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Volumn 2, Issue 45, 2010, Pages

Tissue engineering: Multivalent integrin-specific ligands enhance tissue healing and biomaterial integration

Author keywords

[No Author keywords available]

Indexed keywords

ARGINYLGLYCYLASPARTIC ACID; BIOMATERIAL; BIOMIMETIC MATERIAL; DIMER; FIBRONECTIN; FOCAL ADHESION KINASE; INTEGRIN; MACROGOL; MONOMER; PENTAPEPTIDE; PROLYLHISTIDYLSERYLARGINYLASPARAGINE; SCLEROPROTEIN; TETRAMER; TISSUE ADHESIVE; TITANIUM; UNCLASSIFIED DRUG; VERY LATE ACTIVATION ANTIGEN 5; INTEGRIN ALPHAVBETA1; LIGAND; NANOMATERIAL; VITRONECTIN RECEPTOR;

EID: 77955874342     PISSN: 19466234     EISSN: 19466242     Source Type: Journal    
DOI: 10.1126/scitranslmed.3001002     Document Type: Article
Times cited : (131)

References (39)
  • 1
    • 19644367664 scopus 로고    scopus 로고
    • Synthetic biomaterials as instructive extracellularmicroenvironments for morphogenesis in tissue engineering
    • M. P. Lutolf, J. A. Hubbell, Synthetic biomaterials as instructive extracellularmicroenvironments for morphogenesis in tissue engineering. Nat. Biotechnol. 23, 47-55 (2005).
    • (2005) Nat. Biotechnol. , vol.23 , pp. 47-55
    • Lutolf, M.P.1    Hubbell, J.A.2
  • 2
    • 1842484779 scopus 로고    scopus 로고
    • Designing materials for biology and medicine
    • R. Langer, D. A. Tirrell, Designing materials for biology and medicine. Nature 428, 487-492 (2004).
    • (2004) Nature , vol.428 , pp. 487-492
    • Langer, R.1    Tirrell, D.A.2
  • 4
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • R. O. Hynes, Integrins: Bidirectional, allosteric signaling machines. Cell 110, 673-687 (2002).
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 5
    • 60749130274 scopus 로고    scopus 로고
    • Cell fate regulation by coupling mechanical cycles to biochemical signaling pathways
    • V. Vogel, M. P. Sheetz, Cell fate regulation by coupling mechanical cycles to biochemical signaling pathways. Curr. Opin. Cell Biol. 21, 38-46 (2009).
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 38-46
    • Vogel, V.1    Sheetz, M.P.2
  • 8
    • 0030880903 scopus 로고    scopus 로고
    • Interactions between integrin receptors and fibronectin are required for calvarial osteoblast differentiation in vitro
    • A. M. Moursi, R. K. Globus, C. H. Damsky, Interactions between integrin receptors and fibronectin are required for calvarial osteoblast differentiation in vitro. J. Cell Sci. 110, 2187-2196 (1997).
    • (1997) J. Cell Sci. , vol.110 , pp. 2187-2196
    • Moursi, A.M.1    Globus, R.K.2    Damsky, C.H.3
  • 9
    • 0035139608 scopus 로고    scopus 로고
    • Bone mineralization and osteoblast differentiation are negatively modulated by integrin avb3
    • S. L. Cheng, C. F. Lai, S. D. Blystone, L. V. Avioli, Bone mineralization and osteoblast differentiation are negatively modulated by integrin avb3. J. Bone Miner. Res. 16, 277-288 (2001).
    • (2001) J. Bone Miner. Res. , vol.16 , pp. 277-288
    • Cheng, S.L.1    Lai, C.F.2    Blystone, S.D.3    Avioli, L.V.4
  • 10
    • 23944456131 scopus 로고    scopus 로고
    • Get a grip: Integrins in cell-biomaterial interactions
    • A. J. García, Get a grip: Integrins in cell-biomaterial interactions. Biomaterials 26, 7525-7529 (2005).
    • (2005) Biomaterials , vol.26 , pp. 7525-7529
    • García, A.J.1
  • 11
