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BioMed Research International
Volume 2014, Article ID 302932, 8 pages
http://dx.doi.org/10.1155/2014/302932
Review Article

Potency of Fish Collagen as a Scaffold for Regenerative Medicine

Department of Cardiology, Nagasaki University Graduate School of Biomedical Sciences, Nagasaki 852-8588, Japan

Received 28 January 2014; Accepted 14 May 2014; Published 25 May 2014

Academic Editor: Mitsuo Yamauchi

Copyright © 2014 Shizuka Yamada et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. A. Silvestri, M. Boffito, S. Sartori, and G. Ciardelli, “Biomimetic materials and scaffolds for myocardial tissue regeneration,” Macromolecular Bioscience, vol. 13, no. 8, pp. 984–1019, 2013. View at Publisher · View at Google Scholar · View at Scopus
  2. Y.-C. Lin, F.-J. Tan, K. G. Marra, S.-S. Jan, and D.-C. Liu, “Synthesis and characterization of collagen/hyaluronan/chitosan composite sponges for potential biomedical applications,” Acta Biomaterialia, vol. 5, no. 7, pp. 2591–2600, 2009. View at Publisher · View at Google Scholar · View at Scopus
  3. M. H. Tayebjee, R. J. MacFadyen, and G. Y. H. Lip, “Extracellular matrix biology: a new frontier in linking the pathology and therapy of hypertension?” Journal of Hypertension, vol. 21, no. 12, pp. 2211–2218, 2003. View at Publisher · View at Google Scholar · View at Scopus
  4. X. Wang, C. You, X. Hu et al., “The roles of knitted mesh-reinforced collagen-chitosan hybrid scaffold in the one-step repair of full-thickness skin defects in rats,” Acta Biomaterialia, vol. 9, no. 8, pp. 7822–7832, 2013. View at Publisher · View at Google Scholar · View at Scopus
  5. N. Kawaguchi, K. Hatta, and T. Nakanishi, “3D-culture system for heart regeneration and cardiac medicine,” BioMed Research International, vol. 2013, Article ID 895967, 6 pages, 2013. View at Publisher · View at Google Scholar
  6. R. Langer, “New methods of drug delivery,” Science, vol. 249, no. 4976, pp. 1527–1533, 1990. View at Google Scholar · View at Scopus
  7. R. Langer and J. P. Vacanti, “Tissue engineering,” Science, vol. 260, no. 5110, pp. 920–926, 1993. View at Google Scholar · View at Scopus
  8. R. S. Langer and J. P. Vacanti, “Tissue engineering: the challenges ahead,” Scientific American, vol. 280, no. 4, pp. 86–89, 1999. View at Google Scholar · View at Scopus
  9. L. G. Cima, J. P. Vacanti, C. Vacanti, D. Ingber, D. Mooney, and R. Langer, “Tissue engineering by cell transplantation using degradable polymer substrates,” Journal of Biomechanical Engineering, vol. 113, no. 2, pp. 143–151, 1991. View at Google Scholar · View at Scopus
  10. J. J. Marler, J. Upton, R. Langer, and J. P. Vacanti, “Transplantation of cells in matrices for tissue regeneration,” Advanced Drug Delivery Reviews, vol. 33, no. 1-2, pp. 165–182, 1998. View at Publisher · View at Google Scholar · View at Scopus
  11. S. V. Madihally and H. W. T. Matthew, “Porous chitosan scaffolds for tissue engineering,” Biomaterials, vol. 20, no. 12, pp. 1133–1142, 1999. View at Publisher · View at Google Scholar · View at Scopus
  12. S. J. Hollister, “Scaffold design and manufacturing: from concept to clinic,” Advanced Materials, vol. 21, no. 32-33, pp. 3330–3342, 2009. View at Publisher · View at Google Scholar · View at Scopus
  13. C. Domm, M. Schünke, K. Christesen, and B. Kurz, “Redifferentiation of dedifferentiated bovine articular chondrocytes in alginate culture under low oxygen tension,” Osteoarthritis and Cartilage, vol. 10, no. 1, pp. 13–22, 2002. View at Publisher · View at Google Scholar · View at Scopus
