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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.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.relation.projectID | info:eu-repo/grantAgreement/MICINN//MAT2009-14440-C02-01/ES/Dinamica De Las Proteinas De La Matriz En La Interfase Celula-Material/ / | es_ES |
dc.relation.projectID | info:eu-repo/grantAgreement/MICINN//MAT2009-14440-C02-02/ES/Dinamica De Las Proteinas De La Matriz En La Interfase Celula-Material/ | es_ES |
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 | S | 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 | |
dc.contributor.funder | Ministerio de Ciencia e Innovación | es_ES |
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