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Volumn 29, Issue 2, 2013, Pages 493-504

PEGylated human plasma fibronectin is proteolytically stable, supports cell adhesion, cell migration, focal adhesion assembly, and fibronectin fibrillogenesis

Author keywords

Adhesion; Chymotrypsin; Fibrillogenesis; Fibronectin; Focal adhesion; Migration; Neutrophil elastase; Polyethylene glycol; Proteolysis; Spreading

Indexed keywords

CHYMOTRYPSIN; ELASTASE; FIBRILLOGENESIS; FIBRONECTIN; FOCAL ADHESIONS; MIGRATION; SPREADING;

EID: 84875948110     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.1689     Document Type: Article
Times cited : (14)

References (63)
  • 2
    • 0028129140 scopus 로고
    • Identification of neutrophil elastase as the proteinase in burn wound fluid responsible for degradation of fibronectin
    • Grinnell F, Zhu M. Identification of neutrophil elastase as the proteinase in burn wound fluid responsible for degradation of fibronectin. J Invest Dermatol. 1994;103 155-161.
    • (1994) J Invest Dermatol. , vol.103 , pp. 155-161
    • Grinnell, F.1    Zhu, M.2
  • 3
    • 0028973014 scopus 로고
    • Alpha 1-antitrypsin is degraded and non-functional in chronic wounds but intact and functional in acute wounds: the inhibitor protects fibronectin from degradation by chronic wound fluid enzymes
    • Rao CN, Ladin DA, Liu YY, Chilukuri K, Hou ZZ, Woodley DT. Alpha 1-antitrypsin is degraded and non-functional in chronic wounds but intact and functional in acute wounds: the inhibitor protects fibronectin from degradation by chronic wound fluid enzymes. J Invest Dermatol. 1995;105:572-578.
    • (1995) J Invest Dermatol , vol.105 , pp. 572-578
    • Rao, C.N.1    Ladin, D.A.2    Liu, Y.Y.3    Chilukuri, K.4    Hou, Z.Z.5    Woodley, D.T.6
  • 5
    • 0029759530 scopus 로고    scopus 로고
    • Proteolysis regulates exposure of the IIICS-1 adhesive sequence in plasma fibronectin
    • Ugarova TP, Ljubimov AV, Deng L, Plow EF. Proteolysis regulates exposure of the IIICS-1 adhesive sequence in plasma fibronectin. Biochemistry. 1996;35:10913-10921.
    • (1996) Biochemistry , vol.35 , pp. 10913-10921
    • Ugarova, T.P.1    Ljubimov, A.V.2    Deng, L.3    Plow, E.F.4
  • 7
    • 70350644808 scopus 로고    scopus 로고
    • Proteolytic activity in wound fluids and tissues derived from chronic venous leg ulcers
    • Moor AN, Vachon DJ, Gould LJ. Proteolytic activity in wound fluids and tissues derived from chronic venous leg ulcers. Wound Repair Regen. 2009;17:832-839.
    • (2009) Wound Repair Regen , vol.17 , pp. 832-839
    • Moor, A.N.1    Vachon, D.J.2    Gould, L.J.3
  • 8
    • 53249142131 scopus 로고    scopus 로고
    • Immune cells in the healing skin wound: influential players at each stage of repair
    • Wilgus TA. Immune cells in the healing skin wound: influential players at each stage of repair. Pharmacol Res. 2008;58:112-116.
    • (2008) Pharmacol Res , vol.58 , pp. 112-116
    • Wilgus, T.A.1
  • 9
    • 0025667165 scopus 로고
    • Fibronectin profiles in normal and chronic wound fluid
    • Wysocki AB, Grinnell F. Fibronectin profiles in normal and chronic wound fluid. Lab Invest. 1990;63:825-831.
    • (1990) Lab Invest , vol.63 , pp. 825-831
    • Wysocki, A.B.1    Grinnell, F.2
  • 10
    • 0023851909 scopus 로고
    • Potential roles of fibronectin in cutaneous wound repair
    • Clark RA. Potential roles of fibronectin in cutaneous wound repair. Arch Dermatol. 1988;124:201-206.
    • (1988) Arch Dermatol , vol.124 , pp. 201-206
    • Clark, R.A.1
  • 12
    • 0030245742 scopus 로고    scopus 로고
    • Fibronectin and fibronectin fragments modulate the expression of proteinases and proteinase inhibitors in human periodontal ligament cells
    • Kapila YL, Kapila S, Johnson PW. Fibronectin and fibronectin fragments modulate the expression of proteinases and proteinase inhibitors in human periodontal ligament cells. Matrix Biol. 1996;15:251-261.
