatively charged COOH surface judged by altered cell spreading, focal adhesions formation, and actin cytoskeleton development. Immunofluorescence studies also revealed better Col IV recognition by both ¿ 1 and ¿ 2 integrins on positively charged NH 2 substrata resulting in higher phosphorylated focal adhesion kinase recruitment in the focal adhesion complexes. On COOH surface, no integrin clustering was observed. Taken altogether these results, point to the possibility that combined NH 2 and Col IV functionalization may support endothelization of cardiovascular implants. © 2011 Wiley Periodicals, Inc. es_ES
dc.description.sponsorship AFM was performed under the technical guidance of the Microscopy Service at the Universidad Politecnica de Valencia, whose advice is greatly appreciated. The work was supported by the Spanish Ministry of Science and Innovation through projects MAT2009-14440-C02-01 and MAT2009-14440-C02-02. en_EN
dc.language Inglés es_ES
dc.publisher Wiley-Blackwell es_ES
dc.relation Spanish Ministry of Science and Innovation [MAT2009-14440-C02-01, MAT2009-14440-C02-02] es_ES
dc.relation.ispartof Biotechnology and Bioengineering es_ES
dc.rights Reserva de todos los derechos es_ES
dc.subject AFM es_ES
dc.subject Collagen type IV es_ES
dc.subject Endothelial cells es_ES
dc.subject SAMs es_ES
dc.subject Surface-induced protein assembly es_ES
dc.subject Vascular grafts es_ES
dc.subject Actin cytoskeleton es_ES
dc.subject Adhesive proteins es_ES
dc.subject Adsorption patterns es_ES
dc.subject Basement membrane es_ES
dc.subject Cardiovascular implants es_ES
dc.subject Cell spreading es_ES
dc.subject Cellular response es_ES
dc.subject ECM proteins es_ES
dc.subject Focal adhesion kinase es_ES
dc.subject Focal adhesions es_ES
dc.subject Functionalizations es_ES
dc.subject Functionalized surfaces es_ES
dc.subject Human umbilical vein endothelial cells es_ES
dc.subject I-V behavior es_ES
dc.subject Integrins es_ES
dc.subject Matrix proteins es_ES
dc.subject Nano scale es_ES
dc.subject New model es_ES
dc.subject Positively charged es_ES
dc.subject Protein conformation es_ES
dc.subject Adhesion es_ES
dc.subject Adsorption es_ES
dc.subject Atomic force microscopy es_ES
dc.subject Biological materials es_ES
dc.subject Collagen es_ES
dc.subject Complexation es_ES
dc.subject Focusing es_ES
dc.subject Grafts es_ES
dc.subject Phosphorylation es_ES
dc.subject Self assembled monolayers es_ES
dc.subject Alpha1 integrin es_ES
dc.subject Alpha2 integrin es_ES
dc.subject Amine es_ES
dc.subject Biomaterial es_ES
dc.subject Carboxyl group es_ES
dc.subject Collagen type 4 es_ES
dc.subject Fluorescein isothiocyanate es_ES
dc.subject Functional group es_ES
dc.subject Article es_ES
dc.subject Bioengineering es_ES
dc.subject Blood vessel graft es_ES
dc.subject Cell interaction es_ES
dc.subject Cell structure es_ES
dc.subject Cell surface es_ES
dc.subject Endothelium cell es_ES
dc.subject Enzyme phosphorylation es_ES
dc.subject Human es_ES
dc.subject Human cell es_ES
dc.subject Immunofluorescence es_ES
dc.subject Surface property es_ES
dc.subject Umbilical vein endothelial cell es_ES
dc.subject Wettability es_ES
dc.subject Coated Materials, Biocompatible es_ES
dc.subject Humans es_ES
dc.subject Microscopy, Atomic Force es_ES
dc.subject Protein Binding es_ES
dc.subject Surface Properties es_ES
dc.subject.classification FISICA APLICADA es_ES
dc.title Arrangement of Type IV Collagen on NH2 and COOH Functionalized Surfaces es_ES
dc.type Artículo es_ES
dc.embargo.lift 10000-01-01
dc.embargo.terms forever es_ES
dc.identifier.doi 10.1002/bit.23265
dc.rights.accessRights Cerrado 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 Miranda Coelho, N.; González García, C.; Salmerón Sánchez, M.; Altankov, G. (2011). Arrangement of Type IV Collagen on NH2 and COOH Functionalized Surfaces. Biotechnology and Bioengineering. 108(12):3009-3018. doi:10.1002/bit.23265 es_ES
dc.description.accrualMethod Senia es_ES
dc.relation.publisherversion http://onlinelibrary.wiley.com/doi/10.1002/bit.23265/pdf es_ES
dc.description.upvformatpinicio 3009 es_ES
dc.description.upvformatpfin 3018 es_ES
dc.type.version info:eu-repo/semantics/publishedVersion es_ES
dc.description.volume 108 es_ES
dc.description.issue 12 es_ES
dc.relation.senia 219972


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