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Volumn 102, Issue 1, 2014, Pages 170-179

A comparative study of polyethylene glycol hydrogels derivatized with the RGD peptide and the cell-binding domain of fibronectin

Author keywords

cell adhesion; cell binding domain; fibronectin; polyethylene glycol hydrogel; rheology; spreading

Indexed keywords

ADDITION REACTIONS; AMINO ACIDS; CELL ADHESION; CELLS; ELECTROPHORESIS; FUNCTIONAL GROUPS; PEPTIDES; PHOTOPOLYMERIZATION; POLYETHYLENE GLYCOLS; RHEOLOGY; SODIUM DODECYL SULFATE;

EID: 84888639329     PISSN: 15493296     EISSN: 15524965     Source Type: Journal    
DOI: 10.1002/jbm.a.34687     Document Type: Article
Times cited : (16)

References (40)
  • 1
    • 77951089569 scopus 로고    scopus 로고
    • Bioactive modification of poly(ethylene glycol) hydrogels for tissue engineering
    • Zhu J,. Bioactive modification of poly(ethylene glycol) hydrogels for tissue engineering. Biomaterials 2010; 31: 4639-4656.
    • (2010) Biomaterials , vol.31 , pp. 4639-4656
    • Zhu, J.1
  • 2
    • 0036342297 scopus 로고    scopus 로고
    • Photoencapsulation of osteoblasts in injectable RGD-modified PEG hydrogels for bone tissue engineering
    • Burdick JA, Anseth KS,. Photoencapsulation of osteoblasts in injectable RGD-modified PEG hydrogels for bone tissue engineering. Biomaterials 2002; 23: 4315-4323.
    • (2002) Biomaterials , vol.23 , pp. 4315-4323
    • Burdick, J.A.1    Anseth, K.S.2
  • 3
    • 33846297021 scopus 로고    scopus 로고
    • Physiologic pulsatile flow bioreactor conditioning of poly(ethylene glycol)-based tissue engineered vascular grafts
    • Hahn MS, McHale MK, Wang E, Schmedlen RH, West JL,. Physiologic pulsatile flow bioreactor conditioning of poly(ethylene glycol)-based tissue engineered vascular grafts. Ann Biomed Eng 2007; 35: 190-200.
    • (2007) Ann Biomed Eng , vol.35 , pp. 190-200
    • Hahn, M.S.1    McHale, M.K.2    Wang, E.3    Schmedlen, R.H.4    West, J.L.5
  • 4
    • 0031743721 scopus 로고    scopus 로고
    • Fibroblasts cultured from venous ulcers display cellular characteristics of senescence
    • Mendez MV, Stanley A, Park HY, Shon K, Phillips T, Menzoian JO,. Fibroblasts cultured from venous ulcers display cellular characteristics of senescence. J Vasc Surg 1998; 28: 876-883.
    • (1998) J Vasc Surg , vol.28 , pp. 876-883
    • Mendez, M.V.1    Stanley, A.2    Park, H.Y.3    Shon, K.4    Phillips, T.5    Menzoian, J.O.6
  • 5
    • 0027971378 scopus 로고
    • The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function
    • Aota S, Nomizu M, Yamada KM,. The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function. J Biol Chem 1994; 269: 24756-24761.
    • (1994) J Biol Chem , vol.269 , pp. 24756-24761
    • Aota, S.1    Nomizu, M.2    Yamada, K.M.3
  • 6
    • 0030050396 scopus 로고    scopus 로고
    • 2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region
    • Leahy DJ, Aukhil I, Erickson HP,. 2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell 1996; 84: 155-164.
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 7
    • 11244284850 scopus 로고    scopus 로고
    • Interdomain tilt angle determines integrin-dependent function of the ninth and tenth FIII domains of human fibronectin
    • Altroff H, Schlinkert R, van der Walle CF, Bernini A, Campbell ID, Werner JM, Mardon HJ,. Interdomain tilt angle determines integrin-dependent function of the ninth and tenth FIII domains of human fibronectin. J Biol Chem 2004; 279: 55995-56003.
