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dc.contributor.authorChau, David Y.S.
dc.contributor.authorCollighan, R.J.
dc.contributor.authorVerderio, E.A.M.
dc.contributor.authorAddy, V.L.
dc.contributor.authorGriffin, M.
dc.date.accessioned2013-12-19T14:30:23Z
dc.date.available2013-12-19T14:30:23Z
dc.date.issued2005-11
dc.identifier.citationChau , D Y S , Collighan , R J , Verderio , E A M , Addy , V L & Griffin , M 2005 , ' The cellular response to transglutaminase-cross-linked collagen ' , Biomaterials , vol. 26 , no. 33 , pp. 6518-6529 . https://doi.org/10.1016/j.biomaterials.2005.04.017
dc.identifier.issn0142-9612
dc.identifier.otherPURE: 2586109
dc.identifier.otherPURE UUID: 38b28f45-3549-4add-a4df-930c267ff71e
dc.identifier.otherWOS: 000231189800012
dc.identifier.otherScopus: 22544438722
dc.identifier.urihttp://hdl.handle.net/2299/12443
dc.description.abstractCollagen, type 1, is a highly abundant natural protein material which has been cross-linked by 11 variety of methods including chemical agents, physical heating and UV irradiation with the aim of enhancing its physical characteristics such as mechanical strength, thermal stability, resistance to proteolytic breakdown, thus increasing its overall biocompatibility. However, in view of the toxicity of residual cross-linking agents, or impracticability at large scales, it would be more useful if the collagen Could be crosslinked by a milder, efficient and more practical means by using enzymes as biological catalysts. We demonstrate that on treating native collagen type I (from bovine skin) with both tissue transglutaminase (TG2. tTG)) and microbial transglutaminase (mTG; Streptoverticillium mobaraense) leads to an enhancement in cell attachment, spreading and proliferation of human osteoblasts (HOB) and human foreskin dermal fibroblasts (HFDF) when compared to Culture on native collagen. The transglutaminase-treated collagen substrates also showed a greater resistance to cell-mediated endogenous protease degradation than the native collagen. In addition, the HOB cells were shown to differentiate at a faster rate than on native collagen when assessed by measurement of alkaline phosphatase activity and osteopontin expression. (c) 2005 Elsevier Ltd. All rights reserved.en
dc.format.extent12
dc.language.isoeng
dc.relation.ispartofBiomaterials
dc.subjectbioactivity
dc.subjectbiocompatibility
dc.subjectcollagen
dc.subjectfibroblasts
dc.subjectosteoblasts
dc.subjecttissue engineering
dc.subjectHUMAN DERMAL FIBROBLASTS
dc.subjectTISSUE TRANSGLUTAMINASE
dc.subjectI COLLAGEN
dc.subjectFIBRONECTIN
dc.subjectACTIVATION
dc.subjectEXPRESSION
dc.subjectENZYME
dc.subjectCELLS
dc.subjectPOLYMERIZATION
dc.subjectADHESION
dc.titleThe cellular response to transglutaminase-cross-linked collagenen
dc.contributor.institutionSchool of Life and Medical Sciences
dc.contributor.institutionHealth & Human Sciences Research Institute
dc.contributor.institutionDepartment of Pharmacy
dc.description.statusPeer reviewed
dc.relation.schoolSchool of Life and Medical Sciences
dcterms.dateAccepted2005-11
rioxxterms.versionofrecordhttps://doi.org/10.1016/j.biomaterials.2005.04.017
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue


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