메뉴 건너뛰기




Volumn 34, Issue 3, 2013, Pages 704-712

Improving the osteogenic potential of BMP-2 with hyaluronic acid hydrogel modified with integrin-specific fibronectin fragment

Author keywords

Bone regeneration; Cell adhesion; Fibronectin; Hyaluronic acid hydrogel; Integrins; RhBMP 2

Indexed keywords

BONE REGENERATION; FIBRONECTIN; HYALURONIC ACID HYDROGELS; INTEGRINS; RHBMP-2;

EID: 84868463422     PISSN: 01429612     EISSN: 18785905     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2012.10.015     Document Type: Article
Times cited : (99)

References (50)
  • 1
    • 85045483986 scopus 로고    scopus 로고
    • Clinical effectiveness and cost-effectiveness of bone morphogenetic proteins in the non-healing of fractures and spinal fusion: a systematic review
    • iii-iv
    • Garrison K.R., Donell S., Ryder J., Shemilt I., Mugford M., Harvey I., et al. Clinical effectiveness and cost-effectiveness of bone morphogenetic proteins in the non-healing of fractures and spinal fusion: a systematic review. Health Technol Assess 2007, 11:1-150. iii-iv.
    • (2007) Health Technol Assess , vol.11 , pp. 1-150
    • Garrison, K.R.1    Donell, S.2    Ryder, J.3    Shemilt, I.4    Mugford, M.5    Harvey, I.6
  • 2
    • 70649108638 scopus 로고    scopus 로고
    • Bone morphogenetic proteins in orthopaedic surgery
    • Axelrad T.W., Einhorn T.A. Bone morphogenetic proteins in orthopaedic surgery. Cytokine Growth Factor Rev 2009, 20:481-488.
    • (2009) Cytokine Growth Factor Rev , vol.20 , pp. 481-488
    • Axelrad, T.W.1    Einhorn, T.A.2
  • 3
    • 49749137352 scopus 로고    scopus 로고
    • Periodontal tissue regeneration using fibroblast growth factor-2: randomized controlled phase II clinical trial
    • Kitamura M., Nakashima K., Kowashi Y., Fujii T., Shimauchi H., Sasano T., et al. Periodontal tissue regeneration using fibroblast growth factor-2: randomized controlled phase II clinical trial. PLoS ONE 2008, 3.
    • (2008) PLoS ONE , vol.3
    • Kitamura, M.1    Nakashima, K.2    Kowashi, Y.3    Fujii, T.4    Shimauchi, H.5    Sasano, T.6
  • 4
    • 57049129785 scopus 로고    scopus 로고
    • Addendum: commentary on becaplermin gel (Regranex) for hemangiomas
    • Frieden I.J. Addendum: commentary on becaplermin gel (Regranex) for hemangiomas. Pediatr Dermatol 2008, 25:590.
    • (2008) Pediatr Dermatol , vol.25 , pp. 590
    • Frieden, I.J.1
  • 5
    • 79959950769 scopus 로고    scopus 로고
    • A critical review of recombinant human bone morphogenetic protein-2 trials in spinal surgery: emerging safety concerns and lessons learned
    • Carragee E.J., Hurwitz E.L., Weiner B.K. A critical review of recombinant human bone morphogenetic protein-2 trials in spinal surgery: emerging safety concerns and lessons learned. Spine J 2011, 11:471-491.
    • (2011) Spine J , vol.11 , pp. 471-491
    • Carragee, E.J.1    Hurwitz, E.L.2    Weiner, B.K.3
  • 6
    • 70849099495 scopus 로고    scopus 로고
    • The extracellular matrix: not just pretty fibrils
    • Hynes R.O. The extracellular matrix: not just pretty fibrils. Science 2009, 326:1216-1219.
    • (2009) Science , vol.326 , pp. 1216-1219
    • Hynes, R.O.1
  • 7
    • 0036229695 scopus 로고    scopus 로고
    • Integrin regulation of growth factor receptors
    • Yamada K.M., Even-Ram S. Integrin regulation of growth factor receptors. Nat Cell Biol 2002, 4:E75-E76.