    • (2004) J Biol Chem , vol.279 , pp. 55995-56003
    • Altroff, H.1    Schlinkert, R.2    Van Der Walle, C.F.3    Bernini, A.4    Campbell, I.D.5    Werner, J.M.6    Mardon, H.J.7
  • 8
    • 33645972915 scopus 로고    scopus 로고
    • Effect of RGD secondary structure and the synergy site PHSRN on cell adhesion, spreading and specific integrin engagement
    • Ochsenhirt SE, Kokkoli E, McCarthy JB, Tirrell M,. Effect of RGD secondary structure and the synergy site PHSRN on cell adhesion, spreading and specific integrin engagement. Biomaterials 2006; 27: 3863-3874.
    • (2006) Biomaterials , vol.27 , pp. 3863-3874
    • Ochsenhirt, S.E.1    Kokkoli, E.2    McCarthy, J.B.3    Tirrell, M.4
  • 9
    • 57749206799 scopus 로고    scopus 로고
    • Controlling integrin specificity and stem cell differentiation in 2D and 3D environments through regulation of fibronectin domain stability
    • Martino MM, Mochizuki M, Rothenfluh DA, Rempel SA, Hubbell JA, Barker TH,. 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
  • 10
    • 33746255971 scopus 로고    scopus 로고
    • Integrin specificity and enhanced cellular activities associated with surfaces presenting a recombinant fibronectin fragment compared to RGD supports
    • Petrie TA, Capadona JR, Reyes CD, Garcia AJ,. Integrin specificity and enhanced cellular activities associated with surfaces presenting a recombinant fibronectin fragment compared to RGD supports. Biomaterials 2006; 27: 5459-5470.
    • (2006) Biomaterials , vol.27 , pp. 5459-5470
    • Petrie, T.A.1    Capadona, J.R.2    Reyes, C.D.3    Garcia, A.J.4
  • 11
    • 33646351039 scopus 로고    scopus 로고
    • Fibronectin functional domains coupled to hyaluronan stimulate adult human dermal fibroblast responses critical for wound healing
    • Ghosh K, Ren XD, Shu XZ, Prestwich GD, Clark RA,. 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
  • 12
    • 70449107589 scopus 로고    scopus 로고
    • Capturing complex protein gradients on biomimetic hydrogels for cell-based assays
    • Cosson S, Kobel SA, Lutolf MP,. Capturing complex protein gradients on biomimetic hydrogels for cell-based assays. Adv Funct Mater 2009; 19: 3411-3419.
    • (2009) Adv Funct Mater , vol.19 , pp. 3411-3419
    • Cosson, S.1    Kobel, S.A.2    Lutolf, M.P.3
  • 14
    • 0028931691 scopus 로고
    • Crystal structures of a schistosomal drug and vaccine target: Glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug praziquantel
    • McTigue MA, Williams DR, Tainer JA,. Crystal structures of a schistosomal drug and vaccine target: Glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug praziquantel. J Mol Biol 1995; 246: 21-27.
    • (1995) J Mol Biol , vol.246 , pp. 21-27
    • McTigue, M.A.1    Williams, D.R.2    Tainer, J.A.3
  • 15
    • 0035210936 scopus 로고    scopus 로고
    • Systematic modulation of Michael-type reactivity of thiols through the use of charged amino acids
    • Lutolf MP, Tirelli N, Cerritelli S, Cavalli L, Hubbell JA,. Systematic modulation of Michael-type reactivity of thiols through the use of charged amino acids. Bioconjug Chem 2001; 12: 1051-1056.
    • (2001) Bioconjug Chem , vol.12 , pp. 1051-1056
    • Lutolf, M.P.1    Tirelli, N.2    Cerritelli, S.3    Cavalli, L.4    Hubbell, J.A.5
  • 16
    • 0000189906 scopus 로고
    • Relative nucleophilic reactivities of amino groups and mercaptide ions in addition reactions with α,β-unsaturated compounds
    • Friedman M, Cavins JF, Wall JS,. Relative nucleophilic reactivities of amino groups and mercaptide ions in addition reactions with α,β- unsaturated compounds. J Am Chem Soc 1965; 87: 3672-3682.
