Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
33
pubmed:dateCreated
2005-7-26
pubmed:abstractText
Collagen, type I, is a highly abundant natural protein material which has been cross-linked by a variety of methods including chemical agents, physical heating and UV irradiation with the aim of enhancing its physical characteristics such as mechanical strength, thermal stability, resistance to proteolytic breakdown, thus increasing its overall biocompatibility. However, in view of the toxicity of residual cross-linking agents, or impracticability at large scales, it would be more useful if the collagen could be cross-linked by a milder, efficient and more practical means by using enzymes as biological catalysts. We demonstrate that on treating native collagen type I (from bovine skin) with both tissue transglutaminase (TG2; tTG) and microbial transglutaminase (mTG; Streptoverticillium mobaraense) leads to an enhancement in cell attachment, spreading and proliferation of human osteoblasts (HOB) and human foreskin dermal fibroblasts (HFDF) when compared to culture on native collagen. The transglutaminase-treated collagen substrates also showed a greater resistance to cell-mediated endogenous protease degradation than the native collagen. In addition, the HOB cells were shown to differentiate at a faster rate than on native collagen when assessed by measurement of alkaline phosphatase activity and osteopontin expression.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Alkaline Phosphatase, http://linkedlifedata.com/resource/pubmed/chemical/Biocompatible Materials, http://linkedlifedata.com/resource/pubmed/chemical/Biological Markers, http://linkedlifedata.com/resource/pubmed/chemical/Collagen, http://linkedlifedata.com/resource/pubmed/chemical/Collagen Type I, http://linkedlifedata.com/resource/pubmed/chemical/Collagenases, http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents, http://linkedlifedata.com/resource/pubmed/chemical/Dipeptides, http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Gelatin, http://linkedlifedata.com/resource/pubmed/chemical/Osteopontin, http://linkedlifedata.com/resource/pubmed/chemical/SPP1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Sialoglycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Transglutaminases, http://linkedlifedata.com/resource/pubmed/chemical/epsilon-(gamma-glutamyl)-lysine, http://linkedlifedata.com/resource/pubmed/chemical/transglutaminase 2
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0142-9612
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6518-29
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:15927250-Alkaline Phosphatase, pubmed-meshheading:15927250-Animals, pubmed-meshheading:15927250-Biocompatible Materials, pubmed-meshheading:15927250-Biological Markers, pubmed-meshheading:15927250-Catalysis, pubmed-meshheading:15927250-Cattle, pubmed-meshheading:15927250-Cell Differentiation, pubmed-meshheading:15927250-Cell Proliferation, pubmed-meshheading:15927250-Cell Survival, pubmed-meshheading:15927250-Cells, Cultured, pubmed-meshheading:15927250-Collagen, pubmed-meshheading:15927250-Collagen Type I, pubmed-meshheading:15927250-Collagenases, pubmed-meshheading:15927250-Cross-Linking Reagents, pubmed-meshheading:15927250-Dipeptides, pubmed-meshheading:15927250-Fibroblasts, pubmed-meshheading:15927250-GTP-Binding Proteins, pubmed-meshheading:15927250-Gelatin, pubmed-meshheading:15927250-Hot Temperature, pubmed-meshheading:15927250-Humans, pubmed-meshheading:15927250-Osteoblasts, pubmed-meshheading:15927250-Osteopontin, pubmed-meshheading:15927250-Sialoglycoproteins, pubmed-meshheading:15927250-Time Factors, pubmed-meshheading:15927250-Transglutaminases, pubmed-meshheading:15927250-Ultraviolet Rays, pubmed-meshheading:15927250-Wound Healing
pubmed:year
2005
pubmed:articleTitle
The cellular response to transglutaminase-cross-linked collagen.
pubmed:affiliation
School of Biomedical and Natural Sciences, The Nottingham Trent University, Clifton, Nottingham, NG11 8NS, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't