  14. J. Malda, T. B. F. Woodfield, F. Van Der Vloodt et al., “The effect of PEGT/PBT scaffold architecture on oxygen gradients in tissue engineered cartilaginous constructs,” Biomaterials, vol. 25, no. 26, pp. 5773–5780, 2004. View at Publisher · View at Google Scholar · View at Scopus
  15. P. M. Gallop and S. Seifter, “Preparation and properties of soluble collagens,” Methods in Enzymology, vol. 6, pp. 635–641, 1963. View at Publisher · View at Google Scholar · View at Scopus
  16. K. Yamaguchi, J. Lavety, and R. M. Love, “The connective tissues of fish. VIII. Comparative studies on hake, cod and catfish collagens,” Journal of Food Technolology, vol. 11, pp. 389–399, 1976. View at Google Scholar
  17. B. Kinner and M. Spector, “Smooth muscle actin expression by human articular chondrocytes and their contraction of a collagen-glycosaminoglycan matrix in vitro,” Journal of Orthopaedic Research, vol. 19, no. 2, pp. 233–241, 2001. View at Publisher · View at Google Scholar · View at Scopus
  18. S. Nehrer, H. A. Breinan, A. Ramappa et al., “Matrix collagen type and pore size influence behaviour of seeded canine chondrocytes,” Biomaterials, vol. 18, no. 11, pp. 769–776, 1997. View at Publisher · View at Google Scholar · View at Scopus
  19. S. Nehrer, H. A. Breinan, A. Ramappa et al., “Chondrocyte-seeded collagen matrices implanted in a chondral defect in a canine model,” Biomaterials, vol. 19, no. 24, pp. 2313–2328, 1998. View at Google Scholar · View at Scopus
  20. S. Srivastava, S. D. Gorham, and J. M. Courtney, “The attachment and growth of an established cell line on collagen, chemically modified collagen, and collagen composite surfaces,” Biomaterials, vol. 11, no. 3, pp. 162–168, 1990. View at Publisher · View at Google Scholar · View at Scopus
  21. M. D. Smith, M. G. Shearer, S. Srivastava, R. Scott, and J. M. Courtney, “Quantitative evaluation of the growth of established cell lines on the surface of collagen, collagen composite and reconstituted basement membrane,” Urological Research, vol. 20, no. 4, pp. 285–288, 1992. View at Publisher · View at Google Scholar · View at Scopus
  22. J. B. Smith, M. A. Selak, C. Dangelmaier, and J. L. Daniel, “Cytosolic calcium as a second messenger for collagen-induced platelet responses,” Biochemical Journal, vol. 288, no. 3, pp. 925–929, 1992. View at Google Scholar · View at Scopus
  23. S. Shortkroff, L. Barone, H.-P. Hsu et al., “Healing of chondral and osteochondral defects in a canine model: the role of cultured chondrocytes in regeneration of articular cartilage,” Biomaterials, vol. 17, no. 2, pp. 147–154, 1996. View at Publisher · View at Google Scholar · View at Scopus
  24. T. Fujisato, T. Sajiki, L. Qiang, and Y. Ikada, “Effect of basic fibroblast growth factor on cartilage regeneration in chondrocyte-seeded collagen sponge scaffold,” Biomaterials, vol. 17, no. 2, pp. 155–162, 1996. View at Publisher · View at Google Scholar · View at Scopus
  25. J. Y. Lee, R. Hall, D. Pelinkovic et al., “New use of a three-dimensional pellet culture system for human intervertebral disc cells: initial characterization and potential use for tissue engineering,” Spine, vol. 26, no. 21, pp. 2316–2322, 2001. View at Publisher · View at Google Scholar · View at Scopus
  26. M. Spector, “Novel cell-scaffold interactions encountered in tissue engineering: contractile behavior of musculoskeletal connective tissue cells,” Tissue Engineering, vol. 8, no. 3, pp. 351–357, 2002. View at Publisher · View at Google Scholar · View at Scopus
  27. T. Koide, Y. Takahara, S. Asada, and K. Nagata, “Xaa-Arg-Gly triplets in the collagen triple helix are dominant binding sites for the molecular chaperone HSP47,” Journal of Biological Chemistry, vol. 277, no. 8, pp. 6178–6182, 2002. View at Publisher · View at Google Scholar · View at Scopus
