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dc.contributor.authorFortunati, Dario
dc.contributor.authorChau, David Y.S.
dc.contributor.authorWang, Zhuo
dc.contributor.authorCollighan, Russell John
dc.contributor.authorGriffin, Martin
dc.date.accessioned2014-08-06T14:30:36Z
dc.date.available2014-08-06T14:30:36Z
dc.date.issued2014-07
dc.identifier.citationFortunati , D , Chau , D Y S , Wang , Z , Collighan , R J & Griffin , M 2014 , ' Cross-linking of collagen I by tissue transglutaminase provides a promising biomaterial for promoting bone healing ' , Amino Acids , vol. 46 , no. 7 , pp. 1751-1761 . https://doi.org/10.1007/s00726-014-1732-0
dc.identifier.issn0939-4451
dc.identifier.otherPURE: 2933888
dc.identifier.otherPURE UUID: 040d114c-4dd0-48f8-ba2f-a7d433800b5c
dc.identifier.otherPubMed: 24710705
dc.identifier.otherScopus: 84903646832
dc.identifier.urihttp://hdl.handle.net/2299/14257
dc.description.abstractTransglutaminases (TGs) stabilize proteins by the formation of ε(γ-glutamyl)lysine cross-links. Here, we demonstrate that the cross-linking of collagen I (COL I) by tissue transglutaminase (TG2) causes an alteration in the morphology and rheological properties of the collagen fibers. Human osteoblasts (HOB) attach, spread, proliferate, differentiate and mineralize more rapidly on this cross-linked matrix compared to native collagen. When seeded on cross-linked COL I, HOB are more resistant to the loss of cell spreading by incubation with RGD containing peptides and with α1, α2 and β1 integrin blocking antibodies. Following adhesion on cross-linked collagen, HOB show increased phosphorylation of the focal adhesion kinase, and increased expression of β1 and β3 integrins. Addition of human bone morphogenetic protein to HOB seeded on TG2 cross-linked COL I enhanced the expression of the differentiation marker bone alkaline phosphatase when compared to cross-linked collagen alone. In summary, the use of TG2-modified COL I provides a promising new scaffold for promoting bone healing.en
dc.format.extent11
dc.language.isoeng
dc.relation.ispartofAmino Acids
dc.titleCross-linking of collagen I by tissue transglutaminase provides a promising biomaterial for promoting bone healingen
dc.contributor.institutionSchool of Life and Medical Sciences
dc.contributor.institutionDepartment of Pharmacy
dc.contributor.institutionHealth & Human Sciences Research Institute
dc.contributor.institutionCentre for Research into Topical Drug Delivery and Toxicology
dc.description.statusPeer reviewed
dc.relation.schoolSchool of Life and Medical Sciences
dcterms.dateAccepted2014-07
rioxxterms.versionP
rioxxterms.versionVoR
rioxxterms.versionofrecordhttps://doi.org/10.1007/s00726-014-1732-0
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue


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