    • (2002) Nat Cell Biol , vol.4
    • Yamada, K.M.1    Even-Ram, S.2
  • 8
    • 0345687500 scopus 로고    scopus 로고
    • Positional control of cell fate through joint integrin/receptor protein kinase signaling
    • Giancotti F.G., Tarone G. Positional control of cell fate through joint integrin/receptor protein kinase signaling. Annu Rev Cell Dev Biol 2003, 19:173-206.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 173-206
    • Giancotti, F.G.1    Tarone, G.2
  • 9
    • 78650298934 scopus 로고    scopus 로고
    • Fibronectin growth factor-binding domains are required for fibroblast survival
    • Lin F., Ren X.D., Pan Z., Macri L., Zong W.X., Tonnesen M.G., et al. Fibronectin growth factor-binding domains are required for fibroblast survival. J Invest Dermatol 2011, 131:84-98.
    • (2011) J Invest Dermatol , vol.131 , pp. 84-98
    • Lin, F.1    Ren, X.D.2    Pan, Z.3    Macri, L.4    Zong, W.X.5    Tonnesen, M.G.6
  • 10
    • 33749676409 scopus 로고    scopus 로고
    • Heparin-II domain of fibronectin is a vascular endothelial growth factor-binding domain: enhancement of VEGF biological activity by a singular growth factor/matrix protein synergism
    • Wijelath E.S., Rahman S., Namekata M., Murray J., Nishimura T., Mostafavi-Pour Z., et al. Heparin-II domain of fibronectin is a vascular endothelial growth factor-binding domain: enhancement of VEGF biological activity by a singular growth factor/matrix protein synergism. Circ Res 2006, 99:853-860.
    • (2006) Circ Res , vol.99 , pp. 853-860
    • Wijelath, E.S.1    Rahman, S.2    Namekata, M.3    Murray, J.4    Nishimura, T.5    Mostafavi-Pour, Z.6
  • 11
    • 80052951552 scopus 로고    scopus 로고
    • Engineering the growth factor microenvironment with fibronectin domains to promote wound and bone tissue healing
    • Martino M.M., Tortelli F., Mochizuki M., Traub S., Ben-David D., Kuhn G.A., et al. Engineering the growth factor microenvironment with fibronectin domains to promote wound and bone tissue healing. Sci Transl Med 2011, 3:100ra89.
    • (2011) Sci Transl Med , vol.3
    • Martino, M.M.1    Tortelli, F.2    Mochizuki, M.3    Traub, S.4    Ben-David, D.5    Kuhn, G.A.6
  • 12
    • 0032508626 scopus 로고    scopus 로고
    • Hyaluronidase and its substrate hyaluronan: biochemistry, biological activities and therapeutic uses
    • Menzel E.J., Farr C. Hyaluronidase and its substrate hyaluronan: biochemistry, biological activities and therapeutic uses. Cancer Lett 1998, 131:3-11.
    • (1998) Cancer Lett , vol.131 , pp. 3-11
    • Menzel, E.J.1    Farr, C.2
  • 13
    • 0032407701 scopus 로고    scopus 로고
    • Rapid hyaluronan uptake is associated with enhanced motility: implications for an intracellular mode of action
    • Collis L., Hall C., Lange L., Ziebell M., Prestwich R., Turley E.A. Rapid hyaluronan uptake is associated with enhanced motility: implications for an intracellular mode of action. FEBS Lett 1998, 440:444-449.
    • (1998) FEBS Lett , vol.440 , pp. 444-449
    • Collis, L.1    Hall, C.2    Lange, L.3    Ziebell, M.4    Prestwich, R.5    Turley, E.A.6
  • 14
    • 3042697038 scopus 로고    scopus 로고
    • Hyaluronan: from extracellular glue to pericellular cue
    • Toole B.P. Hyaluronan: from extracellular glue to pericellular cue. Nat Rev Cancer 2004, 4:528-539.
    • (2004) Nat Rev Cancer , vol.4 , pp. 528-539
    • Toole, B.P.1
  • 15
    • 0030820092 scopus 로고    scopus 로고
    • Hyaluronan: its nature, distribution, functions and turnover
    • Fraser J.R., Laurent T.C., Laurent U.B. Hyaluronan: its nature, distribution, functions and turnover. J Intern Med 1997, 242:27-33.
