nach oben

Erschienen in:

2011 | OriginalPaper | Buchkapitel

8. Natural Materials in Tissue Engineering Applications

verfasst von : Elyssa L. Monzack, Karien J. Rodriguez, Chloe M. McCoy, Xiaoxiao Gu, Kristyn S. Masters

Erschienen in: Biomaterials for Tissue Engineering Applications

Verlag: Springer Vienna

Einloggen

Aktivieren Sie unsere intelligente Suche, um passende Fachinhalte oder Patente zu finden.

search-config

KI-gestützte Suche

Aus

Abstract

Materials derived from natural sources are used extensively in tissue engineering. Consisting of proteins, polysaccharides, or ceramics, these materials may be harvested from a wide range of sources and possess an equally wide range of physical and biological properties. This chapter focuses upon seven of these materials, namely collagen, fibrin, elastin, hyaluronic acid, alginate, chitosan, and silk. These materials are first discussed with respect to their intrinsic features that are relevant to tissue engineering, such as structure, source, degradation, mechanics, immunogenicity, and recognition by cells. This is followed by a review of techniques for derivatizing natural materials, forming scaffolds, and tailoring these scaffolds, accompanied by select examples of how these natural materials have been used in tissue engineering applications. While natural materials possess many characteristics that render them attractive for use in tissue engineering, they are also accompanied by some unique challenges; both of these features are highlighted in this chapter.

Sie haben noch keine Lizenz? Dann Informieren Sie sich jetzt über unsere Produkte:

Springer Professional "Wirtschaft+Technik"

Online-Abonnement

Mit Springer Professional "Wirtschaft+Technik" erhalten Sie Zugriff auf:

über 102.000 Bücher
über 537 Zeitschriften

aus folgenden Fachgebieten:

Automobil + Motoren
Bauwesen + Immobilien
Business IT + Informatik
Elektrotechnik + Elektronik
Energie + Nachhaltigkeit
Finance + Banking
Management + Führung
Marketing + Vertrieb
Maschinenbau + Werkstoffe
Versicherung + Risiko

Jetzt Wissensvorsprung sichern!

Jetzt informieren

Springer Professional "Technik"

Online-Abonnement

Mit Springer Professional "Technik" erhalten Sie Zugriff auf:

über 67.000 Bücher
über 390 Zeitschriften

aus folgenden Fachgebieten:

Automobil + Motoren
Bauwesen + Immobilien
Business IT + Informatik
Elektrotechnik + Elektronik
Energie + Nachhaltigkeit
Maschinenbau + Werkstoffe

Jetzt Wissensvorsprung sichern!

Jetzt informieren

Vorheriges Kapitel Bioceramics in Tissue Engineering

Nächstes Kapitel Engineered Polypeptides for Tissue Engineering

C.A. Vacanti, History of tissue engineering and a glimpse into its future, Tissue Eng 12 (2006), pp. 1137–1142.

I.V. Yannas, J.F. Burke, P.L. Gordon, C. Huang, and R.H. Rubenstein, Design of an artificial skin. II. Control of chemical composition, J Biomed Mater Res 14 (1980), pp. 107–132.

E. Bell, B. Ivarsson, and C. Merrill, Production of a tissue-like structure by contraction of collagen lattices by human fibroblasts of different proliferative potential in vitro, Proc Natl Acad Sci U S A 76 (1979), pp. 1274–1278.

C.B. Weinberg, and E. Bell, A blood vessel model constructed from collagen and cultured vascular cells, Science 231 (1986), pp. 397–400.

M. Radosevich, H.I. Goubran, and T. Burnouf, Fibrin sealant: scientific rationale, production methods, properties, and current clinical use, Vox Sang 72 (1997), pp. 133–143.

W. Halsted, The employment of fine silk in preference to catgut and the advantage of transfixing tissues and vessels in controlling hemorrhage, Ann Surg 16 (1892), pp. 505.

C. Demers, C.R. Hamdy, K. Corsi, F. Chellat, M. Tabrizian, and L. Yahia, Natural coral exoskeleton as a bone graft substitute: a review, Biomed Mater Eng 12 (2002), pp. 15–35.

K.P. Rao, Recent developments of collagen-based materials for medical applications and drug delivery systems, J Biomater Sci Polym Ed 7 (1995), pp. 623–645.

H.J. Chung, and T.G. Park, Surface engineered and drug releasing pre-fabricated scaffolds for tissue engineering, Adv Drug Deliv Rev 59 (2007), pp. 249–262.

10.

A.D. Metcalfe, and M.W. Ferguson, Tissue engineering of replacement skin: the crossroads of biomaterials, wound healing, embryonic development, stem cells and regeneration, J R Soc Interface 4 (2007), pp. 413–437.

11.

L.S. Nair, and C.T. Laurencin, Polymers as biomaterials for tissue engineering and controlled drug delivery, Adv Biochem Eng Biotechnol 102 (2006), pp. 47–90.

12.

R.A. Brown, and J.B. Phillips, Cell responses to biomimetic protein scaffolds used in tissue repair and engineering, Int Rev Cytol 262 (2007), pp. 75–150.

13.

M. Mian, F. Beghe, and E. Mian, Collagen as a pharmacological approach in wound healing, Int J Tissue React 14 Suppl (1992), pp. 1–9.

14.

K.H. Stenzel, T. Miyata, and A.L. Rubin, Collagen as a biomaterial, Annu Rev Biophys Bioeng 3 (1974), pp. 231–253.

