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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 John; Griffin, Martin.

In: Amino Acids, Vol. 46, No. 7, 07.2014, p. 1751-1761.

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Fortunati, Dario ; Chau, David Y.S. ; Wang, Zhuo ; Collighan, Russell John ; Griffin, Martin. / Cross-linking of collagen I by tissue transglutaminase provides a promising biomaterial for promoting bone healing. In: Amino Acids. 2014 ; Vol. 46, No. 7. pp. 1751-1761.

Bibtex

@article{040d114c4dd048f8ba2fa7d433800b5c,
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.",
author = "Dario Fortunati and Chau, {David Y.S.} and Zhuo Wang and Collighan, {Russell John} and Martin Griffin",
year = "2014",
month = "7",
doi = "10.1007/s00726-014-1732-0",
language = "English",
volume = "46",
pages = "1751--1761",
journal = "Amino Acids",
issn = "0939-4451",
publisher = "Springer Wien",
number = "7",

}

RIS

TY - JOUR

T1 - Cross-linking of collagen I by tissue transglutaminase provides a promising biomaterial for promoting bone healing

AU - Fortunati, Dario

AU - Chau, David Y.S.

AU - Wang, Zhuo

AU - Collighan, Russell John

AU - Griffin, Martin

PY - 2014/7

Y1 - 2014/7

N2 - 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.

AB - 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.

U2 - 10.1007/s00726-014-1732-0

DO - 10.1007/s00726-014-1732-0

M3 - Article

VL - 46

SP - 1751

EP - 1761

JO - Amino Acids

JF - Amino Acids

SN - 0939-4451

IS - 7

ER -