메뉴 건너뛰기




Volumn 5, Issue 7, 2009, Pages 2623-2632

A chimeric epidermal growth factor with fibrin affinity promotes repair of injured keratinocyte sheets

Author keywords

Chimeric protein; EGF immobilization; Fibrin; Wound healing

Indexed keywords

CELL CULTURE; GROWTH KINETICS; PROTEINS; TISSUE; TISSUE REGENERATION;

EID: 68949148874     PISSN: 17427061     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.actbio.2009.03.022     Document Type: Article
Times cited : (29)

References (41)
  • 1
    • 28344448202 scopus 로고    scopus 로고
    • Fibrinogen and fibrin structure and functions
    • Mosesson M.W. Fibrinogen and fibrin structure and functions. J Thromb Haemost 3 (2005) 1894-1904
    • (2005) J Thromb Haemost , vol.3 , pp. 1894-1904
    • Mosesson, M.W.1
  • 2
    • 0013825447 scopus 로고
    • The stimulation of epidermal proliferation by a specific protein (EGF)
    • Cohen S. The stimulation of epidermal proliferation by a specific protein (EGF). Dev Biol 12 (1965) 394-407
    • (1965) Dev Biol , vol.12 , pp. 394-407
    • Cohen, S.1
  • 3
    • 0017349282 scopus 로고
    • Epidermal growth factor and the multiplication of cultured human epidermal keratinocytes
    • Rheinwald J.G., and Green H. Epidermal growth factor and the multiplication of cultured human epidermal keratinocytes. Nature 265 (1977) 421-424
    • (1977) Nature , vol.265 , pp. 421-424
    • Rheinwald, J.G.1    Green, H.2
  • 4
    • 0000686740 scopus 로고
    • Human epidermal growth factor: Isolation and chemical and biological properties
    • Cohen S., and Carpenter G. Human epidermal growth factor: Isolation and chemical and biological properties. Proc Natl Acad Sci USA 72 (1975) 1317-1321
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 1317-1321
    • Cohen, S.1    Carpenter, G.2
  • 5
    • 0017897928 scopus 로고
    • Control of proliferation of human vascular endothelial cells
    • Gospodarowicz D., Brown K.D., Birdwell C.R., and Zetter B. Control of proliferation of human vascular endothelial cells. J Cell Biol 77 (1978) 774-788
    • (1978) J Cell Biol , vol.77 , pp. 774-788
    • Gospodarowicz, D.1    Brown, K.D.2    Birdwell, C.R.3    Zetter, B.4
  • 7
    • 0011088676 scopus 로고
    • Role of cytokines in wound repair
    • Oppenheim J.J., Rossio J.L., and Gearing A.J.H. (Eds), Oxford University Press, Oxford
    • Jyung R.W., and Mustoe T.A. Role of cytokines in wound repair. In: Oppenheim J.J., Rossio J.L., and Gearing A.J.H. (Eds). Clinical application of cytokines (1993), Oxford University Press, Oxford 307-327
    • (1993) Clinical application of cytokines , pp. 307-327
    • Jyung, R.W.1    Mustoe, T.A.2
  • 8
    • 0035344210 scopus 로고    scopus 로고
    • Development of growth factor fusion proteins for cell-triggered drug delivery
    • Sakiyama-Elbert S.E., Panitch A., and Hubbell J.A. Development of growth factor fusion proteins for cell-triggered drug delivery. FASEB J 13 (2001) 1300-1302
    • (2001) FASEB J , vol.13 , pp. 1300-1302
    • Sakiyama-Elbert, S.E.1    Panitch, A.2    Hubbell, J.A.3
  • 9
    • 2342623399 scopus 로고    scopus 로고
    • Cell-demanded liberation of VEGF121 from fibrin implants induces local and controlled blood vessel growth
    • Ehrbar M., Djonov V.G., Schnell C., Tschanz S.Z., Martiny-Baron G., Schenk U., et al. Cell-demanded liberation of VEGF121 from fibrin implants induces local and controlled blood vessel growth. Circ Res 94 (2004) 1124-1132