    • 21744431870 scopus 로고    scopus 로고
    • Bio-adhesive surfaces to promote osteoblast differentiation and bone formation
    • A. J. García, C. D. Reyes, Bio-adhesive surfaces to promote osteoblast differentiation and bone formation. J. Dent. Res. 84, 407-413 (2005).
    • (2005) J. Dent. Res. , vol.84 , pp. 407-413
    • García, A.J.1    Reyes, C.D.2
  • 12
    • 0023637601 scopus 로고
    • New perspectives in cell adhesion: RGD and integrins
    • E. Ruoslahti, M. D. Pierschbacher, New perspectives in cell adhesion: RGD and integrins. Science 238, 491-497 (1987).
    • (1987) Science , vol.238 , pp. 491-497
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 13
    • 0028954797 scopus 로고
    • Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function
    • S. Miyamoto, S. K. Akiyama, K. M. Yamada, Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science 267, 883-885 (1995).
    • (1995) Science , vol.267 , pp. 883-885
    • Miyamoto, S.1    Akiyama, S.K.2    Yamada, K.M.3
  • 15
    • 0035516140 scopus 로고    scopus 로고
    • Transmembrane crosstalk between the extracellular matrix and the cytoskeleton
    • B. Geiger, A. Bershadsky, R. Pankov, K. M. Yamada, Transmembrane crosstalk between the extracellular matrix and the cytoskeleton. Nat. Rev. Mol. Cell Biol. 2, 793-805 (2001).
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 793-805
    • Geiger, B.1    Bershadsky, A.2    Pankov, R.3    Yamada, K.M.4
  • 17
    • 0036538656 scopus 로고    scopus 로고
    • Co-regulation of cell adhesion by nanoscale RGD organization and mechanical stimulus
    • L. Y. Koo, D. J. Irvine, A. M. Mayes, D. A. Lauffenburger, L. G. Griffith, Co-regulation of cell adhesion by nanoscale RGD organization and mechanical stimulus. J. Cell Sci. 115, 1423-1433 (2002).
    • (2002) J. Cell Sci. , vol.115 , pp. 1423-1433
    • Koo, L.Y.1    Irvine, D.J.2    Mayes, A.M.3    Lauffenburger, D.A.4    Griffith, L.G.5
  • 20
    • 35748963560 scopus 로고    scopus 로고
    • Tumor targeting with RGD peptide ligands - Design of new molecular conjugates for imaging and therapy of cancers
    • E. Garanger, D. Boturyn, P. Dumy, Tumor targeting with RGD peptide ligands - design of new molecular conjugates for imaging and therapy of cancers. Anticancer Agents Med. Chem. 7, 552-558 (2007).
    • (2007) Anticancer Agents Med. Chem. , vol.7 , pp. 552-558
    • Garanger, E.1    Boturyn, D.2    Dumy, P.3
  • 22
    • 0025881229 scopus 로고
    • 3-mediated fibroblast spreading and 140 nm for focal contact and stress fiber formation
    • 3-mediated fibroblast spreading and 140 nm for focal contact and stress fiber formation. J. Cell Biol. 114, 1089-1100 (1991).
    • (1991) J. Cell Biol. , vol.114 , pp. 1089-1100
    • Massia, S.P.1    Hubbell, J.A.2
  • 23
    • 42249087139 scopus 로고    scopus 로고
    • The effect of integrin-specific bioactive coatings on tissue healing and implant osseointegration
    • T. A. Petrie, J. E. Raynor, C. D. Reyes, K. L. Burns, D. M. Collard, A. J. García, The effect of integrin-specific bioactive coatings on tissue healing and implant osseointegration. Biomaterials 29, 2849-2857 (2008).
    • (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    García, A.J.6
  • 24
    • 0036615945 scopus 로고    scopus 로고
    • Effect of RGD peptide coating of titanium implants on periimplant bone formation in the alveolar crest. An experimental pilot study in dogs
