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Osteocalcin/fibronectin‐functionalized collagen matrices for bone tissue engineering
Author(s) -
Kim S. G.,
Lee D. S.,
Lee S.,
Jang J.H.
Publication year - 2015
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.35351
Subject(s) - osteocalcin , fibronectin , alkaline phosphatase , extracellular matrix , materials science , tissue engineering , biocompatibility , type i collagen , matrix (chemical analysis) , bone tissue , decellularization , biomedical engineering , biochemistry , chemistry , biology , enzyme , medicine , endocrinology , composite material , metallurgy
Collagen is the most abundant protein found in the extracellular matrix and is widely used to build scaffolds for biomedical applications which are the result of its biocompatibility and biodegradability. In the present study, we constructed a rhOCN/FN III9‐10 fusion protein and rhOCN/FN III9‐10 ‐functionalized collagen matrices and investigated the potential value for bone tissue engineering. In vitro studies carried out with preosteoblastic MC3T3‐E1 cells showed that rhOCN/FN III9‐10 fusion protein promoted cell adhesion and the mRNA levels of osteogenic markers including osteocalcin, runt‐related transcription factor 2, alkaline phosphatase (ALP), and collagen type I. In addition, rhOCN/FN III9‐10 ‐functionalized collagen matrices showed significant induction of the ALP activity more than rhFN III9‐10 ‐functionalized collagen matrices or collagen matrices alone. These results suggested that rhOCN/FN III9‐10 ‐functionalized collagen matrices have potential for bone tissue engineering. © 2014 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 103A: 2133–2140, 2015.