    • (1997) J Intern Med , vol.242 , pp. 27-33
    • Fraser, J.R.1    Laurent, T.C.2    Laurent, U.B.3
  • 16
    • 80054091847 scopus 로고    scopus 로고
    • Hyaluronic acid-based clinical biomaterials derived for cell and molecule delivery in regenerative medicine
    • Prestwich G.D. Hyaluronic acid-based clinical biomaterials derived for cell and molecule delivery in regenerative medicine. J Control Release 2011, 155:193-199.
    • (2011) J Control Release , vol.155 , pp. 193-199
    • Prestwich, G.D.1
  • 17
    • 79953067209 scopus 로고    scopus 로고
    • Hyaluronic acid hydrogels for biomedical applications
    • Burdick J.A., Prestwich G.D. Hyaluronic acid hydrogels for biomedical applications. Adv Mater 2011, 23:H41-H56.
    • (2011) Adv Mater , vol.23
    • Burdick, J.A.1    Prestwich, G.D.2
  • 18
    • 79959579500 scopus 로고    scopus 로고
    • Recombinant human bone morphogenetic protein-2: a randomized trial in open tibial fractures treated with reamed nail fixation
    • Aro H.T., Govender S., Patel A.D., Hernigou P., Perera de Gregorio A., Popescu G.I., et al. Recombinant human bone morphogenetic protein-2: a randomized trial in open tibial fractures treated with reamed nail fixation. J Bone Jt Surg Am 2011, 93:801-808.
    • (2011) J Bone Jt Surg Am , vol.93 , pp. 801-808
    • Aro, H.T.1    Govender, S.2    Patel, A.D.3    Hernigou, P.4    Perera de Gregorio, A.5    Popescu, G.I.6
  • 19
    • 33744815209 scopus 로고    scopus 로고
    • Recombinant human bone morphogenetic protein-2 in open tibial fractures. A subgroup analysis of data combined from two prospective randomized studies
    • Swiontkowski M.F., Aro H.T., Donell S., Esterhai J.L., Goulet J., Jones A., et al. Recombinant human bone morphogenetic protein-2 in open tibial fractures. A subgroup analysis of data combined from two prospective randomized studies. J Bone Jt Surg Am 2006, 88:1258-1265.
    • (2006) J Bone Jt Surg Am , vol.88 , pp. 1258-1265
    • Swiontkowski, M.F.1    Aro, H.T.2    Donell, S.3    Esterhai, J.L.4    Goulet, J.5    Jones, A.6
  • 22
    • 77951770613 scopus 로고    scopus 로고
    • Bone morphogenetic protein-2 delivered by hyaluronan-based hydrogel induces massive bone formation and healing of cranial defects in minipigs
    • Docherty-Skogh A.C., Bergman K., Waern M.J., Ekman S., Hultenby K., Ossipov D., et al. Bone morphogenetic protein-2 delivered by hyaluronan-based hydrogel induces massive bone formation and healing of cranial defects in minipigs. Plast Reconstr Surg 2010, 125:1383-1392.
    • (2010) Plast Reconstr Surg , vol.125 , pp. 1383-1392
    • Docherty-Skogh, A.C.1    Bergman, K.2    Waern, M.J.3    Ekman, S.4    Hultenby, K.5    Ossipov, D.6
  • 23
    • 0037085254 scopus 로고    scopus 로고
    • Signaling properties of hyaluronan receptors
    • Turley E.A., Noble P.W., Bourguignon L.Y. Signaling properties of hyaluronan receptors. J Biol Chem 2002, 277:4589-4592.
    • (2002) J Biol Chem , vol.277 , pp. 4589-4592
    • Turley, E.A.1    Noble, P.W.2    Bourguignon, L.Y.3
  • 24
    • 0028090359 scopus 로고
    • Intercellular adhesion molecule-1 is a cell surface receptor for hyaluronan
    • McCourt P.A., Ek B., Forsberg N., Gustafson S. Intercellular adhesion molecule-1 is a cell surface receptor for hyaluronan. J Biol Chem 1994, 269:30081-30084.
