Chondrogenic differentiation of human mesenchymal stem cells on fish scale collagen
Section snippets
Collagen observation by scanning electron microscopy
Tilapia collagen was prepared using Cell Campus AQ-03A (Taki Chemical, Hyogo, Japan; 0.3%, pH 3.0). Porcine collagen were prepared with Cellmatrix I-C (Nitta Gelatin, Osaka, Japan; 0.3%, pH 3.0) for comparison. For scanning electron microscopy (SEM) observation, tilapia and porcine collagen solution were adjusted to 0.2 ml 0.1% collagen/PBS and added to a 1.5 ml tube and incubated at 30°C for 3 h. Gel-like collagen fibrils were treated with 4% paraformaldehyde (Sigma–Aldrich, SL, USA) for
Morphology of tilapia scale and porcine collagen fibrils
To compare collagen fibrils formed from tilapia scale and porcine collagen molecules, both collagen fibrils were observed by SEM. Tilapia collagen formed fibrils of 1.0–2.5 μm diameter (Fig. 1A), whereas porcine collagen formed fibrils of 0.5–1.5 μm diameter (Fig. 1B). Images also showed that tilapia collagen fibrils looked helically coiled (Fig. 1A), whereas porcine collagen showed a simpler structure with individual fibrils (Fig. 1B).
Safranin O staining of hMSCs on tilapia and porcine collagens
hMSCs were pre-cultured on tilapia and porcine
Discussion
The rapid regeneration potential of fish scales has been reported previously 8, 9, especially of tilapia scales, in which collagen is highly orientated and has the potential for rapid fibril formation (9). Compared with other fish species, the denaturing temperature of tilapia collagen is higher and suitable for tissue or cell culture at 37°C (5). Furthermore, tilapia collagen showed rapid fibril formation and facilitated early hMSC osteoblastic differentiation (3). On the other hand, the risk
Acknowledgment
We thank Dr. Hiroshi Itoh, Dainichiseika Color & Chemicals Mfg. Co., Ltd., for technical supports.
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Present address: Department of Precision Science and Technology, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan.