Activation of demineralized bone matrix by genetically engineered human bone morphogenetic protein-2 with a collagen binding domain derived from von Willebrand factor propolypeptide
Activation of demineralized bone matrix by genetically engineered human bone morphogenetic protein-2 with a collagen binding domain derived from von Willebrand factor propolypeptide
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DOI：
10.1002/jbm.a.30900
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发表时间：
2007-02-01
影响因子：
4.9
通讯作者：
Dai, Jianwu
中科院分区：
文献类型：
--
作者：
Chen, Bing;Lin, Hang;Dai, Jianwu
在骨损伤期间，对新骨再生以恢复功能存在大量需求。骨填充材料是骨组织修复的重要材料。本研究以工程化人骨形态发生蛋白-2（BMP-2）活化脱钙骨基质（DBM）。为了增强BMP-2与DBM支架的结合，将胶原结合肽融合到BMP-2的N-末端。体外实验结果表明，rhBMP-2-v能与DBM支架特异性结合，并能提高C2 C12细胞的碱性磷酸酶活性。在体内实验中，rhBMP 2-v浸渍的DBM支架显示出更大的异位成骨作用。实验结果表明，以胶原蛋白为载体的BMP-2靶向骨修复系统的骨诱导能力明显高于以常规BMP-2为载体的DBM。(c)2006 Wiley Periodicals，Inc.
There is a large demand for new bone regeneration to restore the function during bone injuries. Bone filling materials are important in bone tissue restoration. In this study, the demineralized bone matrix (DBM) was activated with the engineering human bone morphogenetic protein-2 (BMP-2). To enhance the binding of BMP-2 to the DBM scaffolds, a collagen-binding peptide was fused to the N-terminal of BMP-2. The in vitro results showed that the engineered collagen-targeted BMP-2 (rhBMP2-v) bound to DBM scaffolds specifically and the rhBMP2-v had increased alkaline phosphatase activity in C2C12 cells. In vivo, the DBM scaffolds impregnated with rhBMP2-v showed greater effect on ectopic bone formation. Our data suggested that the collagen-based BMP-2 targeting bone repair system had greater bone inducing ability than DBM loaded with regular BMP-2. (c) 2006 Wiley Periodicals, Inc.