15.

L. Cen, W. Liu, L. Cui, W. Zhang, and Y. Cao, Collagen tissue engineering: development of novel biomaterials and applications, Pediatr Res 63 (2008), pp. 492–496.

16.

I.V. Yannas. Natural Materials. In: B.D. Ratner, A.S. Hoffman, F.J. Shoen, J.E. Lemons, editors. Biomaterials Science. San Diego, CA: Elsevier Academic Press; (2004)

17.

K.S. Masters, and W.L. Murphy. Tissue Engineering. In: J.G. Webster, editor. Encyclopedia of Medical Devices and Instrumentation: John Wiley & Sons, Inc.; (2006), p. 379–395.

18.

J.A. Ramshaw, Y.Y. Peng, V. Glattauer, and J.A. Werkmeister, Collagens as biomaterials, J Mater Sci Mater Med 20 Suppl 1 (2009), pp. S3–S8.

19.

B. Brodsky, and J.A. Ramshaw, The collagen triple-helix structure, Matrix Biol 15 (1997), pp. 545–554.

20.

H. Birkedal-Hansen, W.G. Moore, M.K. Bodden, L.J. Windsor, B. Birkedal-Hansen, A. DeCarlo, et al., Matrix metalloproteinases: a review, Crit Rev Oral Biol Med 4 (1993), pp. 197–250.

21.

S. Young, M. Wong, Y. Tabata, and A.G. Mikos, Gelatin as a delivery vehicle for the controlled release of bioactive molecules, J Control Release 109 (2005), pp. 256–274.

22.

D.J. White, S. Puranen, M.S. Johnson, and J. Heino, The collagen receptor subfamily of the integrins, Int J Biochem Cell Biol 36 (2004), pp. 1405–1410.

23.

A.V. Taubenberger, M.A. Woodruff, H. Bai, D.J. Muller, and D.W. Hutmacher, The effect of unlocking RGD-motifs in collagen I on pre-osteoblast adhesion and differentiation, Biomaterials 31 (2010), pp. 2827–2835.

24.

D. Gullberg, K.R. Gehlsen, D.C. Turner, K. Ahlen, L.S. Zijenah, M.J. Barnes, et al., Analysis of alpha 1 beta 1, alpha 2 beta 1 and alpha 3 beta 1 integrins in cell–collagen interactions: identification of conformation dependent alpha 1 beta 1 binding sites in collagen type I, Embo J 11 (1992), pp. 3865–3873.

25.

J.R. Mauney, V. Volloch, and D.L. Kaplan, Matrix-mediated retention of adipogenic differentiation potential by human adult bone marrow-derived mesenchymal stem cells during ex vivo expansion, Biomaterials 26 (2005), pp. 6167–6175.

26.

A.K. Lynn, I.V. Yannas, and W. Bonfield, Antigenicity and immunogenicity of collagen, J Biomed Mater Res B Appl Biomater 71 (2004), pp. 343–354.

27.

M.W. Mosesson, Fibrinogen and fibrin structure and functions, J Thromb Haemost 3 (2005), pp. 1894–1904.

28.

K. Suzuki, B. Dahlback, and J. Stenflo, Thrombin-catalyzed activation of human coagulation factor V, J Biol Chem 257 (1982), pp. 6556–6564.

29.

P.A. Janmey, J.P. Winer, and J.W. Weisel, Fibrin gels and their clinical and bioengineering applications, J R Soc Interface 6 (2009), pp. 1–10.

30.

C. Buchta, H.C. Hedrich, M. Macher, P. Hocker, and H. Redl, Biochemical characterization of autologous fibrin sealants produced by CryoSeal and Vivostat in comparison to the homologous fibrin sealant product Tissucol/Tisseel, Biomaterials 26 (2005), pp. 6233–6241.

31.

J.J. Calvete, Structures of integrin domains and concerted conformational changes in the bidirectional signaling mechanism of alphaIIbbeta3, Exp Biol Med (Maywood) 229 (2004), pp. 732–744.

32.

R. Gorodetsky, The use of fibrin based matrices and fibrin microbeads (FMB) for cell based tissue regeneration, Expert Opin Biol Ther 8 (2008), pp. 1831–1846.

33.

K. Suehiro, J. Mizuguchi, K. Nishiyama, S. Iwanaga, D.H. Farrell, and S. Ohtaki, Fibrinogen binds to integrin alpha(5)beta(1) via the carboxyl-terminal RGD site of the Aalpha-chain, J Biochem 128 (2000), pp. 705–710.

34.

R.E. Nisato, J.C. Tille, A. Jonczyk, S.L. Goodman, and M.S. Pepper, alphav beta 3 and alphav beta 5 integrin antagonists inhibit angiogenesis in vitro, Angiogenesis 6 (2003), pp. 105–119.

35.

A. Sahni, T. Odrljin, and C.W. Francis, Binding of basic fibroblast growth factor to fibrinogen and fibrin, J Biol Chem 273 (1998), pp. 7554–7559.

36.

A. Sahni, and C.W. Francis, Stimulation of endothelial cell proliferation by FGF-2 in the presence of fibrinogen requires alphavbeta3, Blood 104 (2004), pp. 3635–3641.

37.

A. Sahni, and C.W. Francis, Vascular endothelial growth factor binds to fibrinogen and fibrin and stimulates endothelial cell proliferation, Blood 96 (2000), pp. 3772–3778.

38.

