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dc.contributor.authorDavidenko, Nataliaen
dc.contributor.authorHamaia, Samiren
dc.contributor.authorBax, Danielen
dc.contributor.authorMalcor, Jean-Danielen
dc.contributor.authorSchuster, Carlos Fen
dc.contributor.authorGullberg, Donalden
dc.contributor.authorFarndale, Richarden
dc.contributor.authorBest, Serenaen
dc.contributor.authorCameron, Ruthen
dc.date.accessioned2018-06-05T11:38:49Z
dc.date.available2018-06-05T11:38:49Z
dc.date.issued2018-01en
dc.identifier.issn1742-7061
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/276603
dc.description.abstractAccurate evaluation of the biological performance of biomaterials requires the correct assessment of their native-like cell ligation properties. However, cell attachment studies often overlook the details of the substrate- cell binding mechanisms, be they integrin-mediated or non-specific, and ignore the class- and species-specificities of the cell adhesion receptor involved. In this work we have used different collagen (Col) substrates (fibrillar collagens I, II and III and network-forming Col IV), containing different affinity cell-recognition motifs, to establish the influence of the receptor identity and species-specificity on collagen- cell interactive properties. Receptor expression was varied by using cells of different origin, or transfecting collagen-binding integrins into integrin-null cells. These include mouse C2C12 myoblasts transfected with human α1, α2, α10 or α11; human fibrosarcoma HT1080 cells which constitutively express only human α2β1, and rat glioma Rugli cells, with only rat α1β1. Using these lines, the nature of integrin binding sites was studied in order to delineate the bioactivity of different collagen substrates. Integrin ligation was studied on collagen coatings alongside synthetic (GFOGER/GLOGEN) and Toolkit (Col II-28/Col III-7) triple-helical peptides to evaluate (1) their affinity towards different integrins and (2) to confirm the activity of the inserted integrin in the transfected cells. Thin films of dermal and tendon Col I were used to evaluate the influence of the carbodiimide (EDC)-based treatment on the cellular response on Col of different origin. The results showed that the binding properties of transfected C2C12 cells to collagens depend on the identity of inserted integrin. Similar ligation characteristics were observed using α1+ and α10+ cells, but these were distinct from the similar binding features of α2+ and α11+ cells. Recombinant human and rat-α1 I domain binding to collagens and peptides correlated with the cell adhesion results, showing receptor class- and species-specificities. The understanding of the physiologically relevant cell anchorage characteristics of bio-constructs may assist in the selection of (1) the optimum collagen source for cellular supports and (2) the correct cellular model for their biological assessment. This, in turn, may allow reliable prediction of the biological performance of bio-scaffolds in vivo for specific TE applications.
dc.format.mediumPrint-Electronicen
dc.languageengen
dc.language.isoenen
dc.publisherElsevier
dc.rightsAttribution 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectCell Lineen
dc.subjectCell Line, Tumoren
dc.subjectExtracellular Matrixen
dc.subjectAnimalsen
dc.subjectHumansen
dc.subjectMiceen
dc.subjectRatsen
dc.subjectFibrillar Collagensen
dc.subjectPeptidesen
dc.subjectReceptors, Cell Surfaceen
dc.subjectIntegrinsen
dc.subjectRecombinant Proteinsen
dc.subjectBiocompatible Materialsen
dc.subjectTissue Engineeringen
dc.subjectMaterials Testingen
dc.subjectCell Adhesionen
dc.subjectProtein Bindingen
dc.subjectModels, Biologicalen
dc.titleSelecting the correct cellular model for assessing of the biological response of collagen-based biomaterials.en
dc.typeArticle
prism.endingPage101
prism.publicationDate2018en
prism.publicationNameActa biomaterialiaen
prism.startingPage88
prism.volume65en
dc.identifier.doi10.17863/CAM.14295
dcterms.dateAccepted2017-10-25en
rioxxterms.versionofrecord10.1016/j.actbio.2017.10.035en
rioxxterms.versionVoR*
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by/4.0/en
rioxxterms.licenseref.startdate2018-01en
dc.contributor.orcidBax, Daniel [0000-0002-1162-5319]
dc.contributor.orcidMalcor, Jean-Daniel [0000-0003-4208-1294]
dc.contributor.orcidFarndale, Richard [0000-0001-6130-8808]
dc.contributor.orcidBest, Serena [0000-0001-7866-8607]
dc.contributor.orcidCameron, Ruth [0000-0003-1573-4923]
dc.identifier.eissn1878-7568
rioxxterms.typeJournal Article/Reviewen
pubs.funder-project-idBritish Heart Foundation (SP/15/7/31561)
pubs.funder-project-idEuropean Research Council (320598)
pubs.funder-project-idBritish Heart Foundation (NH/11/1/28922)
pubs.funder-project-idWellcome Trust (094470/Z/10/Z)
pubs.funder-project-idBritish Heart Foundation (RG/15/4/31268)


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Attribution 4.0 International
Except where otherwise noted, this item's licence is described as Attribution 4.0 International