MISC

2009年3月

Immobilized recombinant human bone morphogenetic protein-2 enhances the phosphorylation of receptor-activated Smads

JOURNAL OF BIOMEDICAL MATERIALS RESEARCH PART A
  • Eiki Yamachika
  • ,
  • Hidetsugu Tsujigiwa
  • ,
  • Nobuaki Shirasu
  • ,
  • Takaaki Ueno
  • ,
  • Yoshirou Sakata
  • ,
  • Loji Fukunaga
  • ,
  • Nobuyoshi Mizukawa
  • ,
  • Masao Yamada
  • ,
  • Toshio Sugahara

88A
3
開始ページ
599
終了ページ
607
記述言語
英語
掲載種別
DOI
10.1002/jbm.a.31833
出版者・発行元
WILEY-LISS

Bone morphogenctic protein (BMP)-2 plays an important role in bone growth and regeneration; however, BMP2 is easily lost by diffusion through body fluid and has some inhibitory pathways. To address this problem, we previously immobilized recombinant human BMP-2 (rhBMP-2) oil succinylated type I atelocollagen. Here, we examined the effect of immobilized rhBMP-2 in vitro and vivo. In ST2, MC3T3-E1, and C2C12 cells, alkaline phosphatase activity, which is a marker of osteoblast differentiation, was enhanced more by immobilized than nonimmobilized rhBMP-2. In addition, the phosphorylation of receptor-activated Smads, part of the signaling pathway activated by BMP-2, was prolonged by immobilized rhBW-2 in these cells. Furthermore, implantation of immobilized rhBMP-2 in to the backs of rats prornoted the formation of mature bone-like structure. These results demonstrate that immobilized rhBW-2 has higher bioactivity than nonimmobilized rhBMP-2, and, therefore, immobilization of rhBMP-2 can prolong BMP signaling. (c) 2008 Wiley Periodicals, Inc. J Biomed Mater Res 88A: 599-607, 2009

Web of Science ® 被引用回数 : 29

リンク情報
DOI
https://doi.org/10.1002/jbm.a.31833
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000263126000005&DestApp=WOS_CPL

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