B. Vrhovski, and A.S. Weiss, Biochemistry of tropoelastin, Eur J Biochem 258 (1998), pp. 1–18.

39.

J. Rosenbloom, W.R. Abrams, and R. Mecham, Extracellular matrix 4: the elastic fiber, Faseb J 7 (1993), pp. 1208–1218.

40.

J.E. Wagenseil, and R.P. Mecham, New insights into elastic fiber assembly, Birth Defects Res C Embryo Today 81 (2007), pp. 229–240.

41.

S.M. Mithieux, and A.S. Weiss, Elastin, Adv Protein Chem 70 (2005), pp. 437–461.

42.

E. Petersen, F. Wagberg, and K.A. Angquist, Serum concentrations of elastin-derived peptides in patients with specific manifestations of atherosclerotic disease, Eur J Vasc Endovasc Surg 24 (2002), pp. 440–444.

43.

F.W. Keeley, C.M. Bellingham, and K.A. Woodhouse, Elastin as a self-organizing biomaterial: use of recombinantly expressed human elastin polypeptides as a model for investigations of structure and self-assembly of elastin, Philos Trans R Soc Lond B Biol Sci 357 (2002), pp. 185–189.

44.

W.F. Daamen, J.H. Veerkamp, J.C. van Hest, and T.H. van Kuppevelt, Elastin as a biomaterial for tissue engineering, Biomaterials 28 (2007), pp. 4378–4398.

45.

A. Hinek, D.S. Wrenn, R.P. Mecham, and S.H. Barondes, The elastin receptor: a galactoside-binding protein, Science 239 (1988), pp. 1539–1541.

46.

U.R. Rodgers, and A.S. Weiss, Integrin alpha v beta 3 binds a unique non-RGD site near the C-terminus of human tropoelastin, Biochimie 86 (2004), pp. 173–178.

47.

S.M. Partridge, H.F. Davis, and G.S. Adair, The chemistry of connective tissues. 2. Soluble proteins derived from partial hydrolysis of elastin, Biochem J 61 (1955), pp. 11–21.

48.

S.M. Mithieux, J.E. Rasko, and A.S. Weiss, Synthetic elastin hydrogels derived from massive elastic assemblies of self-organized human protein monomers, Biomaterials 25 (2004), pp. 4921–4927.

49.

L. Nivison-Smith, J. Rnjak, and A.S. Weiss, Synthetic human elastin microfibers: Stable cross-linked tropoelastin and cell interactive constructs for tissue engineering applications, Acta Biomater 6 (2010), pp. 354–359.

50.

J. Rnjak, Z. Li, P.K. Maitz, S.G. Wise, and A.S. Weiss, Primary human dermal fibroblast interactions with open weave three-dimensional scaffolds prepared from synthetic human elastin, Biomaterials 30 (2009), pp. 6469–6477.

51.

M. Gomes, H. Azevedo, P. Malafaya, S. Silva, J. Oliveira, G. Silva, et al. Natural polymers in tissue engineering applications. In: C. van Blitterswijk, editor. Tissue Engineering. London, UK: Elsevier Inc.; (2008)

52.

P. Prehm, Hyaluronate is synthesized at plasma membranes, Biochem J 220 (1984), pp. 597–600.

53.

P.H. Weigel, V.C. Hascall, and M. Tammi, Hyaluronan synthases, J Biol Chem 272 (1997), pp. 13997–14000.

54.

T.C. Laurent, U.B. Laurent, and J.R. Fraser, The structure and function of hyaluronan: an overview, Immunol Cell Biol 74 (1996), pp. A1–A7.

55.

J. Baier Leach, and C.E. Schmidt. Hyaluronan. In: G.E. Wnek, G.L. Bowlin, editors. Encyclopedia of Biomaterials and Biomedical Engineering. New York, NY: Marcel Dekker, Inc.; (2004), p. 779–789.

56.

C.B. Knudson, and W. Knudson, Hyaluronan-binding proteins in development, tissue homeostasis, and disease, FASEB J 7 (1993), pp. 1233–1241.

57.

E.A. Turley, P.W. Noble, and L.Y. Bourguignon, Signaling properties of hyaluronan receptors, J Biol Chem 277 (2002), pp. 4589–4592.

58.

D.C. West, and S. Kumar, The effect of hyaluronate and its oligosaccharides on endothelial cell proliferation and monolayer integrity, Exp Cell Res 183 (1989), pp. 179–196.

59.

K.S. Masters, D.N. Shah, L.A. Leinwand, and K.S. Anseth, Crosslinked hyaluronan scaffolds as a biologically active carrier for valvular interstitial cells, Biomaterials 26 (2005), pp. 2517–2525.

60.

T.C. Laurent, and J.R. Fraser, Hyaluronan, FASEB J 6 (1992), pp. 2397–2404.

61.

J.R. Fraser, T.C. Laurent, and U.B. Laurent, Hyaluronan: its nature, distribution, functions and turnover, J Intern Med 242 (1997), pp. 27–33.

62.

D.C. West, and S. Kumar, Hyaluronan and angiogenesis, Ciba Found Symp 143 (1989), pp. 187–201; discussion 201–207, 281–285.

63.

D.D. Allison, and K.J. Grande-Allen, Review. Hyaluronan: a powerful tissue engineering tool, Tissue Eng 12 (2006), pp. 2131–2140.

64.

W.Y. Chen, and G. Abatangelo, Functions of hyaluronan in wound repair, Wound Repair Regen 7 (1999), pp. 79–89.

