Involvement of tissue transglutaminase in the stabilisation of biomaterial/tissue interfaces important in medical devices

Deborah J. Heath, Paul Christian, Martin Griffin

Research output: Contribution to journalArticle

Abstract

Tissue transglutaminase (tTG) has recently been established as a novel cell surface adhesion protein that binds with high affinity to fibronectin in the pericellular matrix. In this study, we have made use of this property to enhance the biocompatibility of poly(epsilon-caprolactone) (PCL), a biomaterial currently used in bone repair. Poly(epsilon-caprolactone) discs were first coated with fibronectin and then tTG. The surface localisation of the two proteins was confirmed using ELISA and the tTG shown to be active on the surface by incorporation of biotin cadaverine into the fibronectin coating. When human osteoblasts (HOBs) were seeded onto the coated polymer surfaces in serum free medium, the surface coated with fibronectin and then tTG showed an increase in the spreading of the cells as compared to the surface coated with fibronectin alone, when analysed using environmental scanning electron microscopy. The presence of tTG had no effect on HOB cell differentiation when analysed by determining alkaline phosphatase activity. The use of tTG as a novel adhesion protein in this way may therefore have considerable potential in forming a stable tissue/biomaterial interface for application in medical devices.
Original languageEnglish
Pages (from-to)1519-1526
Number of pages8
JournalBiomaterials
Volume23
Issue number6
Early online date27 Sep 2001
DOIs
Publication statusPublished - Mar 2002

Keywords

  • human osteoblasts
  • tissue transglutaminase
  • ECM stabilisation
  • poly(ε-caprolactone)
  • bioactive biomaterial

Fingerprint Dive into the research topics of 'Involvement of tissue transglutaminase in the stabilisation of biomaterial/tissue interfaces important in medical devices'. Together they form a unique fingerprint.

Cite this