  28. D. Swatschek, W. Schatton, J. Kellermann, W. E. G. MullerMüller, and J. Kreuter, “Marine sponge collagen: isolation, characterization and effects on the skin parameters surface-pH, moisture and sebum,” European Journal of Pharmaceutics and Biopharmaceutics, vol. 53, no. 1, pp. 107–113, 2002. View at Publisher · View at Google Scholar · View at Scopus
  29. S. Kimura, “Vertebrate skin type I collagen: comparison of bony fishes with lamprey and calf,” Comparative Biochemistry and Physiology Part B, vol. 74, no. 3, pp. 525–528, 1983. View at Google Scholar · View at Scopus
  30. S. Kimura, X. P. Zhu, R. Matsui, M. Shinjoh, and S. Takamizawa, “Characterization of fish muscle type I collagen,” Journal of Food Science, vol. 53, no. 5, pp. 1315–1318, 1988. View at Google Scholar
  31. T. Nagai, E. Yamashita, K. Taniguchi, N. Kanamori, and N. Suzuki, “Isolation and characterisation of collagen from the outer skin waste material of cuttlefish (Sepia lycidas),” Food Chemistry, vol. 72, no. 4, pp. 425–429, 2001. View at Publisher · View at Google Scholar · View at Scopus
  32. N. Nagai, S. Yunoki, T. Suzuki, M. Sakata, K. Tajima, and M. Munekata, “Application of cross-linked salmon atelocollagen to the scaffold of human periodontal ligament cells,” Journal of Bioscience and Bioengineering, vol. 97, no. 6, pp. 389–394, 2004. View at Google Scholar · View at Scopus
  33. I. Bae, K. Osatomi, A. Yoshida, K. Osako, A. Yamaguchi, and K. Hara, “Biochemical properties of acid-soluble collagens extracted from the skins of underutilised fishes,” Food Chemistry, vol. 108, no. 1, pp. 49–54, 2008. View at Google Scholar
  34. M. D. Pierschbacher and E. Ruoslahti, “Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule,” Nature, vol. 309, no. 5963, pp. 30–33, 1984. View at Google Scholar · View at Scopus
  35. Y. Nomura, S. Toki, Y. Ishii, and K. Shirai, “The physicochemical property of shark type I collagen gel and membrane,” Journal of Agricultural and Food Chemistry, vol. 48, no. 6, pp. 2028–2032, 2000. View at Publisher · View at Google Scholar · View at Scopus
  36. Y. Nomura, S. Toki, Y. Ishii, and K. Shirai, “Improvement of the material property of shark type I collagen by composing with pig type I collagen,” Journal of Agricultural and Food Chemistry, vol. 48, no. 12, pp. 6332–6336, 2000. View at Publisher · View at Google Scholar · View at Scopus
  37. Y. Nomura, M. Yamano, and K. Shirai, “Renaturation of alpha 1 chains from shark skin collagen type I,” Journal of Food Science, vol. 60, pp. 1233–1236, 1995. View at Google Scholar
  38. R. Matsui, M. Ishida, and S. Kimura, “Characterization of an α3 chain from the skin type I collagen of chum salmon (Oncorhynchus keta),” Comparative Biochemistry and Physiology Part B, vol. 99, no. 1, pp. 171–174, 1991. View at Publisher · View at Google Scholar · View at Scopus
  39. T. Ikoma, H. Kobayashi, J. Tanaka, D. Walsh, and S. Mann, “Physical properties of type I collagen extracted from fish scales of Pagrus major and Oreochromis niloticas,” International Journal of Biological Macromolecules, vol. 32, no. 3-5, pp. 199–204, 2003. View at Publisher · View at Google Scholar · View at Scopus
  40. N. Nagai, K. Mori, Y. Satoh et al., “In vitro growth and differentiated activities of human periodontal ligament fibroblasts cultured on salmon collagen gel,” Journal of Biomedical Materials Research Part A, vol. 82, no. 2, pp. 395–402, 2007. View at Publisher · View at Google Scholar · View at Scopus
  41. K. S. Weadock, E. J. Miller, L. D. Bellincampi, J. P. Zawadsky, and M. G. Dunn, “Physical crosslinking of collagen fibers: comparison of ultraviolet irradiation and dehydrothermal treatment,” Journal of Biomedical Materials Research, vol. 29, no. 11, pp. 1373–1379, 1995. View at Publisher · View at Google Scholar · View at Scopus