65.

J.A. Kluge, O. Rabotyagova, G.G. Leisk, and D.L. Kaplan, Spider silks and their applications, Trends Biotechnol 26 (2008), pp. 244–251.

66.

T.D. Sutherland, S. Weisman, H.E. Trueman, A. Sriskantha, J.W. Trueman, and V.S. Haritos, Conservation of essential design features in coiled coil silks, Mol Biol Evol 24 (2007), pp. 2424–2432.

67.

E. Carrington, Along the silk road, spiders make way for mussels, Trends Biotechnol 26 (2008), pp. 55–57.

68.

L. Romer, and T. Scheibel, The elaborate structure of spider silk: structure and function of a natural high performance fiber, Prion 2 (2008), pp. 154–161.

69.

G.H. Altman, F. Diaz, C. Jakuba, T. Calabro, R.L. Horan, J. Chen, et al., Silk-based biomaterials, Biomaterials 24 (2003), pp. 401–416.

70.

Y. Cao, and B. Wang, Biodegradation of silk biomaterials, Int J Mol Sci 10 (2009), pp. 1514–1524.

71.

Y. Wang, H.J. Kim, G. Vunjak-Novakovic, and D.L. Kaplan, Stem cell-based tissue engineering with silk biomaterials, Biomaterials 27 (2006), pp. 6064–6082.

72.

R.V. Lewis, Spider silk: ancient ideas for new biomaterials, Chem Rev 106 (2006), pp. 3762–3774.

73.

K.I. Draget, and C. Taylor, Chemical, physical and biological properties of alginates and their biomedical implications, Food Hydrocoll 25 (2011), pp. 251–256.

74.

O. Smidsrød, and K.I. Draget, Chemistry and physical properties of alginates, Carbohydr Eur 14 (1996), pp. 6–13.

75.

P.H. Calumpong, P.A. Maypa, and M. Magbanua, Population and alginate yield and quality of four Sargassum species in Negros Island, central Philippines, Hydrobiologia 398 (1999), pp. 211–215.

76.

A.D. Augst, H.J. Kong, and D.J. Mooney, Alginate hydrogels as biomaterials, Macromol Biosci 6 (2006), pp. 623–633.

77.

O. Smidsrod, and G. Skjak-Braek, Alginate as immobilization matrix for cells, Trends Biotechnol 8 (1990), pp. 71–78.

78.

A. Martinsen, G. Skjak-Braek, and O. Smidsrod, Alginate as immobilization material: I. Correlation between chemical and physical properties of alginate gel beads, Biotechnol Bioeng 33 (1989), pp. 79–89.

79.

T.Y. Wong, L.A. Preston, and N.L. Schiller, ALGINATE LYASE: review of major sources and enzyme characteristics, structure-function analysis, biological roles, and applications, Annu Rev Microbiol 54 (2000), pp. 289–340.

80.

K.H. Bouhadir, K.Y. Lee, E. Alsberg, K.L. Damm, K.W. Anderson, and D.J. Mooney, Degradation of partially oxidized alginate and its potential application for tissue engineering, Biotechnol Prog 17 (2001), pp. 945–950.

81.

I.Y. Kim, S.J. Seo, H.S. Moon, M.K. Yoo, I.Y. Park, B.C. Kim, et al., Chitosan and its derivatives for tissue engineering applications, Biotechnol Adv 26 (2008), pp. 1–21.

82.

D.W. Hutmacher, J.C. Goh, and S.H. Teoh, An introduction to biodegradable materials for tissue engineering applications, Ann Acad Med Singapore 30 (2001), pp. 183–191.

83.

T. Jiang, S.G. Kumbar, L.S. Nair, and C.T. Laurencin, Biologically active chitosan systems for tissue engineering and regenerative medicine, Curr Top Med Chem 8 (2008), pp. 354–364.

84.

Y.C. Ho, F.L. Mi, H.W. Sung, and P.L. Kuo, Heparin-functionalized chitosan-alginate scaffolds for controlled release of growth factor, Int J Pharm 376 (2009), pp. 69–75.

85.

G.G. d’Ayala, M. Malinconico, and P. Laurienzo, Marine derived polysaccharides for biomedical applications: chemical modification approaches, Molecules 13 (2008), pp. 2069–2106.

86.

M. Ganan, A.V. Carrascosa, and A.J. Martinez-Rodriguez, Antimicrobial activity of chitosan against Campylobacter spp. and other microorganisms and its mechanism of action, J Food Prot 72 (2009), pp. 1735–1738.

87.

A.K. Singla, and M. Chawla, Chitosan: some pharmaceutical and biological aspects – an update, J Pharm Pharmacol 53 (2001), pp. 1047–1067.

88.

D. Olsen, C. Yang, M. Bodo, R. Chang, S. Leigh, J. Baez, et al., Recombinant collagen and gelatin for drug delivery, Adv Drug Deliv Rev 55 (2003), pp. 1547–1567.

89.

C. Yang, P.J. Hillas, J.A. Baez, M. Nokelainen, J. Balan, J. Tang, et al., The application of recombinant human collagen in tissue engineering, BioDrugs 18 (2004), pp. 103–119.

90.

A. Khademhosseini, and R. Langer, Microengineered hydrogels for tissue engineering, Biomaterials 28 (2007), pp. 5087–5092.

91.