    • (1965) J Am Chem Soc , vol.87 , pp. 3672-3682
    • Friedman, M.1    Cavins, J.F.2    Wall, J.S.3
  • 17
    • 0034888333 scopus 로고    scopus 로고
    • Conjugate addition reactions combined with free-radical cross-linking for the design of materials for tissue engineering
    • Elbert DL, Hubbell JA,. Conjugate addition reactions combined with free-radical cross-linking for the design of materials for tissue engineering. Biomacromolecules 2001; 2: 430-441.
    • (2001) Biomacromolecules , vol.2 , pp. 430-441
    • Elbert, D.L.1    Hubbell, J.A.2
  • 18
    • 0032125816 scopus 로고    scopus 로고
    • Characterization of permeability and network structure of interfacially photopolymerized poly(ethylene glycol) diacrylate hydrogels
    • Cruise GM, Scharp DS, Hubbell JA,. Characterization of permeability and network structure of interfacially photopolymerized poly(ethylene glycol) diacrylate hydrogels. Biomaterials 1998; 19: 1287-1294.
    • (1998) Biomaterials , vol.19 , pp. 1287-1294
    • Cruise, G.M.1    Scharp, D.S.2    Hubbell, J.A.3
  • 19
    • 67650473662 scopus 로고    scopus 로고
    • Decorin moieties tethered into PEG networks induce chondrogenesis of human mesenchymal stem cells
    • Salinas CN, Anseth KS,. Decorin moieties tethered into PEG networks induce chondrogenesis of human mesenchymal stem cells. J Biomed Mater Res 2009; 90: 456-464.
    • (2009) J Biomed Mater Res , vol.90 , pp. 456-464
    • Salinas, C.N.1    Anseth, K.S.2
  • 20
    • 84855682038 scopus 로고    scopus 로고
    • A surface derivatization strategy for combinatorial analysis of cell response to mixtures of protein domains
    • Chiang C, Karuri SW, Kshatriya PP, Schwartz J, Schwarzbauer J, Karuri NW,. A surface derivatization strategy for combinatorial analysis of cell response to mixtures of protein domains. Langmuir 2012; 28: 548-556.
    • (2012) Langmuir , vol.28 , pp. 548-556
    • Chiang, C.1    Karuri, S.W.2    Kshatriya, P.P.3    Schwartz, J.4    Schwarzbauer, J.5    Karuri, N.W.6
  • 21
    • 84862199593 scopus 로고    scopus 로고
    • A combinatorial approach for directing the amount of fibronectin fibrils assembled by cells that uses surfaces derivatized with mixtures of fibronectin and cell binding domains
    • Kshatriya PP, Karuri SW, Chiang C, Karuri NW,. A combinatorial approach for directing the amount of fibronectin fibrils assembled by cells that uses surfaces derivatized with mixtures of fibronectin and cell binding domains. Biotechnol Prog 2012; 28: 862-871.
    • (2012) Biotechnol Prog , vol.28 , pp. 862-871
    • Kshatriya, P.P.1    Karuri, S.W.2    Chiang, C.3    Karuri, N.W.4
  • 22
    • 2942558681 scopus 로고    scopus 로고
    • Encapsulating chondrocytes in degrading PEG hydrogels with high modulus: Engineering gel structural changes to facilitate cartilaginous tissue production
    • Bryant SJ, Bender RJ, Durand KL, Anseth KS,. Encapsulating chondrocytes in degrading PEG hydrogels with high modulus: Engineering gel structural changes to facilitate cartilaginous tissue production. Biotechnol Bioeng 2004; 86: 747-755.