  42. N. Nagai, T. Anzawa, Y. Satoh, T. Suzuki, K. Tajima, and M. Munekata, “Activities of MC3T3-E1 cells cultured on γ-irradiated salmon atelocollagen scaffold,” Journal of Bioscience and Bioengineering, vol. 101, no. 6, pp. 511–514, 2006. View at Publisher · View at Google Scholar · View at Scopus
  43. M. Koide, K. Osaki, J. Konishi et al., “A new type of biomaterial for artificial skin: dehydrothermally cross-linked composites of fibrillar and denatured collagens,” Journal of Biomedical Materials Research, vol. 27, no. 1, pp. 79–87, 1993. View at Publisher · View at Google Scholar · View at Scopus
  44. M.-C. Wang, G. D. Pins, and F. H. Silver, “Collagen fibres with improved strength for the repair of soft tissue injuries,” Biomaterials, vol. 15, no. 7, pp. 507–512, 1994. View at Publisher · View at Google Scholar · View at Scopus
  45. J. S. Pieper, A. Oosterhof, P. J. Dijkstra, J. H. Veerkamp, and T. H. Van Kuppevelt, “Preparation and characterization of porous crosslinked collagenous matrices containing bioavailable chondroitin sulphate,” Biomaterials, vol. 20, no. 9, pp. 847–858, 1999. View at Publisher · View at Google Scholar · View at Scopus
  46. M. J. White, I. Kohno, A. L. Rubin, K. H. Stenzel, and T. Miyata, “Collagen films: effect of cross linking on physical and biological properties,” Biomaterials Medical Devices and Artificial Organs, vol. 1, no. 4, pp. 703–715, 1973. View at Google Scholar · View at Scopus
  47. S. Yunoki, N. Nagai, T. Suzuki, and M. Munekata, “Novel biomaterial from reinforced salmon collagen gel prepared by fibril formation and cross-linking,” Journal of Bioscience and Bioengineering, vol. 98, no. 1, pp. 40–47, 2004. View at Google Scholar · View at Scopus
  48. L. L. H. Huang-Lee, D. T. Cheung, and M. E. Nimni, “Biochemical changes and cytotoxicity associated with the degradation of polymeric glutaraldehyde derived crosslinks,” Journal of Biomedical Materials Research, vol. 24, no. 9, pp. 1185–1201, 1990. View at Publisher · View at Google Scholar · View at Scopus
  49. S. Yunoki, T. Suzuki, and M. Takai, “Stabilization of low denaturation temperature collagen from fish by physical cross-linking methods,” Journal of Bioscience and Bioengineering, vol. 96, no. 6, pp. 575–577, 2003. View at Publisher · View at Google Scholar · View at Scopus
  50. F. Pati, P. Datta, B. Adhikari, S. Dhara, K. Ghosh, and P. K. D. Mohapatra, “Collagen scaffolds derived from fresh water fish origin and their biocompatibility,” Journal of Biomedical Materials Research Part A, vol. 100, no. 4, pp. 1068–1079, 2012. View at Publisher · View at Google Scholar · View at Scopus
  51. C. H. Lee, A. Singla, and Y. Lee, “Biomedical applications of collagen,” International Journal of Pharmaceutics, vol. 221, no. 1-2, pp. 1–22, 2001. View at Publisher · View at Google Scholar · View at Scopus
  52. N. Nagai, Y. Nakayama, Y.-M. Zhou, K. Takamizawa, K. Mori, and M. Munekata, “Development of salmon collagen vascular graft: mechanical and biological properties and preliminary implantation study,” Journal of Biomedical Materials Research Part B, vol. 87, no. 2, pp. 432–439, 2008. View at Publisher · View at Google Scholar · View at Scopus
  53. H. Sugiura, S. Yunoki, E. Kondo, T. Ikoma, J. Tanaka, and K. Yasuda, “In vivo biological responses and bioresorption of tilapia scale collagen as a potential biomaterial,” Journal of Biomaterials Science, Polymer Edition, vol. 20, no. 10, pp. 1353–1368, 2009. View at Publisher · View at Google Scholar · View at Scopus