H. Schoof, J. Apel, I. Heschel, and G. Rau, Control of pore structure and size in freeze-dried collagen sponges, J Biomed Mater Res 58 (2001), pp. 352–357.

92.

K. Weadock, R.M. Olson, and F.H. Silver, Evaluation of collagen crosslinking techniques, Biomater Med Devices Artif Organs 11 (1983), pp. 293–318.

93.

L. Gonzalez, and T. Wess, Use of attenuated total reflection-Fourier transform infrared spectroscopy to measure collagen degradation in historical parchments, Appl Spectrosc 62 (2008), pp. 1108–1114.

94.

U. Hersel, C. Dahmen, and H. Kessler, RGD modified polymers: biomaterials for stimulated cell adhesion and beyond, Biomaterials 24 (2003), pp. 4385–4415.

95.

E.V. Dare, M. Griffith, P. Poitras, J.A. Kaupp, S.D. Waldman, D.J. Carlsson, et al., Genipin cross-linked fibrin hydrogels for in vitro human articular cartilage tissue-engineered regeneration, Cells Tissues Organs 190 (2009), pp. 313–325.

96.

C.M. Elvin, S.J. Danon, A.G. Brownlee, J.F. White, M. Hickey, N.E. Liyou, et al., Evaluation of photo-crosslinked fibrinogen as a rapid and strong tissue adhesive, J Biomed Mater Res A 93 (2010), pp. 687–695

97.

E.D. Grassl, T.R. Oegema, and R.T. Tranquillo, Fibrin as an alternative biopolymer to type-I collagen for the fabrication of a media equivalent, J Biomed Mater Res 60 (2002), pp. 607–612.

98.

E. Cholewinski, M. Dietrich, T.C. Flanagan, T. Schmitz-Rode, and S. Jockenhoevel, Tranexamic acid – an alternative to aprotinin in fibrin-based cardiovascular tissue engineering, Tissue Eng Part A 15 (2009), pp. 3645–3653.

99.

C.B. Herbert, C. Nagaswami, G.D. Bittner, J.A. Hubbell, and J.W. Weisel, Effects of fibrin micromorphology on neurite growth from dorsal root ganglia cultured in three-dimensional fibrin gels, J Biomed Mater Res 40 (1998), pp. 551–559.

100.

L. Yao, D.D. Swartz, S.F. Gugino, J.A. Russell, and S.T. Andreadis, Fibrin-based tissue-engineered blood vessels: differential effects of biomaterial and culture parameters on mechanical strength and vascular reactivity, Tissue Eng 11 (2005), pp. 991–1003.

101.

S.L. Rowe, S. Lee, and J.P. Stegemann, Influence of thrombin concentration on the mechanical and morphological properties of cell-seeded fibrin hydrogels, Acta Biomater 3 (2007), pp. 59–67.

102.

S.L. Rowe, and J.P. Stegemann, Interpenetrating collagen-fibrin composite matrices with varying protein contents and ratios, Biomacromolecules 7 (2006), pp. 2942–2948.

103.

T.A. Ahmed, E.V. Dare, and M. Hincke, Fibrin: a versatile scaffold for tissue engineering applications, Tissue Eng Part B Rev 14 (2008), pp. 199–215.

104.

B.C. Isenberg, C. Williams, and R.T. Tranquillo, Small-diameter artificial arteries engineered in vitro, Circ Res 98 (2006), pp. 25–35.

105.

F.M. Shaikh, A. Callanan, E.G. Kavanagh, P.E. Burke, P.A. Grace, and T.M. McGloughlin, Fibrin: a natural biodegradable scaffold in vascular tissue engineering, Cells Tissues Organs 188 (2008), pp. 333–346.

106.

L.J. Currie, J.R. Sharpe, and R. Martin, The use of fibrin glue in skin grafts and tissue-engineered skin replacements: a review, Plast Reconstr Surg 108 (2001), pp. 1713–1726.

107.

A.C. MacIntosh, V.R. Kearns, A. Crawford, and P.V. Hatton, Skeletal tissue engineering using silk biomaterials, J Tissue Eng Regen Med 2 (2008), pp. 71–80.

108.

S. Sofia, M.B. McCarthy, G. Gronowicz, and D.L. Kaplan, Functionalized silk-based biomaterials for bone formation, J Biomed Mater Res 54 (2001), pp. 139–148.

109.

E. Bini, C.W. Foo, J. Huang, V. Karageorgiou, B. Kitchel, and D.L. Kaplan, RGD-functionalized bioengineered spider dragline silk biomaterial, Biomacromolecules 7 (2006), pp. 3139–3145.

110.

C. Kirker-Head, V. Karageorgiou, S. Hofmann, R. Fajardo, O. Betz, H.P. Merkle, et al., BMP-silk composite matrices heal critically sized femoral defects, Bone 41 (2007), pp. 247–255.

111.

A. Sugihara, K. Sugiura, H. Morita, T. Ninagawa, K. Tubouchi, R. Tobe, et al., Promotive effects of a silk film on epidermal recovery from full-thickness skin wounds, Proc Soc Exp Biol Med 225 (2000), pp. 58–64.

112.

H. Fan, H. Liu, S.L. Toh, and J.C. Goh, Anterior cruciate ligament regeneration using mesenchymal stem cells and silk scaffold in large animal model, Biomaterials 30 (2009), pp. 4967–4977.

113.

