Cross-linking of collagen I by tissue transglutaminase provides a promising biomaterial for promoting bone healing

Dario Fortunati, David Y.S. Chau, Zhuo Wang, Russell J. Collighan, Martin Griffin

Research output: Contribution to journalArticle

Abstract

Transglutaminases (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.

LanguageEnglish
Pages1751-1761
Number of pages11
JournalAmino Acids
Volume46
Issue number7
Early online date8 Apr 2014
DOIs
Publication statusPublished - 31 Jul 2014

Fingerprint

Biocompatible Materials
Bone
Collagen
Bone and Bones
Osteoblasts
Integrins
Focal Adhesion Protein-Tyrosine Kinases
Bone Morphogenetic Proteins
Phosphorylation
Transglutaminases
Blocking Antibodies
transglutaminase 2
Differentiation Antigens
Scaffolds
Alkaline Phosphatase
Adhesion
Peptides
Fibers

Bibliographical note

Funding: European Community [MRTN-CT-2006-036032]; EPSRC [GR/S21755/02]

Keywords

  • collagen I
  • cross-linking
  • HOB
  • integrins
  • tissue transglutaminase

Cite this

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title = "Cross-linking of collagen I by tissue transglutaminase provides a promising biomaterial for promoting bone healing",
abstract = "Transglutaminases (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.",
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Cross-linking of collagen I by tissue transglutaminase provides a promising biomaterial for promoting bone healing. / Fortunati, Dario; Chau, David Y.S.; Wang, Zhuo; Collighan, Russell J.; Griffin, Martin.

In: Amino Acids, Vol. 46, No. 7, 31.07.2014, p. 1751-1761.

Research output: Contribution to journalArticle

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AU - Chau, David Y.S.

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AU - Griffin, Martin

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