    • (1996) Matrix Biol , vol.15 , pp. 251-261
    • Kapila, Y.L.1    Kapila, S.2    Johnson, P.W.3
  • 14
    • 0034929831 scopus 로고    scopus 로고
    • A 10-kda fragment of fibronectin type III domain is a neutrophil chemoattractant purified from conditioned medium of rat granulation tissue
    • Shiota S, Takano K, Nakagawa H. A 10-kda fragment of fibronectin type III domain is a neutrophil chemoattractant purified from conditioned medium of rat granulation tissue. Biol Pharm Bull. 2001;24:835-837.
    • (2001) Biol Pharm Bull , vol.24 , pp. 835-837
    • Shiota, S.1    Takano, K.2    Nakagawa, H.3
  • 15
    • 0021742978 scopus 로고
    • Fibronectin and wound healing
    • Grinnell F. Fibronectin and wound healing. J Cell Biochem. 1984;26:107-116.
    • (1984) J Cell Biochem , vol.26 , pp. 107-116
    • Grinnell, F.1
  • 16
    • 0023178166 scopus 로고
    • Fibronectin's cell-adhesive domain and an amino-terminal matrix assembly domain participate in its assembly into fibroblast pericellular matrix
    • McDonald JA, Quade BJ, Broekelmann TJ, LaChance R, Forsman K, Hasegawa E, Akiyama S. Fibronectin's cell-adhesive domain and an amino-terminal matrix assembly domain participate in its assembly into fibroblast pericellular matrix. J Biol Chem. 1987;262:2957-2967.
    • (1987) J Biol Chem , vol.262 , pp. 2957-2967
    • McDonald, J.A.1    Quade, B.J.2    Broekelmann, T.J.3    LaChance, R.4    Forsman, K.5    Hasegawa, E.6    Akiyama, S.7
  • 18
    • 0018838451 scopus 로고
    • Fibroblast adhesion to fibrinogen and fibrin substrata: requirement for cold-insoluble globulin (plasma fibronectin)
    • Grinnell F, Feld M, Minter D. Fibroblast adhesion to fibrinogen and fibrin substrata: requirement for cold-insoluble globulin (plasma fibronectin). Cell. 1980;19:517-525.
    • (1980) Cell , vol.19 , pp. 517-525
    • Grinnell, F.1    Feld, M.2    Minter, D.3
  • 19
    • 79953186583 scopus 로고    scopus 로고
    • How PEGylation enhances the stability and potency of insulin: a molecular dynamics simulation
    • Yang C, Lu D, Liu Z. How PEGylation enhances the stability and potency of insulin: a molecular dynamics simulation. Biochemistry. 2011;50:2585-2593.
    • (2011) Biochemistry , vol.50 , pp. 2585-2593
    • Yang, C.1    Lu, D.2    Liu, Z.3
  • 20
    • 0032782071 scopus 로고    scopus 로고
    • Instability, stabilization, and formulation of liquid protein pharmaceuticals
    • Wang W. Instability, stabilization, and formulation of liquid protein pharmaceuticals. Int J Pharm. 1999;185:129-188.
    • (1999) Int J Pharm , vol.185 , pp. 129-188
    • Wang, W.1
  • 21
    • 51549092094 scopus 로고    scopus 로고
    • The impact of PEGylation on biological therapies
    • Veronese FM, Mero A. The impact of PEGylation on biological therapies. BioDrugs. 2008;22:315-329.
    • (2008) BioDrugs , vol.22 , pp. 315-329
    • Veronese, F.M.1    Mero, A.2
  • 22
    • 0023791465 scopus 로고
    • Transforming growth factor beta increases cell surface binding and assembly of exogenous (plasma) fibronectin by normal human fibroblasts
    • Allen-Hoffmann BL, Crankshaw CL, Mosher DF. Transforming growth factor beta increases cell surface binding and assembly of exogenous (plasma) fibronectin by normal human fibroblasts. Mol Cell Biol. 1988;8:4234-4242.
    • (1988) Mol Cell Biol , vol.8 , pp. 4234-4242
    • Allen-Hoffmann, B.L.1    Crankshaw, C.L.2    Mosher, D.F.3
  • 24
    • 80053232334 scopus 로고    scopus 로고
    • Plasma and cellular fibronectin: distinct and independent functions during tissue repair
    • To WS, Midwood KS. Plasma and cellular fibronectin: distinct and independent functions during tissue repair. Fibrogenesis Tissue Repair. 2011;4:21-38.