    • H. Schliephake, D. Scharnweber, M. Dard, S. Rössler, A. Sewing, J. Meyer, D. Hoogestraat, Effect of RGD peptide coating of titanium implants on periimplant bone formation in the alveolar crest. An experimental pilot study in dogs. Clin. Oral Implants Res. 13, 312-319 (2002).
    • (2002) Clin. Oral Implants Res. , vol.13 , pp. 312-319
    • Schliephake, H.1    Scharnweber, D.2    Dard, M.3    Rössler, S.4    Sewing, A.5    Meyer, J.6    Hoogestraat, D.7
  • 25
    • 33846267301 scopus 로고    scopus 로고
    • Peri-implant bone formation and implant integration strength of peptide-modified p(AAM-co-EG/AAC) interpenetrating polymer network-coated titanium implants
    • T. A. Barber, J. E. Ho, A. De Ranieri, A. S. Virdi, D. R. Sumner, K. E. Healy, Peri-implant bone formation and implant integration strength of peptide-modified p(AAM-co-EG/AAC) interpenetrating polymer network-coated titanium implants. J. Biomed. Mater. Res. A 80, 306-320 (2007).
    • (2007) J Biomed Mater Res A , vol.80 , pp. 306-320
    • Barber, T.A.1    Ho, J.E.2    De Ranieri, A.3    Virdi, A.S.4    Sumner, D.R.5    Healy, K.E.6
  • 27
    • 0037096170 scopus 로고    scopus 로고
    • Trimers of the fibronectin cell adhesion domain localize to actin filament bundles and undergo rearward translocation
    • F. Coussen, D. Choquet, M. P. Sheetz, H. P. Erickson, Trimers of the fibronectin cell adhesion domain localize to actin filament bundles and undergo rearward translocation. J. Cell Sci. 115, 2581-2590 (2002).
    • (2002) J. Cell Sci. , vol.115 , pp. 2581-2590
    • Coussen, F.1    Choquet, D.2    Sheetz, M.P.3    Erickson, H.P.4
  • 28
    • 33746255971 scopus 로고    scopus 로고
    • Integrin specificity and enhanced cellular activities associated with surfaces presenting a recombinant fibronectin fragment compared to RGD supports
    • T. A. Petrie, J. R. Capadona, C. D. Reyes, A. J. García, Integrin specificity and enhanced cellular activities associated with surfaces presenting a recombinant fibronectin fragment compared to RGD supports. Biomaterials 27, 5459-5470 (2006).
    • (2006) Biomaterials , vol.27 , pp. 5459-5470
    • Petrie, T.A.1    Capadona, J.R.2    Reyes, C.D.3    García, A.J.4
  • 29
    • 34547362369 scopus 로고    scopus 로고
    • Controlling cell adhesion to titanium: Functionalization of poly[oligo(ethylene glycol)methacrylate] brushes with cell-adhesive peptides
    • J. E. Raynor, T. A. Petrie, A. J. García, D. M. Collard, Controlling cell adhesion to titanium: Functionalization of poly[oligo(ethylene glycol)methacrylate] brushes with cell-adhesive peptides. Adv. Mater. 19, 1724-1728 (2007).
    • (2007) Adv. Mater. , vol.19 , pp. 1724-1728
    • Raynor, J.E.1    Petrie, T.A.2    García, A.J.3    Collard, D.M.4
  • 31
    • 3242661774 scopus 로고    scopus 로고
    • Quantitative methods for analysis of integrin binding and focal adhesion formation on biomaterial surfaces
    • B. G. Keselowsky, A. J. García, Quantitative methods for analysis of integrin binding and focal adhesion formation on biomaterial surfaces. Biomaterials 26, 413-418 (2005).
    • (2005) Biomaterials , vol.26 , pp. 413-418
    • Keselowsky, B.G.1    García, A.J.2
  • 32
    • 0034803052 scopus 로고    scopus 로고
    • Focal adhesion kinase activity is required for bone morphogenetic protein - Smad1 signaling and osteoblastic differentiation in murine MC3T3-E1 cells
