Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2010-2-26
pubmed:abstractText
Textile chitosan fibre scaffolds were evaluated in terms of interaction with osteoclast-like cells, derived from human primary monocytes. Part of the scaffolds was further modified by coating with fibrillar collagen type I in order to make the surface biocompatible. Monocytes were cultured directly on the scaffolds in the presence of macrophage colony stimulating factor (M-CSF) and receptor activator of nuclear factor kappaB ligand (RANKL) for up to 18 days. Confocal laser scanning microscopy (CLSM) as well as scanning electron microscopy (SEM) revealed the formation of multinuclear osteoclast-like cells on both the raw chitosan fibres and the collagen-coated scaffolds. The modified surface supported the osteoclastogenesis. Differentiation towards the osteoclastic lineage was confirmed by the microscopic detection of cathepsin K, tartrate resistant acid phosphatase (TRAP), acidic compartments using 3-(2,4-dinitroanillino)-3'-amino-N-methyldipropylamine (DAMP), immunological detection of TRAP isoform 5b, and analysis of gene expression of the osteoclastic markers TRAP, cathepsin K, vitronectin receptor, and calcitonin receptor using reverse transcription-polymerase chain reaction (RT-PCR). The feature of the collagen-coated but also of the raw chitosan fibre scaffolds to support attachment and differentiation of human monocytes facilitates cell-induced material resorption--one main requirement for successful bone tissue engineering.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Acid Phosphatase, http://linkedlifedata.com/resource/pubmed/chemical/Biological Markers, http://linkedlifedata.com/resource/pubmed/chemical/Bone Substitutes, http://linkedlifedata.com/resource/pubmed/chemical/CTSK protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin K, http://linkedlifedata.com/resource/pubmed/chemical/Chitosan, http://linkedlifedata.com/resource/pubmed/chemical/Collagen, http://linkedlifedata.com/resource/pubmed/chemical/Integrin alphaVbeta3, http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes, http://linkedlifedata.com/resource/pubmed/chemical/Macrophage Colony-Stimulating Factor, http://linkedlifedata.com/resource/pubmed/chemical/RANK Ligand, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Calcitonin, http://linkedlifedata.com/resource/pubmed/chemical/TNFSF11 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/tartrate-resistant acid phosphatase
pubmed:status
MEDLINE
pubmed:issn
1473-2262
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
96-106
pubmed:meshHeading
pubmed-meshheading:20186669-Acid Phosphatase, pubmed-meshheading:20186669-Biological Markers, pubmed-meshheading:20186669-Bone Substitutes, pubmed-meshheading:20186669-Cathepsin K, pubmed-meshheading:20186669-Cell Differentiation, pubmed-meshheading:20186669-Cell Lineage, pubmed-meshheading:20186669-Cell Proliferation, pubmed-meshheading:20186669-Cells, Cultured, pubmed-meshheading:20186669-Chitosan, pubmed-meshheading:20186669-Collagen, pubmed-meshheading:20186669-Humans, pubmed-meshheading:20186669-Integrin alphaVbeta3, pubmed-meshheading:20186669-Isoenzymes, pubmed-meshheading:20186669-Macrophage Colony-Stimulating Factor, pubmed-meshheading:20186669-Microscopy, Confocal, pubmed-meshheading:20186669-Microscopy, Electron, Scanning, pubmed-meshheading:20186669-Monocytes, pubmed-meshheading:20186669-Osteoclasts, pubmed-meshheading:20186669-RANK Ligand, pubmed-meshheading:20186669-Receptors, Calcitonin, pubmed-meshheading:20186669-Tissue Engineering, pubmed-meshheading:20186669-Tissue Scaffolds
pubmed:year
2010
pubmed:articleTitle
In vitro osteoclastogenesis on textile chitosan scaffold.
pubmed:affiliation
Max Bergmann Center of Biomaterials and Institute of Materials Science, Dresden University of Technology, Budapester Str. 27, D-01069 Dresden, Germany. christiane.heinemann@tu-dresden.de
pubmed:publicationType
Journal Article