  54. T. Miyata, T. Taira, and Y. Noishiki, “Collagen engineering for biomaterial use,” Clinical Materials, vol. 9, no. 3-4, pp. 139–148, 1992. View at Google Scholar · View at Scopus
  55. K. Hanai, F. Takeshita, K. Honma et al., “Atelocollagen-mediated systemic DDS for nucleic acid medicines,” Annals of the New York Academy of Sciences, vol. 1082, pp. 9–17, 2006. View at Publisher · View at Google Scholar · View at Scopus
  56. A. Sano, M. Maeda, S. Nagahara et al., “Atelocollagen for protein and gene delivery,” Advanced Drug Delivery Reviews, vol. 55, no. 12, pp. 1651–1677, 2003. View at Publisher · View at Google Scholar · View at Scopus
  57. E. Song, S. Yeon Kim, T. Chun, H.-J. Byun, and Y. M. Lee, “Collagen scaffolds derived from a marine source and their biocompatibility,” Biomaterials, vol. 27, no. 15, pp. 2951–2961, 2006. View at Publisher · View at Google Scholar · View at Scopus
  58. J.-H. Wang, C.-H. Hung, and T.-H. Young, “Proliferation and differentiation of neural stem cells on lysine-alanine sequential polymer substrates,” Biomaterials, vol. 27, no. 18, pp. 3441–3450, 2006. View at Publisher · View at Google Scholar · View at Scopus
  59. G. Chen, T. Ushida, and T. Tateishi, “Scaffold design for tissue engineering,” Macromolecular Bioscience, vol. 2, pp. 67–77, 2002. View at Google Scholar
  60. S. Yang, K.-F. Leong, Z. Du, and C.-K. Chua, “The design of scaffolds for use in tissue engineering. Part I. Traditional factors,” Tissue Engineering, vol. 7, no. 6, pp. 679–689, 2001. View at Publisher · View at Google Scholar · View at Scopus
  61. B. L. Seal, T. C. Otero, and A. Panitch, “Polymeric biomaterials for tissue and organ regeneration,” Materials Science and Engineering: R: Reports, vol. 34, no. 4-5, 2001. View at Google Scholar · View at Scopus
  62. A. K. Dillow and A. M. Lowman, Biomimetic Materials and Design: Biointerfacial Strategies, Tissue Engineering, and Targeted Drug Delivery, Marcel Dekker, New York, NY, USA, 2002.
  63. J. F. Bateman, S. R. Lamande, and J. A. M. Ramshaw, “Collagen superfamily,” in Extracellular Matrix, W. D. Comper, Ed., pp. 22–67, Harwood Academic Publishers, Amsterdam, The Netherlands.
  64. J. C. Brown and R. Timpl, “The collagen superfamily,” International Archives of Allergy and Immunology, vol. 107, no. 4, pp. 484–490, 1995. View at Google Scholar · View at Scopus
  65. B. Chevallay and D. Herbage, “Collagen-based biomaterials as 3D scaffold for cell cultures: applications for tissue engineering and gene therapy,” Medical and Biological Engineering and Computing, vol. 38, no. 2, pp. 211–218, 2000. View at Google Scholar · View at Scopus
  66. D. R. Eyre, “Collagen: molecular diversity in the body's protein scaffold,” Science, vol. 207, no. 4437, pp. 1315–1322, 1980. View at Google Scholar · View at Scopus
  67. K. Kadler, “Extracellular matrix 1: fibril-forming collagens,” Protein Profile, vol. 2, no. 5, pp. 491–619, 1995. View at Google Scholar · View at Scopus
  68. P. D. Kemp, “Tissue engineering and cell-populated collagen matrices,” Methods in Molecular Biology, vol. 139, pp. 287–293, 2000. View at Google Scholar · View at Scopus
  69. M. G. Patino, M. E. Neiders, S. Andreana, B. Noble, and R. E. Cohen, “Collagen as an implantable material in medicine and dentistry,” The Journal of oral Implantology, vol. 28, no. 5, pp. 220–225, 2002. View at Google Scholar · View at Scopus
  70. D. J. Prockop and K. I. Kivirikko, “Collagens: molecular biology, diseases, and potentials for therapy,” Annual Review of Biochemistry, vol. 64, pp. 403–434, 1995. View at Google Scholar · View at Scopus
  71. S. Ricard-Blum, B. Dublet, and M. van der Rest, Unconventional Collagens, Oxford University Press, New York, NY, USA, 2000.
