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Improvements of osteoblast adhesion, proliferation, and differentiation in vitro via fibrin network formation in collagen sponge scaffold
Author(s) -
Kim BeomSu,
Kim Jin Seong,
Lee Jun
Publication year - 2013
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.34567
Subject(s) - fibrin , biocompatibility , materials science , scaffold , adhesion , sponge , alkaline phosphatase , cell adhesion , osteoblast , in vitro , biomedical engineering , microbiology and biotechnology , biochemistry , biology , immunology , botany , enzyme , composite material , medicine , metallurgy
Collagen sponges (COL‐S) are used as scaffolds to support osteoblasts and stimulate bone repair because of their flexibility, biocompatibility, and biodegradability. In this study, we added fibrin networks to COL‐S scaffolds by using a fibrinogen (FNG) cross‐linking reaction and evaluated the proliferation, differentiation, and adhesion of MG‐63 cells on these scaffolds. The fibrin network that formed in COL‐S with various concentrations of FNG was characterized with regard to morphology, porosity, and water‐uptake ability. Successful fibrin network formation was observed by scanning electron microscopy (SEM). As the FNG concentration increased, network formation increased, but porosity and water‐uptake ability were slightly reduced at high FNG concentrations. An MTS assay, DNA content assay, live/dead fluorescence assay, and SEM imaging showed that MG‐63 cells attached and spread on COL‐S and COL‐S/FNG scaffolds, particularly on scaffolds modified using FNG. In addition, alkaline phosphatase (ALP) activity was significantly increased in cells cultured on scaffolds modified using 10, 40, and 80 mg/mL FNG. Thus, the addition of a fibrin network could increase the biocompatibility of COL‐S for bone regeneration. © 2013 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 101A: 2661–2666, 2013.