    • (2004) Biotechnol Bioeng , vol.86 , pp. 747-755
    • Bryant, S.J.1    Bender, R.J.2    Durand, K.L.3    Anseth, K.S.4
  • 23
    • 36249003877 scopus 로고    scopus 로고
    • Differential response of adult and embryonic mesenchymal progenitor cells to mechanical compression in hydrogels
    • Terraciano V, Hwang N, Moroni L, Park HB, Zhang Z, Mizrahi J, Seliktar D, Elisseeff J,. Differential response of adult and embryonic mesenchymal progenitor cells to mechanical compression in hydrogels. Stem Cells 2007; 25: 2730-2738.
    • (2007) Stem Cells , vol.25 , pp. 2730-2738
    • Terraciano, V.1    Hwang, N.2    Moroni, L.3    Park, H.B.4    Zhang, Z.5    Mizrahi, J.6    Seliktar, D.7    Elisseeff, J.8
  • 24
    • 0038676822 scopus 로고    scopus 로고
    • Fibronectin matrix polymerization regulates small airway epithelial cell migration
    • Hocking DC, Chang CH,. Fibronectin matrix polymerization regulates small airway epithelial cell migration. Am J Physiol Lung Cell Mol Physiol 2003; 285: L169-L179.
    • (2003) Am J Physiol Lung Cell Mol Physiol , vol.285
    • Hocking, D.C.1    Chang, C.H.2
  • 25
    • 0030036963 scopus 로고    scopus 로고
    • Altered rate of fibronectin matrix assembly by deletion of the first type III repeats
    • Sechler JL, Takada Y, Schwarzbauer JE,. Altered rate of fibronectin matrix assembly by deletion of the first type III repeats. J Cell Biol 1996; 134: 573-583.
    • (1996) J Cell Biol , vol.134 , pp. 573-583
    • Sechler, J.L.1    Takada, Y.2    Schwarzbauer, J.E.3
  • 26
    • 49749177569 scopus 로고
    • A colorimetric method for determining low concentrations of mercaptans
    • Ellman GL,. A colorimetric method for determining low concentrations of mercaptans. Arch Biochem Biophys 1958; 74: 443-450.
    • (1958) Arch Biochem Biophys , vol.74 , pp. 443-450
    • Ellman, G.L.1
  • 27
    • 51549098607 scopus 로고    scopus 로고
    • Mixed mode thiol-acrylate photopolymerizations for the synthesis of PEG-peptide hydrogels
    • Salinas CN, Anseth KS,. Mixed mode thiol-acrylate photopolymerizations for the synthesis of PEG-peptide hydrogels. Macromolecules 2008; 41: 6019-6026.
    • (2008) Macromolecules , vol.41 , pp. 6019-6026
    • Salinas, C.N.1    Anseth, K.S.2
  • 28
    • 0035284411 scopus 로고    scopus 로고
    • Peptide and protein PEGylation: A review of problems and solutions
    • Veronese FM,. Peptide and protein PEGylation: A review of problems and solutions. Biomaterials 2001; 22: 405-417.
    • (2001) Biomaterials , vol.22 , pp. 405-417
    • Veronese, F.M.1
  • 29
    • 0026536995 scopus 로고
    • Detection and molecular weight determination of polyethylene glycol-modified hirudin by staining after sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Kurfurst MM,. Detection and molecular weight determination of polyethylene glycol-modified hirudin by staining after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Anal Biochem 1992; 200: 244-248.
    • (1992) Anal Biochem , vol.200 , pp. 244-248
    • Kurfurst, M.M.1
  • 31
    • 63649087809 scopus 로고    scopus 로고
    • Probing the conformation of the fibronectin III1-2 domain by fluorescence resonance energy transfer
    • Karuri NW, Lin Z, Rye HS, Schwarzbauer JE,. Probing the conformation of the fibronectin III1-2 domain by fluorescence resonance energy transfer. J Biol Chem 2009; 284: 3445-3452.