    • (1994) J Biol Chem , vol.269 , pp. 30081-30084
    • McCourt, P.A.1    Ek, B.2    Forsberg, N.3    Gustafson, S.4
  • 25
    • 33646351039 scopus 로고    scopus 로고
    • Fibronectin functional domains coupled to hyaluronan stimulate adult human dermal fibroblast responses critical for wound healing
    • Ghosh K., Ren X.D., Shu X.Z., Prestwich G.D., Clark R.A. Fibronectin functional domains coupled to hyaluronan stimulate adult human dermal fibroblast responses critical for wound healing. Tissue Eng 2006, 12:601-613.
    • (2006) Tissue Eng , vol.12 , pp. 601-613
    • Ghosh, K.1    Ren, X.D.2    Shu, X.Z.3    Prestwich, G.D.4    Clark, R.A.5
  • 26
    • 1942421295 scopus 로고    scopus 로고
    • Attachment and spreading of fibroblasts on an RGD peptide-modified injectable hyaluronan hydrogel
    • Shu X.Z., Ghosh K., Liu Y., Palumbo F.S., Luo Y., Clark R.A., et al. Attachment and spreading of fibroblasts on an RGD peptide-modified injectable hyaluronan hydrogel. J Biomed Mater Res A 2004, 68:365-375.
    • (2004) J Biomed Mater Res A , vol.68 , pp. 365-375
    • Shu, X.Z.1    Ghosh, K.2    Liu, Y.3    Palumbo, F.S.4    Luo, Y.5    Clark, R.A.6
  • 28
    • 0027997413 scopus 로고
    • Selective recognition of cyclic RGD peptides of NMR defined conformation by alpha IIb beta 3, alpha V beta 3, and alpha 5 beta 1 integrins
    • Pfaff M., Tangemann K., Muller B., Gurrath M., Muller G., Kessler H., et al. Selective recognition of cyclic RGD peptides of NMR defined conformation by alpha IIb beta 3, alpha V beta 3, and alpha 5 beta 1 integrins. J Biol Chem 1994, 269:20233-20238.
    • (1994) J Biol Chem , vol.269 , pp. 20233-20238
    • Pfaff, M.1    Tangemann, K.2    Muller, B.3    Gurrath, M.4    Muller, G.5    Kessler, H.6
  • 29
    • 33344461837 scopus 로고    scopus 로고
    • Integrins and angiogenesis: a sticky business
    • Serini G., Valdembri D., Bussolino F. Integrins and angiogenesis: a sticky business. Exp Cell Res 2006, 312:651-658.
    • (2006) Exp Cell Res , vol.312 , pp. 651-658
    • Serini, G.1    Valdembri, D.2    Bussolino, F.3
  • 30
    • 84877009256 scopus 로고    scopus 로고
    • Priming integrin alpha5 promotes human mesenchymal stromal cell osteoblast differentiation and osteogenesis
    • Hamidouche Z., Fromigue O., Ringe J., Haupl T., Vaudin P., Srouji S., et al. Priming integrin alpha5 promotes human mesenchymal stromal cell osteoblast differentiation and osteogenesis. Bone 2009, 44:S218-S219.
    • (2009) Bone , vol.44
    • Hamidouche, Z.1    Fromigue, O.2    Ringe, J.3    Haupl, T.4    Vaudin, P.5    Srouji, S.6
  • 31
    • 42249087139 scopus 로고    scopus 로고
    • The effect of integrin-specific bioactive coatings on tissue healing and implant osseointegration
    • Petrie T.A., Raynor J.E., Reyes C.D., Burns K.L., Collard D.M., Garcia A.J. The effect of integrin-specific bioactive coatings on tissue healing and implant osseointegration. Biomaterials 2008, 29:2849-2857.
    • (2008) Biomaterials , vol.29 , pp. 2849-2857
    • Petrie, T.A.1    Raynor, J.E.2    Reyes, C.D.3    Burns, K.L.4    Collard, D.M.5    Garcia, A.J.6
  • 32
    • 0036941808 scopus 로고    scopus 로고
    • Novel mutant human fibronectin FIII9-10 domain pair with increased conformational stability and biological activity
    • van der Walle C.F., Altroff H., Mardon H.J. Novel mutant human fibronectin FIII9-10 domain pair with increased conformational stability and biological activity. Protein Eng 2002, 15:1021-1024.
