Rapid oriented fibril formation of fish scale collagen facilitates early osteoblastic differentiation of human mesenchymal stem cells

被引:42
作者
Matsumoto, Rena [1 ]
Uemura, Toshimasa [1 ]
Xu, Zhefeng [2 ]
Yamaguchi, Isamu [3 ]
Ikoma, Toshiyuki [2 ]
Tanaka, Junzo [2 ]
机构
[1] AIST Natl Inst Adv Ind Sci & Technol, Nanosyst Res Insutitute, Tsukuba, Ibaraki 3058562, Japan
[2] Tokyo Inst Technol, Dept Met & Ceram Sci, Meguro Ku, Tokyo 1528550, Japan
[3] Taki Chem Co Ltd, Res Dept, R&D Div, Harima, Hyogo 6750145, Japan
关键词
type I collagen; tilapia scales; human mesenchymal stem cells; osteoblastic differentiation; fibril formation; high-speed atomic force microscopy; I COLLAGEN; PAGRUS-MAJOR; CULTURE; BONE; OSTEOGENESIS; FIBROBLASTS; MODEL; VITRO;
D O I
10.1002/jbm.a.35387
中图分类号
R318 [生物医学工程];
学科分类号
0831 ;
摘要
We studied the effect of fibril formation of fish scale collagen on the osteoblastic differentiation of human mesenchymal stem cells (hMSCs). We found that hMSCs adhered easily to tilapia scale collagen, which remarkably accelerated the early stage of osteoblastic differentiation in hMSCs during in vitro cell culture. Osteoblastic markers such as ALP activity, osteopontin, and bone morphogenetic protein 2 were markedly upregulated when the hMSCs were cultured on a tilapia collagen surface, especially in the early osteoblastic differentiation stage. We hypothesized that this phenomenon occurs due to specific fibril formation of tilapia collagen. Thus, we examined the time course of collagen fibril formation using high-speed atomic force microscopy. Moreover, to elucidate the effect of the orientation of fibril formation on the differentiation of hMSCs, we measured ALP activity of hMSCs cultured on two types of tilapia scale collagen membranes with different degrees of fibril formation. The ALP activity in hMSCs cultured on a fibrous collagen membrane was significantly higher than on a non-fibrous collagen membrane even before adding osteoblastic differentiation medium. These results showed that the degree of the fibril formation of tilapia collagen was essential for the osteoblastic differentiation of hMSCs. (c) 2014 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 103A: 2531-2539, 2015.
引用
收藏
页码:2531 / 2539
页数:9
相关论文
共 33 条
[11]   Microstructure, mechanical, and biomimetic properties of fish scales from Pagrus major [J].
Ikoma, T ;
Kobayashi, H ;
Tanaka, J ;
Walsh, D ;
Mann, S .
JOURNAL OF STRUCTURAL BIOLOGY, 2003, 142 (03) :327-333
[12]  
Ke N, 2011, METHODS MOL BIOL, V740, P33, DOI 10.1007/978-1-61779-108-6_6
[13]   CHARACTERIZATION OF FISH MUSCLE TYPE-I COLLAGEN [J].
KIMURA, S ;
ZHU, XP ;
MATSUI, R ;
SHIJOH, M ;
TAKAMIZAWA, S .
JOURNAL OF FOOD SCIENCE, 1988, 53 (05) :1315-1318
[14]   Evaluation and Comparison of the Species-Specificity of 3 Antiparvalbumin IgG Antibodies [J].
Lee, Poi-Wah ;
Nordlee, Julie A. ;
Koppelman, Stef J. ;
Baumert, Joseph L. ;
Taylor, Steve L. .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2011, 59 (23) :12309-12316
[15]  
LEWKO WM, 1989, CANCER-AM CANCER SOC, V64, P1600, DOI 10.1002/1097-0142(19891015)64:8<1600::AID-CNCR2820640808>3.0.CO
[16]  
2-S
[17]   Tropomyosin from tilapia (Oreochromis mossambicus) as an allergen [J].
Liu, R. ;
Holck, A. L. ;
Yang, E. ;
Liu, C. ;
Xue, W. .
CLINICAL AND EXPERIMENTAL ALLERGY, 2013, 43 (03) :365-377
[18]   In vitro growth and differentiated activities of human periodontal ligament fibroblasts cultured on salmon collagen gel [J].
Nagai, Nobuhiro ;
Mori, Kazuo ;
Satoh, Yasuharu ;
Takahashi, Noritaka ;
Yunoki, Shunji ;
Tajima, Kenji ;
Munekata, Masanobu .
JOURNAL OF BIOMEDICAL MATERIALS RESEARCH PART A, 2007, 82A (02) :395-402
[19]   Isolation of collagen from fish waste material - skin, bone and fins [J].
Nagai, T ;
Suzuki, N .
FOOD CHEMISTRY, 2000, 68 (03) :277-281
[20]  
NORRIS WD, 1990, J CELL SCI, V95, P255