  72. C. Wong Po Foo and D. L. Kaplan, “Genetic engineering of fibrous proteins: spider dragline silk and collagen,” Advanced Drug Delivery Reviews, vol. 54, no. 8, pp. 1131–1143, 2002. View at Publisher · View at Google Scholar · View at Scopus
  73. C. Yang, S.-W. Li, H. J. Helminen, J. S. Khillan, B. Yunhua, and D. J. Prockop, “Apoptosis of chondrocytes in transgenic mice lacking collagen II,” Experimental Cell Research, vol. 235, no. 2, pp. 370–373, 1997. View at Publisher · View at Google Scholar · View at Scopus
  74. T. Sugahara, M. Ueno, Y. Goto et al., “Immunostimulation effect of jellyfish collagen,” Bioscience, Biotechnology and Biochemistry, vol. 70, no. 9, pp. 2131–2137, 2006. View at Publisher · View at Google Scholar · View at Scopus
  75. S. Nishimoto, Y. Goto, H. Morishige et al., “Mode of action of the immunostimulatory effect of collagen from jellyfish,” Bioscience, Biotechnology and Biochemistry, vol. 72, no. 11, pp. 2806–2814, 2008. View at Publisher · View at Google Scholar · View at Scopus
  76. K. Iohara, L. Zheng, M. Ito, A. Tomokiyo, K. Matsushita, and M. Nakashima, “Side population cells isolated from porcine dental pulp tissue with self-renewal and multipotency for dentinogenesis, chondrogenesis, adipogenesis, and neurogenesis,” Stem Cells, vol. 24, no. 11, pp. 2493–2503, 2006. View at Publisher · View at Google Scholar · View at Scopus
  77. M. Nakashima, K. Iohara, and L. Zheng, “Gene therapy for dentin regeneration with bone morphogenetic proteins,” Current Gene Therapy, vol. 6, no. 5, pp. 551–560, 2006. View at Publisher · View at Google Scholar · View at Scopus
  78. K. Iohara, L. Zheng, H. Wake et al., “A novel stem cell source for vasculogenesis in ischemia: subfraction of side population cells from dental pulp,” Stem Cells, vol. 26, no. 9, pp. 2408–2418, 2008. View at Publisher · View at Google Scholar · View at Scopus
  79. K. Iohara, L. Zheng, M. Ito et al., “Regeneration of dental pulp after pulpotomy by transplantation of CD31/CD146 side population cells from a canine tooth,” Regenerative Medicine, vol. 4, no. 3, pp. 377–385, 2009. View at Publisher · View at Google Scholar · View at Scopus
  80. L. Zheng, K. Amano, K. Iohara et al., “Matrix metalloproteinase-3 accelerates wound healing following dental pulp injury,” American Journal of Pathology, vol. 175, no. 5, pp. 1905–1914, 2009. View at Publisher · View at Google Scholar · View at Scopus
  81. M. Nakashima, K. Iohara, and M. Sugiyama, “Human dental pulp stem cells with highly angiogenic and neurogenic potential for possible use in pulp regeneration,” Cytokine & Growth Factor Reviews, vol. 20, no. 5-6, pp. 435–440, 2009. View at Publisher · View at Google Scholar · View at Scopus
  82. M. Sugiyama, K. Iohara, H. Wakita et al., “Dental pulp-derived CD31/CD146 side population stem/progenitor cells enhance recovery of focal cerebral ischemia in rats,” Tissue Engineering Part A, vol. 17, no. 9-10, pp. 1303–1311, 2011. View at Publisher · View at Google Scholar · View at Scopus
  83. K. Iohara, K. Imabayashi, R. Ishizaka et al., “Complete pulp regeneration after pulpectomy by transplantation of CD105+ stem cells with stromal cell-derived factor-1,” Tissue Engineering Part A, vol. 17, no. 15-16, pp. 1911–1920, 2011. View at Publisher · View at Google Scholar · View at Scopus
