Functional glass slides for in vitro evaluation of interactions between bone cells and mineral-binding surfaces
UMass Chan AffiliationsDepartment of Cell Biology
Department of Orthopedics and Physical Rehabilitation
Document TypeJournal Article
Rehabilitation and Therapy
MetadataShow full item record
AbstractPrimary amine-functionalized glass slides obtained through a multi-step plasma treatment were conjugated with anionic amino acids that are frequently found as mineral binding elements in acidic extracellular matrix components of natural bone. The modified glass surfaces were characterized by X-ray photoelectron spectroscopy (XPS) and contact angle measurements. Human osteosarcoma TE85 cells were cultured on these functionalized slides and analyses on both protein and gene expression levels were performed to probe the ‘‘biocompatibility’’ of the surface ligands. Cell attachment and proliferation on anionic surfaces were either better than or comparable to those of cells cultured on tissue culture polystyrene (TCPS). The modified glass surfaces promoted the expression of osteocalcin, alkaline phosphatase activity and ECM proteins such as fibronectin and vitronectin under differentiation culture conditions. Transcript analysis using gene chip microarrays confirmed that culturing TE85 cells on anionic surfaces did not activate apoptotic pathways. Collectively, these results suggest that the potential mineral-binding anionic ligands examined here do not exert significant adverse effects on the expression of important osteogenic markers of TE85 cells. This work paves the way for the incorporation of these ligands into 3-dimensional artificial bone-like scaffolds.
SourceSong J, Chen J, Klapperich CM, Eng V, Bertozzi CR. Functional glass slides for in vitro evaluation of interactions between bone cells and mineral-binding surfaces. J Mater Chem. 2004 Jan; 14: 2643-2648. Link to article on publisher's website
Permanent Link to this Itemhttp://hdl.handle.net/20.500.14038/43072
At the time of publication, Jie Song was not yet affiliated with the University of Massachusetts Medical School.