H. Liu, H. Fan, S.L. Toh, and J.C. Goh, A comparison of rabbit mesenchymal stem cells and anterior cruciate ligament fibroblasts responses on combined silk scaffolds, Biomaterials 29 (2008), pp. 1443–1453.

114.

F.A. Petrigliano, D.R. McAllister, and B.M. Wu, Tissue engineering for anterior cruciate ligament reconstruction: a review of current strategies, Arthroscopy 22 (2006), pp. 441–451.

115.

Y. Wang, D.J. Blasioli, H.J. Kim, H.S. Kim, and D.L. Kaplan, Cartilage tissue engineering with silk scaffolds and human articular chondrocytes, Biomaterials 27 (2006), pp. 4434–4442.

116.

M. Fini, A. Motta, P. Torricelli, G. Giavaresi, N. Nicoli Aldini, M. Tschon, et al., The healing of confined critical size cancellous defects in the presence of silk fibroin hydrogel, Biomaterials 26 (2005), pp. 3527–3536.

117.

Y. Tamada, New process to form a silk fibroin porous 3-D structure, Biomacromolecules 6 (2005), pp. 3100–3106.

118.

B.S. Brooke, A. Bayes-Genis, and D.Y. Li, New insights into elastin and vascular disease, Trends Cardiovasc Med 13 (2003), pp. 176–181.

119.

W. Shi, S. Bellusci, and D. Warburton, Lung development and adult lung diseases, Chest 132 (2007), pp. 651–656.

120.

J.B. Leach, J.B. Wolinsky, P.J. Stone, and J.Y. Wong, Crosslinked alpha-elastin biomaterials: towards a processable elastin mimetic scaffold, Acta Biomater 1 (2005), pp. 155–164.

121.

W.F. Daamen, S.T. Nillesen, T. Hafmans, J.H. Veerkamp, M.J. van Luyn, and T.H. van Kuppevelt, Tissue response of defined collagen-elastin scaffolds in young and adult rats with special attention to calcification, Biomaterials 26 (2005), pp. 81–92.

122.

K. Trabbic-Carlson, L.A. Setton, and A. Chilkoti, Swelling and mechanical behaviors of chemically cross-linked hydrogels of elastin-like polypeptides, Biomacromolecules 4 (2003), pp. 572–580.

123.

F.J. Arias, V. Reboto, S. Martin, I. Lopez, and J.C. Rodriguez-Cabello, Tailored recombinant elastin-like polymers for advanced biomedical and nano(bio)technological applications, Biotechnol Lett 28 (2006), pp. 687–695.

124.

Y. Wu, J.A. MacKay, J.R. McDaniel, A. Chilkoti, and R.L. Clark, Fabrication of elastin-like polypeptide nanoparticles for drug delivery by electrospraying, Biomacromolecules 10 (2009), pp. 19–24.

125.

H. Betre, L.A. Setton, D.E. Meyer, and A. Chilkoti, Characterization of a genetically engineered elastin-like polypeptide for cartilaginous tissue repair, Biomacromolecules 3 (2002), pp. 910–916.

126.

H. Betre, S.R. Ong, F. Guilak, A. Chilkoti, B. Fermor, and L.A. Setton, Chondrocytic differentiation of human adipose-derived adult stem cells in elastin-like polypeptide, Biomaterials 27 (2006), pp. 91–99.

127.

S. Ito, S. Ishimaru, and S.E. Wilson, Effect of coacervated alpha-elastin on proliferation of vascular smooth muscle and endothelial cells, Angiology 49 (1998), pp. 289–297.

128.

N. Annabi, S.M. Mithieux, A.S. Weiss, and F. Dehghani, The fabrication of elastin-based hydrogels using high pressure CO(2), Biomaterials 30 (2009), pp. 1–7.

129.

M. Li, M.J. Mondrinos, M.R. Gandhi, F.K. Ko, A.S. Weiss, and P.I. Lelkes, Electrospun protein fibers as matrices for tissue engineering, Biomaterials 26 (2005), pp. 5999–6008.

130.

S.A. Sell, M.J. McClure, K. Garg, P.S. Wolfe, and G.L. Bowlin, Electrospinning of collagen/biopolymers for regenerative medicine and cardiovascular tissue engineering, Adv Drug Deliv Rev 61 (2009), pp. 1007–1019.

131.

L. Buttafoco, N.G. Kolkman, P. Engbers-Buijtenhuijs, A.A. Poot, P.J. Dijkstra, I. Vermes, et al., Electrospinning of collagen and elastin for tissue engineering applications, Biomaterials 27 (2006), pp. 724–734.

132.

E.D. Boland, J.A. Matthews, K.J. Pawlowski, D.G. Simpson, G.E. Wnek, and G.L. Bowlin, Electrospinning collagen and elastin: preliminary vascular tissue engineering, Front Biosci 9 (2004), pp. 1422–1432.

133.

G.D. Prestwich, and J.W. Kuo, Chemically-modified HA for therapy and regenerative medicine, Curr Pharm Biotechnol 9 (2008), pp. 242–245.

134.

K.L. Beasley, M.A. Weiss, and R.A. Weiss, Hyaluronic acid fillers: a comprehensive review, Facial Plast Surg 25 (2009), pp. 86–94.

135.

N. Bellamy, J. Campbell, V. Robinson, T. Gee, R. Bourne, and G. Wells, Viscosupplementation for the treatment of osteoarthritis of the knee, Cochrane Database Syst Rev (2006), pp. CD005321.

136.

