Effect of BMP-2 and/or BMP-9 on preosteoblasts attached to polycaprolactone functionalized by adhesive peptides derived from bone sialoprotein

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• 作者：Olivier Drevelle ; Alex Daviau ; Marc-Antoine Lauzon ; Nathalie Faucheux ; ^{Nathalie.Faucheux@usherbrooke.ca}
• 关键词：Alkaline phosphatase ; Cell signalling ; Cell activation ; Gene expression ; RGD peptide
• 刊名：Biomaterials
• 出版年：2013
• 出版时间：January, 2013
• 年：2013
• 卷：34
• 期：4
• 页码：1051-1062
• 全文大小：1607 K

文摘

Biomaterials functionalized by adhesive peptides improve the cell-substratum interaction. However, their influence on the response of cells to growth factors is still poorly understood. We have shown that bone morphogenetic protein (BMP) 2 activates the Smad pathway only in murine MC3T3-E1 preosteoblasts attached to polycaprolactone (PCL) film functionalized by RGD peptides derived from bone sialoprotein (pRGD). We have now analysed the way recombinant human BMP-2 and/or BMP-9 (0.38?nM) influence the signal transduction and differentiation of MC3T3-E1 preosteoblasts attached to PCL-pRGD. While kinetics of MAPK activation were similar in cells treated by BMP-2 and BMP-9, different kinetics of Smad activation and ¦Â-catenin stabilization were observed. BMP-2 induced Smad1/5/8 phosphorylation within 0.5 and BMP-9 within 4?h, while the ¦Â-catenin was lower at 2?h only in cells treated with BMP-9. However, both BMPs induced the translocation of phosphorylated Smad1/5/8 to the nucleus at 4?h and increased Dlx5, osterix and osteocalcin transcripts as well as alkaline phosphatase activity at 72?h. A BMP-2/BMP-9 combination that maintained the ¦Â-catenin amount constant but reduced that of phosphorylated Smad within 4?h had quite similar effect than BMP-2 alone. It is therefore important to determine how biomimetic materials influence the response of cells to BMPs.