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An artificial fusion protein between bone morphogenetic protein 2 and titanium‐binding peptide is functional in vivo
Author(s) -
Yuasa Kazuaki,
Kokubu Eitoyo,
Kokubun Katsutoshi,
Matsuzaka Kenichi,
Shiba Kiyotaka,
Kashiwagi Kenji,
Inoue Takashi
Publication year - 2014
Publication title -
journal of biomedical materials research part a
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.849
H-Index - 150
eISSN - 1552-4965
pISSN - 1549-3296
DOI - 10.1002/jbm.a.34765
Subject(s) - bone sialoprotein , in vivo , materials science , bone morphogenetic protein 2 , bone morphogenetic protein , alkaline phosphatase , microbiology and biotechnology , titanium , biochemistry , chemistry , in vitro , biology , osteocalcin , gene , enzyme , metallurgy
The purpose of this study was to investigate osteogenesis using an artificial fusion protein (AFP) composed of modified bone morphogenetic protein 2 (BMP‐2) with a titanium (Ti)‐binding peptide (TBP) motif on a Ti surface in vivo . In the in vivo study, 5‐μm thick Ti was coated with electron cyclotron resonance sputtering on a porous carbon scaffold which was then dipped in one of three different mixtures of collagen gel: (1) collagen gel only, (2) collagen gel with TBP, and (3) collagen gel with the AFP between BMP‐2 and the TBP motif (AFP‐TBP–BMP‐2). These scaffolds were then implanted into rat abdominal muscles and were studied histologically at various times and the expression of several bone‐related protein messenger RNAs (mRNAs) was also analyzed. The Ti‐coated scaffold of the collagen gel with AFP‐TBP–BMP‐2 produced cartilage in the muscle and the expression of alkaline phosphatase, bone sialoprotein, and runt‐related gene 2 mRNAs was significantly increased. These results suggest that the scaffold of the collagen gel with AFP‐TBP–BMP‐2 accelerates osteogenesis in vivo . © 2013 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 102A: 1180–1186, 2014.