    • (2011) Fibrogenesis Tissue Repair , vol.4 , pp. 21-38
    • To, W.S.1    Midwood, K.S.2
  • 25
    • 0018377938 scopus 로고
    • Isolation of a collagen-binding fragment from fibronectin and cold-insoluble globulin
    • Balian G, Click EM, Crouch E, Davidson JM, Bornstein P. Isolation of a collagen-binding fragment from fibronectin and cold-insoluble globulin. J Biol Chem. 1979;254:1429-1432.
    • (1979) J Biol Chem , vol.254 , pp. 1429-1432
    • Balian, G.1    Click, E.M.2    Crouch, E.3    Davidson, J.M.4    Bornstein, P.5
  • 26
    • 79960686720 scopus 로고    scopus 로고
    • Probing the folded state of fibronectin type III domains in stretched fibrils by measuring buried cysteine accessibility
    • Lemmon CA, Ohashi T, Erickson HP. Probing the folded state of fibronectin type III domains in stretched fibrils by measuring buried cysteine accessibility. J Biol Chem. 2011;286:26375-26382.
    • (2011) J Biol Chem , vol.286 , pp. 26375-26382
    • Lemmon, C.A.1    Ohashi, T.2    Erickson, H.P.3
  • 27
    • 0028043949 scopus 로고
    • Fibronectin self-association is mediated by complementary sites within the amino-terminal one-third of the molecule
    • Aguirre KM, McCormick RJ, Schwarzbauer JE. Fibronectin self-association is mediated by complementary sites within the amino-terminal one-third of the molecule. J Biol Chem. 1994; 269:27863-27868.
    • (1994) J Biol Chem , vol.269 , pp. 27863-27868
    • Aguirre, K.M.1    McCormick, R.J.2    Schwarzbauer, J.E.3
  • 28
    • 0028364087 scopus 로고
    • Fibronectin's III-1 module contains a conformation-dependent binding site for the amino-terminal region of fibronectin
    • Hocking DC, Sottile J, McKeown-Longo PJ. Fibronectin's III-1 module contains a conformation-dependent binding site for the amino-terminal region of fibronectin. J Biol Chem. 1994; 269:19183-19187.
    • (1994) J Biol Chem , vol.269 , pp. 19183-19187
    • Hocking, D.C.1    Sottile, J.2    McKeown-Longo, P.J.3
  • 29
    • 36549012798 scopus 로고    scopus 로고
    • The heparin III-binding domain of fibronectin (III4-5 repeats) binds to fibronectin and inhibits fibronectin matrix assembly
    • Maqueda A, Moyano JV, Hernandez Del Cerro M, Peters DM, Garcia-Pardo A. The heparin III-binding domain of fibronectin (III4-5 repeats) binds to fibronectin and inhibits fibronectin matrix assembly. Matrix Biol. 2007;26:642-651.
    • (2007) Matrix Biol , vol.26 , pp. 642-651
    • Maqueda, A.1    Moyano, J.V.2    Hernandez Del Cerro, M.3    Peters, D.M.4    Garcia-Pardo, A.5
  • 30
    • 0029897753 scopus 로고    scopus 로고
    • A novel role for the integrin-binding III-10 module in fibronectin matrix assembly
    • Hocking DC, Smith RK, McKeown-Longo PJ. A novel role for the integrin-binding III-10 module in fibronectin matrix assembly. J Cell Biol. 1996;133:431-444.
    • (1996) J Cell Biol , vol.133 , pp. 431-444
    • Hocking, D.C.1    Smith, R.K.2    McKeown-Longo, P.J.3
  • 31
    • 0032579376 scopus 로고    scopus 로고
    • Fibronectin fibrillogenesis involves the heparin II binding domain of fibronectin
    • Bultmann H, Santas AJ, Peters DMP. Fibronectin fibrillogenesis involves the heparin II binding domain of fibronectin. J Biol Chem. 1998;273:2601-2609.
    • (1998) J Biol Chem , vol.273 , pp. 2601-2609
    • Bultmann, H.1    Santas, A.J.2    Peters, D.M.P.3
  • 32
    • 0021990020 scopus 로고
    • Incoporation of cellular and plasma fibronectin into smooth-muscle cell exreacellular-matrix invitro
    • Millis AJT, Hoyle M, Mann DM, Brennan MJ. Incoporation of cellular and plasma fibronectin into smooth-muscle cell exreacellular-matrix invitro. Proc Natl Acad Sci USA. 1985; 82:2746-2750.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 2746-2750
    • Millis, A.J.T.1    Hoyle, M.2    Mann, D.M.3    Brennan, M.J.4
  • 33
    • 78649727712 scopus 로고    scopus 로고
    • The 12th-14th type III repeats of fibronectin function as a highly promiscuous growth factor-binding domain
    • Martino MM. Hubbell JA. 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
  • 34
    • 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
  • 35
    • 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
  • 36
    • 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
  • 37
    • 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
  • 38
    • 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
  • 39
    • 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 Progr. 2012; 28: 862-871.