    • (2009) J Biol Chem , vol.284 , pp. 3445-3452
    • Karuri, N.W.1    Lin, Z.2    Rye, H.S.3    Schwarzbauer, J.E.4
  • 34
    • 84864483207 scopus 로고    scopus 로고
    • Structural characteristics determine the cause of the low enzyme activity of two thiopurine S-methyltransferase allelic variants: A biophysical characterization of TPMT*2 and TPMT*5
    • Wennerstrand P, Dametto P, Hennig J, Klingstedt T, Skoglund K, Appell ML, Martensson LG,. Structural characteristics determine the cause of the low enzyme activity of two thiopurine S-methyltransferase allelic variants: A biophysical characterization of TPMT*2 and TPMT*5. Biochemistry 2012; 51: 5912-5920.
    • (2012) Biochemistry , vol.51 , pp. 5912-5920
    • Wennerstrand, P.1    Dametto, P.2    Hennig, J.3    Klingstedt, T.4    Skoglund, K.5    Appell, M.L.6    Martensson, L.G.7
  • 35
    • 0037181179 scopus 로고    scopus 로고
    • Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins
    • Masino L, Kelly G, Leonard K, Trottier Y, Pastore A,. Solution structure of polyglutamine tracts in GST-polyglutamine fusion proteins. FEBS Lett 2002; 513: 267-272.
    • (2002) FEBS Lett , vol.513 , pp. 267-272
    • Masino, L.1    Kelly, G.2    Leonard, K.3    Trottier, Y.4    Pastore, A.5
  • 36
    • 0032007690 scopus 로고    scopus 로고
    • Incorporation of adhesion peptides into non-adhesive hydrogels useful for tissue resurfacing
    • Hern DL, Hubbell JA,. Incorporation of adhesion peptides into non-adhesive hydrogels useful for tissue resurfacing. J Biomed Mater Res 1998; 39: 266-276.
    • (1998) J Biomed Mater Res , vol.39 , pp. 266-276
    • Hern, D.L.1    Hubbell, J.A.2
  • 37
    • 33745001030 scopus 로고    scopus 로고
    • The use of poly(ethylene glycol) hydrogels to investigate the impact of ECM chemistry and mechanics on smooth muscle cells
    • Peyton SR, Raub CB, Keschrumrus VP, Putnam AJ,. The use of poly(ethylene glycol) hydrogels to investigate the impact of ECM chemistry and mechanics on smooth muscle cells. Biomaterials 2006; 27: 4881-4893.
    • (2006) Biomaterials , vol.27 , pp. 4881-4893
    • Peyton, S.R.1    Raub, C.B.2    Keschrumrus, V.P.3    Putnam, A.J.4
  • 38
    • 4544264684 scopus 로고    scopus 로고
    • Myotubes differentiate optimally on substrates with tissue-like stiffness: Pathological implications for soft or stiff microenvironments
    • Engler AJ, Griffin MA, Sen S, Bonnemann CG, Sweeney HL, Discher DE,. Myotubes differentiate optimally on substrates with tissue-like stiffness: Pathological implications for soft or stiff microenvironments. J Cell Biol 2004; 166: 877-887.
    • (2004) J Cell Biol , vol.166 , pp. 877-887
    • Engler, A.J.1    Griffin, M.A.2    Sen, S.3    Bonnemann, C.G.4    Sweeney, H.L.5    Discher, D.E.6
  • 39
    • 0033917881 scopus 로고    scopus 로고
    • Cell movement is guided by the rigidity of the substrate
    • Lo CM, Wang HB, Dembo M, Wang YL,. Cell movement is guided by the rigidity of the substrate. Biophys J 2000; 79: 144-152.
    • (2000) Biophys J , vol.79 , pp. 144-152
    • Lo, C.M.1    Wang, H.B.2    Dembo, M.3    Wang, Y.L.4
  • 40
    • 0037107551 scopus 로고    scopus 로고
    • Fibronectin at a glance
    • Pankov R, Yamada KM,. Fibronectin at a glance. J Cell Sci 2002; 115: 3861-3863.
    • (2002) J Cell Sci , vol.115 , pp. 3861-3863
    • Pankov, R.1    Yamada, K.M.2


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