Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2002-2-6
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0142-9612
pubmed:author
pubmed:issnType
Print
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1519-26
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Involvement of tissue transglutaminase in the stabilisation of biomaterial/tissue interfaces important in medical devices.
pubmed:affiliation
School of Biomedical Sciences, Medical School, Queens Medical Centre, University of Nottingham, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't