  84. M. Nakashima and K. Iohara, “Regeneration of dental pulp by stem cells,” Advances in Dental Research, vol. 23, no. 3, pp. 313–319, 2011. View at Publisher · View at Google Scholar · View at Scopus
  85. R. Ishizaka, K. Iohara, M. Murakami, O. Fukuta, and M. Nakashima, “Regeneration of dental pulp following pulpectomy by fractionated stem/progenitor cells from bone marrow and adipose tissue,” Biomaterials, vol. 33, no. 7, pp. 2109–2118, 2012. View at Publisher · View at Google Scholar · View at Scopus
  86. M. Murakami, K. Imabayashi, A. Watanabe et al., “Identification of novel function of vimentin for quality standard for regenerated pulp tissue,” Journal of Endodontics, vol. 38, no. 7, pp. 920–926, 2012. View at Publisher · View at Google Scholar · View at Scopus
  87. T. Ikeda, K. Yanagiguchi, I. L. Viloria, and Y. Hayashi, “Relationship between lysozyme activity and clinical symptoms following the application of chitin/chitosan in endodntic treatment,” in ChitOsan Per os: From Dietary Supplrmrnt to Drug Carrier, R. A. A. Muzzarelli, Ed., pp. 275–292, Atec Edizioni, Italy, 2000. View at Google Scholar
  88. T. Ikeda, K. Yanagiguchi, and Y. Hayashi, “Application to dental medicine—in focus on dental caries and alveolar bone healing,” Bioindustry, vol. 19, pp. 22–30, 2002 (Japanese). View at Google Scholar
  89. S. Yamada, N. Ohara, and Y. Hayashi, “Mineralization of matrix vesicles isolated from a human osteosarcoma cell line in culture with water-soluble chitosan-containing medium,” Journal of Biomedical Materials Research Part A, vol. 66, no. 3, pp. 500–506, 2003. View at Google Scholar · View at Scopus
  90. M. Fujiwara, Y. Hayashi, and N. Ohara, “Inhibitory effect of water-soluble chitosan on growth of Streptococcus mutans,” New Microbiologica, vol. 27, no. 1, pp. 83–86, 2004. View at Google Scholar · View at Scopus
  91. N. Ohara, Y. Hayashi, S. Yamada et al., “Early gene expression analyzed by cDNA microarray and RT-PCR in osteoblasts cultured with water-soluble and low molecular chitooligosaccharide,” Biomaterials, vol. 25, no. 10, pp. 1749–1754, 2004. View at Publisher · View at Google Scholar · View at Scopus
  92. T. Ikeda, K. Yanagiguchi, T. Matsunaga et al., “Immunohistochemical and electron microscopic study of the biodegradation processes of chitin and chitosan implanted in rat alveolar bone,” Oral Medicine & Pathology, vol. 10, pp. 131–138, 2005. View at Google Scholar
  93. T. Matsunaga, K. Yanagiguchi, S. Yamada, N. Ohara, T. Ikeda, and Y. Hayashi, “Chitosan monomer promotes tissue regeneration on dental pulp wounds,” Journal of Biomedical Materials Research Part A, vol. 76, no. 4, pp. 711–720, 2006. View at Publisher · View at Google Scholar · View at Scopus
  94. T. Ganno, S. Yamada, N. Ohara et al., “Early gene expression analyzed by cDNA microarray and real-time PCR in osteoblasts cultured with chitosan monomer,” Journal of Biomedical Materials Research Part A, vol. 82, no. 1, pp. 188–194, 2007. View at Publisher · View at Google Scholar · View at Scopus
  95. S. Yamada, T. Ganno, N. Ohara, and Y. Hayashi, “Chitosan monomer accelerates alkaline phosphatase activity on human osteoblastic cells under hypofunctional conditions,” Journal of Biomedical Materials Research Part A, vol. 83, no. 2, pp. 290–295, 2007. View at Publisher · View at Google Scholar · View at Scopus