V. Colletta, D. Dioguardi, A. Di Lonardo, G. Maggio, and F. Torasso, A trial to assess the efficacy and tolerability of Hyalofill-F in non-healing venous leg ulcers, J Wound Care 12 (2003), pp. 357–360.

137.

G.D. Prestwich, D.M. Marecak, J.F. Marecek, K.P. Vercruysse, and M.R. Ziebell, Controlled chemical modification of hyaluronic acid: synthesis, applications, and biodegradation of hydrazide derivatives, J Control Release 53 (1998), pp. 93–103.

138.

D. Campoccia, P. Doherty, M. Radice, P. Brun, G. Abatangelo, and D.F. Williams, Semisynthetic resorbable materials from hyaluronan esterification, Biomaterials 19 (1998), pp. 2101–2127.

139.

J.W. Kuo, D.A. Swann, and G.D. Prestwich, Chemical modification of hyaluronic acid by carbodiimides, Bioconjug Chem 2 (1991), pp. 232–241.

140.

A. Magnani, A. Albanese, S. Lamponi, and R. Barbucci, Blood-interaction performance of differently sulphated hyaluronic acids, Thromb Res 81 (1996), pp. 383–395.

141.

X. Jia, J. Burdick, J. Kobler, R. Clifton, J. Rosowski, S. Zeitels, et al., Synthesis and characterization of in situ cross-linkable hyaluronic acid-based hydrogels with potential application for vocal fold regeneration, Macromolecules 37 (2004), pp. 3239–3248.

142.

K. Tomihata, and Y. Ikada, Crosslinking of hyaluronic acid with glutaraldehyde, J Polym Sci A Polym Chem 35 (1997), pp. 3553–3559.

143.

T. Miyazaki, C. Yomota, and S. Okada, Development and release characterization of hyaluronan-doxycycline gels based on metal coordination, J Control Release 76 (2001), pp. 337–347.

144.

K. Tomihata, and Y. Ikada, Crosslinking of hyaluronic acid with water-soluble carbodiimide, J Biomed Mater Res 37 (1997), pp. 243–251.

145.

K.A. Smeds, A. Pfister-Serres, D. Miki, K. Dastgheib, M. Inoue, D.L. Hatchell, et al., Photocrosslinkable polysaccharides for in situ hydrogel formation, J Biomed Mater Res 54 (2001), pp. 115–121.

146.

J. Baier Leach, K.A. Bivens, C.W. Patrick, Jr., and C.E. Schmidt, Photocrosslinked hyaluronic acid hydrogels: natural, biodegradable tissue engineering scaffolds, Biotechnol Bioeng 82 (2003), pp. 578–589.

147.

S. Sahoo, C. Chung, S. Khetan, and J.A. Burdick, Hydrolytically degradable hyaluronic acid hydrogels with controlled temporal structures, Biomacromolecules 9 (2008), pp. 1088–1092.

148.

K.R. Kirker, Y. Luo, J.H. Nielson, J. Shelby, and G.D. Prestwich, Glycosaminoglycan hydrogel films as bio-interactive dressings for wound healing, Biomaterials 23 (2002), pp. 3661–3671.

149.

B. Grigolo, G. Lisignoli, G. Desando, C. Cavallo, E. Marconi, M. Tschon, et al., Osteoarthritis treated with mesenchymal stem cells on hyaluronan-based scaffold in rabbit, Tissue Eng Part C Methods 15 (2009), pp. 647–658.

150.

L.A. Solchaga, J.E. Dennis, V.M. Goldberg, and A.I. Caplan, Hyaluronic acid-based polymers as cell carriers for tissue-engineered repair of bone and cartilage, J Orthop Res 17 (1999), pp. 205–213.

151.

K.Y. Lee, L. Jeong, Y.O. Kang, S.J. Lee, and W.H. Park, Electrospinning of polysaccharides for regenerative medicine, Adv Drug Deliv Rev 61 (2009), pp. 1020–1032.

152.

J. Li, A. He, J. Zheng, and C.C. Han, Gelatin and gelatin-hyaluronic acid nanofibrous membranes produced by electrospinning of their aqueous solutions, Biomacromolecules 7 (2006), pp. 2243–2247.

153.

J.L. Ifkovits, H.G. Sundararaghavan, and J.A. Burdick, Electrospinning fibrous polymer scaffolds for tissue engineering and cell culture, J Vis Exp 32 (2009), http://www.jove.com/index/Details.stp?ID=1589, doi: 10.3791/1589.

154.

G. Orive, S.K. Tam, J.L. Pedraz, and J.P. Halle, Biocompatibility of alginate-poly-L-lysine microcapsules for cell therapy, Biomaterials 27 (2006), pp. 3691–3700.

155.

L. Shapiro, and S. Cohen, Novel alginate sponges for cell culture and transplantation, Biomaterials 18 (1997), pp. 583–590.

156.

K. Draget, K. Ostgaard, and O. Smidsrod, Homogeneous alginate gels – a technical approach, Carbohydr Polym 14 (1990), pp. 159–178.

157.

C.K. Kuo, and P.X. Ma, Ionically crosslinked alginate hydrogels as scaffolds for tissue engineering: part 1. Structure, gelation rate and mechanical properties, Biomaterials 22 (2001), pp. 511–521.

158.

O. Jeon, K.H. Bouhadir, J.M. Mansour, and E. Alsberg, Photocrosslinked alginate hydrogels with tunable biodegradation rates and mechanical properties, Biomaterials 30 (2009), pp. 2724–2734.