    • (2012) Biotechnol Progr , vol.28 , pp. 862-871
    • Kshatriya, P.P.1    Karuri, S.W.2    Chiang, C.3    Karuri, N.W.4
  • 40
    • 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
  • 41
    • 0037053359 scopus 로고    scopus 로고
    • Analysis of tissue transglutaminase function in the migration of swiss 3T3 fibroblasts - The active-state conformation of the enzyme does not affect cell motility but is important for its secretion
    • Balklava Z, Verderio E, Collighan R, Gross S, Adams J, Griffin M. Analysis of tissue transglutaminase function in the migration of swiss 3T3 fibroblasts - The active-state conformation of the enzyme does not affect cell motility but is important for its secretion. J Biol Chem. 2002;277:16567-16575.
    • (2002) J Biol Chem , vol.277 , pp. 16567-16575
    • Balklava, Z.1    Verderio, E.2    Collighan, R.3    Gross, S.4    Adams, J.5    Griffin, M.6
  • 43
    • 0026674919 scopus 로고
    • Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin
    • Hanks SK, Calalb MB, Harper MC, Patel SK. Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. Proc Natl Acad Sci USA. 1992;89:8487-8491.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8487-8491
    • Hanks, S.K.1    Calalb, M.B.2    Harper, M.C.3    Patel, S.K.4
  • 44
    • 34249746927 scopus 로고    scopus 로고
    • Attachment and proliferation of human dermal fibroblasts onto ECM-immobilized PLGA films
    • Zhang X, Tanaka J, Yu Y, Tabata Y. editors. Zurich-Uetikon: Trans Tech Publications Ltd; :-, 291-294.
    • Son HJ, Han DW, Kim HH, Kim HJ, Lee IS, Kim JK, Park JC. Attachment and proliferation of human dermal fibroblasts onto ECM-immobilized PLGA films. In: Zhang X, Tanaka J, Yu Y, Tabata Y. editors. ASBM6: Advanced Biomaterials VI. Zurich-Uetikon: Trans Tech Publications Ltd; 2005:288-289, 291-294.
    • (2005) ASBM6: Advanced Biomaterials VI , pp. 288-289
    • Son, H.J.1    Han, D.W.2    Kim, H.H.3    Kim, H.J.4    Lee, I.S.5    Kim, J.K.6    Park, J.C.7
  • 45
    • 23344453824 scopus 로고    scopus 로고
    • Fibronectin's central cell-binding domain supports focal adhesion formation and rho signal transduction
    • Wang RX, Clark RAF, Mosher DF, Ren XD. Fibronectin's central cell-binding domain supports focal adhesion formation and rho signal transduction. J Biol Chem. 2005;280:28803-28810.
    • (2005) J Biol Chem , vol.280 , pp. 28803-28810
    • Wang, R.X.1    Clark, R.A.F.2    Mosher, D.F.3    Ren, X.D.4
  • 47
    • 0019423313 scopus 로고
    • Induction of fibroblast chemotaxis by fibronectin. Localization of the chemotactic region to a 140,000-molecular weight non-gelatin-binding fragment
    • Postlethwaite AE, Keski-Oja J, Balian G, Kang AH., Induction of fibroblast chemotaxis by fibronectin. Localization of the chemotactic region to a 140, 000-molecular weight non-gelatin-binding fragment. J Exp Med. 1981;153:494-499.
    • (1981) J Exp Med , vol.153 , pp. 494-499
    • Postlethwaite, A.E.1    Keski-Oja, J.2    Balian, G.3    Kang, A.H.4
  • 48
    • 0041560152 scopus 로고    scopus 로고
    • Integrin alpha5beta1 supports the migration of Xenopus cranial neural crest on fibronectin
    • Alfandari D, Cousin H, Gaultier A, Hoffstrom BG, DeSimone DW. Integrin alpha5beta1 supports the migration of Xenopus cranial neural crest on fibronectin. Dev Biol. 2003;260:449-464.
    • (2003) Dev Biol , vol.260 , pp. 449-464
    • Alfandari, D.1    Cousin, H.2    Gaultier, A.3    Hoffstrom, B.G.4    DeSimone, D.W.5
  • 49
    • 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
  • 51
    • 0026233153 scopus 로고
    • Alternative splicing of fibronectin: three variants, three functions
    • Schwarzbauer JE. Alternative splicing of fibronectin: three variants, three functions. Bioessays. 1991;13:527-533.