    • Y. Tamura, Y. Takeuchi, M. Suzawa, S. Fukumoto, M. Kato, K. Miyazono, T. Fujita, Focal adhesion kinase activity is required for bone morphogenetic protein - Smad1 signaling and osteoblastic differentiation in murine MC3T3-E1 cells. J. Bone Miner. Res. 16, 1772-1779 (2001).
    • (2001) J. Bone Miner. Res. , vol.16 , pp. 1772-1779
    • Tamura, Y.1    Takeuchi, Y.2    Suzawa, M.3    Fukumoto, S.4    Kato, M.5    Miyazono, K.6    Fujita, T.7
  • 33
    • 17844376765 scopus 로고    scopus 로고
    • Integrin binding specificity regulates biomaterial surface chemistry effects on cell differentiation
    • B. G. Keselowsky, D. M. Collard, A. J. García, Integrin binding specificity regulates biomaterial surface chemistry effects on cell differentiation. Proc. Natl. Acad. Sci. U.S.A. 102, 5953-5957 (2005).
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 5953-5957
    • Keselowsky, B.G.1    Collard, D.M.2    García, A.J.3
  • 34
    • 72949101455 scopus 로고    scopus 로고
    • Simple application of fibronectin-mimetic coating enhances osseointegration of titanium implants
    • T. A. Petrie, C. D. Reyes, K. L. Burns, A. J. García, Simple application of fibronectin-mimetic coating enhances osseointegration of titanium implants. J. Cell. Mol. Med. 13, 2602-2612 (2009).
    • (2009) J. Cell. Mol. Med. , vol.13 , pp. 2602-2612
    • Petrie, T.A.1    Reyes, C.D.2    Burns, K.L.3    García, A.J.4
  • 35
    • 34247494794 scopus 로고    scopus 로고
    • Biomolecular surface coating to enhance orthopaedic tissue healing and integration
    • C. D. Reyes, T. A. Petrie, K. L. Burns, Z. Schwartz, A. J. García, Biomolecular surface coating to enhance orthopaedic tissue healing and integration. Biomaterials 28, 3228-3235 (2007).
    • (2007) Biomaterials , vol.28 , pp. 3228-3235
    • Reyes, C.D.1    Petrie, T.A.2    Burns, K.L.3    Schwartz, Z.4    García, A.J.5
  • 36
    • 0036214480 scopus 로고    scopus 로고
    • Simulations of cell-surface integrin binding to nanoscale-clustered adhesion ligands
    • D. J. Irvine, K. A. Hue, A. M. Mayes, L. G. Griffith, Simulations of cell-surface integrin binding to nanoscale-clustered adhesion ligands. Biophys. J. 82, 120-132 (2002).
    • (2002) Biophys. J. , vol.82 , pp. 120-132
    • Irvine, D.J.1    Hue, K.A.2    Mayes, A.M.3    Griffith, L.G.4
  • 37
    • 21844461558 scopus 로고    scopus 로고
    • Integrin dimerization and ligand organization: Key components in integrin clustering for cell adhesion
    • C. J. Brinkerhoff, J. J. Linderman, Integrin dimerization and ligand organization: Key components in integrin clustering for cell adhesion. Tissue Eng. 11, 865-876 (2005).
    • (2005) Tissue Eng. , vol.11 , pp. 865-876
    • Brinkerhoff, C.J.1    Linderman, J.J.2
  • 38
    • 0041461882 scopus 로고    scopus 로고
    • Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin
    • G. Jiang, G. Giannone, D. R. Critchley, E. Fukumoto, M. P. Sheetz, Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin. Nature 424, 334-337 (2003).
    • (2003) Nature , vol.424 , pp. 334-337
    • Jiang, G.1    Giannone, G.2    Critchley, D.R.3    Fukumoto, E.4    Sheetz, M.P.5
  • 39
    • 77955879680 scopus 로고    scopus 로고
    • note
    • 7-10 for orthopedic repair. The authors declare that they have no competing interests.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.