159.

K. Lee, K. Bouhadir, and D. Mooney, Degradation behavior of covalently cross-linked poly(aldehyde guluronate) hydrogels, Macromolecules 33 (2000), pp. 97–101.

160.

J.L. Drury, R.G. Dennis, and D.J. Mooney, The tensile properties of alginate hydrogels, Biomaterials 25 (2004), pp. 3187–3199.

161.

E.R. West, L.D. Shea, and T.K. Woodruff, Engineering the follicle microenvironment, Semin Reprod Med 25 (2007), pp. 287–299.

162.

J.A. Rowley, G. Madlambayan, and D.J. Mooney, Alginate hydrogels as synthetic extracellular matrix materials, Biomaterials 20 (1999), pp. 45–53.

163.

E. Alsberg, K.W. Anderson, A. Albeiruti, J.A. Rowley, and D.J. Mooney, Engineering growing tissues, Proc Natl Acad Sci U S A 99 (2002), pp. 12025–12030.

164.

N. Cheng, E. Wauthier, and L.M. Reid, Mature human hepatocytes from ex vivo differentiation of alginate-encapsulated hepatoblasts, Tissue Eng Part A 14 (2008), pp. 1–7.

165.

M. Dvir-Ginzberg, I. Gamlieli-Bonshtein, R. Agbaria, and S. Cohen, Liver tissue engineering within alginate scaffolds: effects of cell-seeding density on hepatocyte viability, morphology, and function, Tissue Eng 9 (2003), pp. 757–766.

166.

C. Shi, Y. Zhu, X. Ran, M. Wang, Y. Su, and T. Cheng, Therapeutic potential of chitosan and its derivatives in regenerative medicine, J Surg Res 133 (2006), pp. 185–192.

167.

I.K. Park, J. Yang, H.J. Jeong, H.S. Bom, I. Harada, T. Akaike, et al., Galactosylated chitosan as a synthetic extracellular matrix for hepatocytes attachment, Biomaterials 24 (2003), pp. 2331–2337.

168.

T.H. Kim, J.W. Nah, M.H. Cho, T.G. Park, and C.S. Cho, Receptor-mediated gene delivery into antigen presenting cells using mannosylated chitosan/DNA nanoparticles, J Nanosci Nanotechnol 6 (2006), pp. 2796–2803.

169.

M. Suzuki, S. Itoh, I. Yamaguchi, K. Takakuda, H. Kobayashi, K. Shinomiya, et al., Tendon chitosan tubes covalently coupled with synthesized laminin peptides facilitate nerve regeneration in vivo, J Neurosci Res 72 (2003), pp. 646–659.

170.

M.H. Ho, D.M. Wang, H.J. Hsieh, H.C. Liu, T.Y. Hsien, J.Y. Lai, et al., Preparation and characterization of RGD-immobilized chitosan scaffolds, Biomaterials 26 (2005), pp. 3197–3206.

171.

Z.M. Wu, X.G. Zhang, C. Zheng, C.X. Li, S.M. Zhang, R.N. Dong, et al., Disulfide-crosslinked chitosan hydrogel for cell viability and controlled protein release, Eur J Pharm Sci 37 (2009), pp. 198–206.

172.

D.L. Nettles, S.H. Elder, and J.A. Gilbert, Potential use of chitosan as a cell scaffold material for cartilage tissue engineering, Tissue Eng 8 (2002), pp. 1009–1016.

173.

S. Hirano, Chitin biotechnology applications, Biotechnol Annu Rev 2 (1996), pp. 237–258.

174.

H.C. Ott, T.S. Matthiesen, S.K. Goh, L.D. Black, S.M. Kren, T.I. Netoff, et al., Perfusion-decellularized matrix: using nature's platform to engineer a bioartificial heart, Nat Med 14 (2008), pp. 213–221.

175.

K.L. Chen, D. Eberli, J.J. Yoo, and A. Atala, Regenerative Medicine Special Feature: Bioengineered corporal tissue for structural and functional restoration of the penis, Proc Natl Acad Sci U S A 107 (2010), pp. 3346–3350

176.

J.M. Singelyn, J.A. DeQuach, S.B. Seif-Naraghi, R.B. Littlefield, P.J. Schup-Magoffin, and K.L. Christman, Naturally derived myocardial matrix as an injectable scaffold for cardiac tissue engineering, Biomaterials 30 (2009), pp. 5409–5416.

177.

K. Narayanan, K.J. Leck, S. Gao, and A.C. Wan, Three-dimensional reconstituted extracellular matrix scaffolds for tissue engineering, Biomaterials 30 (2009), pp. 4309–4317.

Titel: Natural Materials in Tissue Engineering Applications
verfasst von: Elyssa L. Monzack
Karien J. Rodriguez
Chloe M. McCoy
Xiaoxiao Gu
Kristyn S. Masters
Verlag: Springer Vienna
Buch: Biomaterials for Tissue Engineering Applications
Print ISBN: 978-3-7091-0384-5

Electronic ISBN: 978-3-7091-0385-2

Copyright-Jahr: 2011
DOI: https://doi.org/10.1007/978-3-7091-0385-2_8

Premium Partner

Marktübersichten

Die im Laufe eines Jahres in der „adhäsion“ veröffentlichten Marktübersichten helfen Anwendern verschiedenster Branchen, sich einen gezielten Überblick über Lieferantenangebote zu verschaffen.

Zur Marktübersicht