  96. Y. Hayashi, N. Ohara, T. Ganno et al., “Chewing chitosan-containing gum effectively inhibits the growth of cariogenic bacteria,” Archives of Oral Biology, vol. 52, no. 3, pp. 290–294, 2007. View at Publisher · View at Google Scholar · View at Scopus
  97. Y. Hayashi, N. Ohara, T. Ganno, H. Ishizaki, and K. Yanagiguchi, “Chitosan-containing gum chewing accelerates antibacterial effect with an increase in salivary secretion,” Journal of Dentistry, vol. 35, no. 11, pp. 871–874, 2007. View at Publisher · View at Google Scholar · View at Scopus
  98. H. Ishizaki, S. Yamada, K. Yanagiguchi, Z. Koyama, T. Ikeda, and Y. Hayashi, “Pre-treatment with tannic acid inhibits the intracellular IL-8 production by chitosan in a human oral epithelial cancer cell line,” Oral Medicine & Pathology, vol. 13, pp. 135–141, 2009. View at Google Scholar
  99. Y. Hayashi, “Applications of chitosan oligosaccharide and glucosamine in dentistry,” in Chitin, Chitosan, Oligosaccharides and Their Derivatives, S.-K. Kim, Ed., pp. 447–460, CRC Press, Boca Raton, Fla, USA, 2010. View at Google Scholar
  100. Y. Hayashi, S. Yamada, T. Ikeda, Z. Koyama, and K. Yanagiguchi, “Chitosan and fish collagen as biomaterials for regenerative medicine,” in Marine Medical Food, S.-K. Kim, Ed., vol. 65, chapter 6, pp. 107–120, Academic Press, London, UK, 2012. View at Google Scholar
  101. K. Yanagiguchi, T. Ikeda, F. Takai, K. Ogawa, and Y. Hayashi, “Wound healing following direct pulp capping with chitosan-ascorbic acid complex in rat incisors,” in Chitin and Chitosan, T. Uragami, K. Kurita, and T. Fukamizo, Eds., pp. 240–243, Kodansha Scientific, Tokyo, Japan, 2001. View at Google Scholar
  102. W. Zhang, H. Abukawa, M. J. Troulis, L. B. Kaban, J. P. Vacanti, and P. C. Yelick, “Tissue engineered hybrid tooth-bone constructs,” Methods, vol. 47, no. 2, pp. 122–128, 2009. View at Publisher · View at Google Scholar · View at Scopus
  103. F.-M. Chen, R. M. Shelton, Y. Jin, and I. L. C. Chapple, “Localized delivery of growth factors for periodontal tissue regeneration: role, strategies, and perspectives,” Medicinal Research Reviews, vol. 29, no. 3, pp. 472–513, 2009. View at Publisher · View at Google Scholar · View at Scopus
  104. T. Kawase, K. Okuda, H. Kogami, H. Nakayama, M. Nagata, and H. Yoshie, “Osteogenic activity of human periosteal sheets cultured on salmon collagen-coated ePTFE meshes,” Journal of Materials Science: Materials in Medicine, vol. 21, no. 2, pp. 731–739, 2010. View at Publisher · View at Google Scholar · View at Scopus
  105. S. Yamada, Y. Yoshizawa, A. Kawakubo, T. Ikeda, K. Yanagiguchi, and Y. Hayashi, “Early gene and protein expression associated with osteoblast differentiation in response to fish collagen peptides powder,” Dental Materials Journal, vol. 32, no. 2, pp. 233–240, 2013. View at Publisher · View at Google Scholar · View at Scopus
  106. S. Yamada, H. Nagaoka, M. Terajima, N. Tsuda, Y. Hayashi, and M. Yamauchi, “Effects of fish collagen peptides on collagen post-translational modifications and mineralization in an osteoblastic cell culture system,” Dental Materials Journal, vol. 32, no. 1, pp. 88–95, 2013. View at Publisher · View at Google Scholar · View at Scopus