    • (1991) Bioessays , vol.13 , pp. 527-533
    • Schwarzbauer, J.E.1
  • 52
    • 0021131134 scopus 로고
    • A single rat fibronectin gene generates three different mRNAs by alternative splicing of a complex exon
    • Tamkun JW, Schwarzbauer JE, Hynes RO. A single rat fibronectin gene generates three different mRNAs by alternative splicing of a complex exon. Proc Natl Acad Sci USA. 1984;81:5140-5144.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 5140-5144
    • Tamkun, J.W.1    Schwarzbauer, J.E.2    Hynes, R.O.3
  • 53
    • 0033515070 scopus 로고    scopus 로고
    • Dynamics and elasticity of the fibronectin matrix in living cell culture visualized by fibronectin-green fluorescent protein
    • Ohashi T, Kiehart DP, Erickson HP. Dynamics and elasticity of the fibronectin matrix in living cell culture visualized by fibronectin-green fluorescent protein. Proc Natl Acad Sci USA. 1999;96:2153-2158.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 2153-2158
    • Ohashi, T.1    Kiehart, D.P.2    Erickson, H.P.3
  • 55
    • 23944441761 scopus 로고    scopus 로고
    • Fibronectin fragmentation promotes alpha4beta1 integrin-mediated contraction of a fibrin-fibronectin provisional matrix
    • Valenick LV, Hsia HC, Schwarzbauer JE. Fibronectin fragmentation promotes alpha4beta1 integrin-mediated contraction of a fibrin-fibronectin provisional matrix. Exp Cell Res. 2005;309:48-55.
    • (2005) Exp Cell Res , vol.309 , pp. 48-55
    • Valenick, L.V.1    Hsia, H.C.2    Schwarzbauer, J.E.3
  • 56
    • 0024804591 scopus 로고
    • Selective secretion of alternatively spliced fibronectin variants
    • Schwarzbauer JE, Spencer CS, Wilson CL. Selective secretion of alternatively spliced fibronectin variants. J Cell Biol. 1989;109:3445-3453.
    • (1989) J Cell Biol , vol.109 , pp. 3445-3453
    • Schwarzbauer, J.E.1    Spencer, C.S.2    Wilson, C.L.3
  • 57
    • 0030753274 scopus 로고    scopus 로고
    • Modulation of cell-adhesive activity of fibronectin by the alternatively spliced EDA segment
    • Manabe R, Ohe N, Maeda T, Fukuda T, Sekiguchi K. Modulation of cell-adhesive activity of fibronectin by the alternatively spliced EDA segment. J Cell Biol. 1997;139:295-307.
    • (1997) J Cell Biol. , vol.139 , pp. 295-307
    • Manabe, R.1    Ohe, N.2    Maeda, T.3    Fukuda, T.4    Sekiguchi, K.5
  • 58
    • 0020490907 scopus 로고
    • Carbohydrates selectively protect a specific domain of fibronectin against proteases
    • Bernard BA, Yamada KM, Olden K. Carbohydrates selectively protect a specific domain of fibronectin against proteases. J Biol Chem. 1982;257:8549-8554.
    • (1982) J Biol Chem , vol.257 , pp. 8549-8554
    • Bernard, B.A.1    Yamada, K.M.2    Olden, K.3
  • 59
    • 0018383990 scopus 로고
    • Identification and isolation of a collagen-binding fragment of the adhesive glycoprotein fibronectin
    • Hahn LH, Yamada KM. Identification and isolation of a collagen-binding fragment of the adhesive glycoprotein fibronectin. Proc Natl Acad Sci USA. 1979;76:1160-1163.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 1160-1163
    • Hahn, L.H.1    Yamada, K.M.2
  • 60
    • 0027818981 scopus 로고
    • Basics of cutaneous wound repair
    • Clark RA. Basics of cutaneous wound repair. J Dermatol Surg Oncol. 1993;19:693-706.
    • (1993) J Dermatol Surg Oncol , vol.19 , pp. 693-706
    • Clark, R.A.1
  • 61
    • 68249159451 scopus 로고    scopus 로고
    • Instructional PowerPoint presentations for cutaneous wound healing and tissue response to sutures
    • Stroncek JD, Bell N, Reichert WM. Instructional PowerPoint presentations for cutaneous wound healing and tissue response to sutures. J Biomed Mater Res A. 2009;90:1230-1238.
    • (2009) J Biomed Mater Res A , vol.90 , pp. 1230-1238
    • Stroncek, J.D.1    Bell, N.2    Reichert, W.M.3


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