    • (2002) Protein Eng , vol.15 , pp. 1021-1024
    • van der Walle, C.F.1    Altroff, H.2    Mardon, H.J.3
  • 33
    • 57749206799 scopus 로고    scopus 로고
    • Controlling integrin specificity and stem cell differentiation in 2D and 3D environments through regulation of fibronectin domain stability
    • Martino M.M., Mochizuki M., Rothenfluh D.A., Rempel S.A., Hubbell J.A., Barker T.H. Controlling integrin specificity and stem cell differentiation in 2D and 3D environments through regulation of fibronectin domain stability. Biomaterials 2009, 30:1089-1097.
    • (2009) Biomaterials , vol.30 , pp. 1089-1097
    • Martino, M.M.1    Mochizuki, M.2    Rothenfluh, D.A.3    Rempel, S.A.4    Hubbell, J.A.5    Barker, T.H.6
  • 34
    • 84865808757 scopus 로고    scopus 로고
    • Critical assessment of rhBMP-2 mediated bone induction: an in vitro and in vivo evaluation
    • Kisiel M., Ventura M., Oommen O.P., George A., Walboomers X.F., Hilborn J., et al. Critical assessment of rhBMP-2 mediated bone induction: an in vitro and in vivo evaluation. J Control Release 2012, 162:646-653.
    • (2012) J Control Release , vol.162 , pp. 646-653
    • Kisiel, M.1    Ventura, M.2    Oommen, O.P.3    George, A.4    Walboomers, X.F.5    Hilborn, J.6
  • 36
    • 78049360698 scopus 로고    scopus 로고
    • Modular approach to functional hyaluronic acid hydrogels using orthogonal chemical reactions
    • Ossipov D.A., Yang X., Varghese O., Kootala S., Hilborn J. Modular approach to functional hyaluronic acid hydrogels using orthogonal chemical reactions. Chem Commun 2010, 46:8368-8370.
    • (2010) Chem Commun , vol.46 , pp. 8368-8370
    • Ossipov, D.A.1    Yang, X.2    Varghese, O.3    Kootala, S.4    Hilborn, J.5
  • 37
    • 77956526891 scopus 로고    scopus 로고
    • Functionalization of hyaluronic acid with chemoselective groups via a disulfide-based protection strategy for in situ formation of mechanically stable hydrogels
    • Ossipov D.A., Piskounova S., Varghese O.P., Hilborn J. Functionalization of hyaluronic acid with chemoselective groups via a disulfide-based protection strategy for in situ formation of mechanically stable hydrogels. Biomacromolecules 2010, 11:2247-2254.
    • (2010) Biomacromolecules , vol.11 , pp. 2247-2254
    • Ossipov, D.A.1    Piskounova, S.2    Varghese, O.P.3    Hilborn, J.4
  • 38
    • 79961150251 scopus 로고    scopus 로고
    • Preparation of hyaluronic acid nanoparticles via hydrophobic association assisted chemical cross-linking - an orthogonal modular approach
    • Yang X., Kootala S., Hilborn J., Ossipov D.A. Preparation of hyaluronic acid nanoparticles via hydrophobic association assisted chemical cross-linking - an orthogonal modular approach. Soft Matter 2011, 7:7517-7525.
    • (2011) Soft Matter , vol.7 , pp. 7517-7525
    • Yang, X.1    Kootala, S.2    Hilborn, J.3    Ossipov, D.A.4
  • 39
    • 14844329852 scopus 로고    scopus 로고
    • Design and synthesis of N-maleimido-functionalized hydrophilic polymers via copper-mediated living radical polymerization: a suitable alternative to PEGylation chemistry
    • Mantovani G., Lecolley F., Tao L., Haddleton D.M., Clerx J., Cornelissen J.J., et al. Design and synthesis of N-maleimido-functionalized hydrophilic polymers via copper-mediated living radical polymerization: a suitable alternative to PEGylation chemistry. J Am Chem Soc 2005, 127:2966-2973.
