Pre-osteoblasts on poly(L-lactic acid) and silicon oxide: Influence of fibronectin and albumin adsorption.
Cell adhesion and subsequent viability are critical initial steps in biomaterial-tissue integration and are strongly dependent on the material properties and the presence of matrix proteins. In the present study MC3T3-E1 osteoblast-like cell behavior on silicon oxide (SO) and poly(L-lactic acid) (PLLA) substrates has been examined, with a focus on the influence of the adhesive protein fibronectin and the non-adhesive protein albumin adsorbed on the substrates. Quartz crystal microgravimetry showed adsorption of fibronectin and albumin to be nearly identical on SO and PLLA. Subsequent exposure a previously adsorbed fibronectin layer to albumin decreased the rigidity of the adsorbed layer without any measurable increase in adsorbed mass. Cell adhesion and spreading were significantly enhanced on both SO and PLLA substrates coated with fibronectin or with fibronectin and albumin, compared with uncoated or albumin-coated substrates. The only statistically significant difference between the two substrates in these assays was increased spreading on PLLA compared with SO in the presence of fibronectin and albumin. Cell proliferation was significantly higher on SO compared with PLLA after 7 days culture, but depended on the presence of fibronectin only in the PLLA system. In contrast, mitochondrial activity was higher on PLLA than on SO, and was enhanced by fibronectin on both substrates. PLLA substrates coated with fibronectin and subsequently exposed to albumin exhibited the highest level of cell differentiation, as assayed via alkaline phosphatase activity. These results demonstrate the importance of adsorbed proteins on osteoblast-like cell-surface interactions.
Hindié
Mathilde
M
ERRMECe, Université de Cergy-Pontoise, Site Saint-Martin, France.
Degat
Marie-Christelle
MC
Gaudière
Fabien
F
Gallet
Olivier
O
Van Tassel
Paul R
PR
Pauthe
Emmanuel
E
D000327:Adsorption / Q000187:drug effects; D000469:Alkaline Phosphatase / Q000378:metabolism; D000818:Animals; D002448:Cell Adhesion / Q000187:drug effects; D049109:Cell Proliferation / Q000187:drug effects; D048430:Cell Shape / Q000187:drug effects; D002478:Cells, Cultured; D003599:Cytoskeleton / Q000187:drug effects / Q000378:metabolism; D005353:Fibronectins / Q000378:metabolism*; D006801:Humans; D019344:Lactic Acid / Q000494:pharmacology*; D051379:Mice; D018625:Microscopy, Atomic Force; D008928:Mitochondria / Q000187:drug effects / Q000378:metabolism; D010006:Osteoblasts / Q000166:cytology* / Q000187:drug effects* / Q000201:enzymology; D010087:Oxides / Q000494:pharmacology*; D011091:Polyesters; D011108:Polymers / Q000494:pharmacology*; D012709:Serum Albumin / Q000378:metabolism*; D012825:Silicon / Q000494:pharmacology*; D017655:Silicon Compounds / Q000494:pharmacology*; D013499:Surface Properties / Q000187:drug effects
D005353:Fibronectins; D010087:Oxides; D011091:Polyesters; D011108:Polymers; D012709:Serum Albumin; D017655:Silicon Compounds; D019344:Lactic Acid; C033616:poly(lactide); D000469:Alkaline Phosphatase; D012825:Silicon