    • (2005) J Am Chem Soc , vol.127 , pp. 2966-2973
    • Mantovani, G.1    Lecolley, F.2    Tao, L.3    Haddleton, D.M.4    Clerx, J.5    Cornelissen, J.J.6
  • 40
    • 48449102772 scopus 로고    scopus 로고
    • Synthesis of versatile thiol-reactive polymer scaffolds via RAFT polymerization
    • Wong L., Boyer C., Jia Z., Zareie H.M., Davis T.P., Bulmus V. Synthesis of versatile thiol-reactive polymer scaffolds via RAFT polymerization. Biomacromolecules 2008, 9:1934-1944.
    • (2008) Biomacromolecules , vol.9 , pp. 1934-1944
    • Wong, L.1    Boyer, C.2    Jia, Z.3    Zareie, H.M.4    Davis, T.P.5    Bulmus, V.6
  • 41
    • 3242661774 scopus 로고    scopus 로고
    • Quantitative methods for analysis of integrin binding and focal adhesion formation on biomaterial surfaces
    • Keselowsky B.G., Garcia A.J. Quantitative methods for analysis of integrin binding and focal adhesion formation on biomaterial surfaces. Biomaterials 2005, 26:413-418.
    • (2005) Biomaterials , vol.26 , pp. 413-418
    • Keselowsky, B.G.1    Garcia, A.J.2
  • 44
    • 79957809134 scopus 로고    scopus 로고
    • The biology of fracture healing
    • Marsell R., Einhorn T.A. The biology of fracture healing. Injury 2011, 42:551-555.
    • (2011) Injury , vol.42 , pp. 551-555
    • Marsell, R.1    Einhorn, T.A.2
  • 45
    • 33947312170 scopus 로고    scopus 로고
    • Human mesenchymal stem cells in contact with their environment: surface characteristics and the integrin system
    • Docheva D., Popov C., Mutschler W., Schieker M. Human mesenchymal stem cells in contact with their environment: surface characteristics and the integrin system. J Cell Mol Med 2007, 11:21-38.
    • (2007) J Cell Mol Med , vol.11 , pp. 21-38
    • Docheva, D.1    Popov, C.2    Mutschler, W.3    Schieker, M.4
  • 46
    • 46049108806 scopus 로고    scopus 로고
    • Bone development and its relation to fracture repair. The role of mesenchymal osteoblasts and surface osteoblasts
    • Shapiro F. Bone development and its relation to fracture repair. The role of mesenchymal osteoblasts and surface osteoblasts. Eur Cell Mater 2008, 15:53-76.
    • (2008) Eur Cell Mater , vol.15 , pp. 53-76
    • Shapiro, F.1
  • 48
    • 48049110299 scopus 로고    scopus 로고
    • Characterizing proteins and their interactions in cells and tissues using the in situ proximity ligation assay
    • Soderberg O., Leuchowius K.J., Gullberg M., Jarvius M., Weibrecht I., Larsson L.G., et al. Characterizing proteins and their interactions in cells and tissues using the in situ proximity ligation assay. Methods 2008, 45:227-232.
    • (2008) Methods , vol.45 , pp. 227-232
    • Soderberg, O.1    Leuchowius, K.J.2    Gullberg, M.3    Jarvius, M.4    Weibrecht, I.5    Larsson, L.G.6
  • 49
    • 0037089824 scopus 로고    scopus 로고
    • Temporal progression of angiogenesis and basal lamina deposition after contusive spinal cord injury in the adult rat
    • Loy D.N., Crawford C.H., Darnall J.B., Burke D.A., Onifer S.M., Whittemore S.R. Temporal progression of angiogenesis and basal lamina deposition after contusive spinal cord injury in the adult rat. J Comp Neurol 2002, 445:308-324.
    • (2002) J Comp Neurol , vol.445 , pp. 308-324
    • Loy, D.N.1    Crawford, C.H.2    Darnall, J.B.3    Burke, D.A.4    Onifer, S.M.5    Whittemore, S.R.6
  • 50
    • 78649727712 scopus 로고    scopus 로고
    • The 12th-14th type III repeats of fibronectin function as a highly promiscuous growth factor-binding domain
    • Martino M.M., Hubbell J.A. The 12th-14th type III repeats of fibronectin function as a highly promiscuous growth factor-binding domain. FASEB J 2010, 24:4711-4721.
    • (2010) FASEB J , vol.24 , pp. 4711-4721
    • Martino, M.M.1    Hubbell, J.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.