    • (2004) Circ Res , vol.94 , pp. 1124-1132
    • Ehrbar, M.1    Djonov, V.G.2    Schnell, C.3    Tschanz, S.Z.4    Martiny-Baron, G.5    Schenk, U.6
  • 12
    • 0020553956 scopus 로고
    • Domain structure of human plasma fibronectin
    • Sekiguchi K., and Hakomori S.-I. Domain structure of human plasma fibronectin. J Biol Chem 258 (1983) 3967-3973
    • (1983) J Biol Chem , vol.258 , pp. 3967-3973
    • Sekiguchi, K.1    Hakomori, S.-I.2
  • 13
    • 0002490733 scopus 로고
    • Fibronectin domains and receptors
    • Mosher D.F. (Ed), Academic Press, San Diego, CA
    • Yamada K.M. Fibronectin domains and receptors. In: Mosher D.F. (Ed). Biology of extracellular matrix: series A. Fibronectin (1989), Academic Press, San Diego, CA 47-121
    • (1989) Biology of extracellular matrix: series A. Fibronectin , pp. 47-121
    • Yamada, K.M.1
  • 14
    • 0026569766 scopus 로고
    • Construction and characterization of a fusion protein with epidermal growth factor and the cell-binding domain of fibronectin
    • Kawase Y., Ohdate Y., Shimojo T., Taguchi Y., Kimizuka F., and Kato I. Construction and characterization of a fusion protein with epidermal growth factor and the cell-binding domain of fibronectin. FEBS Lett 298 (1992) 126-128
    • (1992) FEBS Lett , vol.298 , pp. 126-128
    • Kawase, Y.1    Ohdate, Y.2    Shimojo, T.3    Taguchi, Y.4    Kimizuka, F.5    Kato, I.6
  • 15
    • 0035045554 scopus 로고    scopus 로고
    • Production of a biologically active epidermal growth factor fusion protein with high collagen affinity
    • Ishikawa T., Terai H., and Kitajima T. Production of a biologically active epidermal growth factor fusion protein with high collagen affinity. J Biochem 129 (2001) 627-633
    • (2001) J Biochem , vol.129 , pp. 627-633
    • Ishikawa, T.1    Terai, H.2    Kitajima, T.3
  • 16
    • 33846567513 scopus 로고    scopus 로고
    • A fusion protein of hepatocyte growth factor for immobilization to collagen
    • Kitajima T., Terai H., and Ito Y. A fusion protein of hepatocyte growth factor for immobilization to collagen. Biomaterials 28 (2007) 1989-1997
    • (2007) Biomaterials , vol.28 , pp. 1989-1997
    • Kitajima, T.1    Terai, H.2    Ito, Y.3
  • 17
    • 0028177855 scopus 로고
    • 2-terminal fibrin-binding site of fibronectin is formed by interacting fourth and fifth finger domains. Studies with recombinant finger fragments expressed in Escherichia coli
    • 2-terminal fibrin-binding site of fibronectin is formed by interacting fourth and fifth finger domains. Studies with recombinant finger fragments expressed in Escherichia coli. J Biol Chem 269 (1994) 9539-9546
    • (1994) J Biol Chem , vol.269 , pp. 9539-9546
    • Matsuka, Y.V.1    Medved, L.V.2    Brew, S.A.3    Ingham, K.C.4
  • 19
    • 0033104923 scopus 로고    scopus 로고
    • Comparison of the fibrin-binding activities in the N- and C-termini of fibronectin
    • Rostagno A.A., Schwarzbauer J.E., and Gold L.I. Comparison of the fibrin-binding activities in the N- and C-termini of fibronectin. Biochem J 338 (1999) 375-386
    • (1999) Biochem J , vol.338 , pp. 375-386
    • Rostagno, A.A.1    Schwarzbauer, J.E.2    Gold, L.I.3
  • 20
    • 34548524413 scopus 로고    scopus 로고
    • Surface modification of plastic, glass and titanium by photoimmobilization of polyethylene glycol for antibiofouling
    • Ito Y., Hasuda H., Sakuragi M., and Tsuzuki S. Surface modification of plastic, glass and titanium by photoimmobilization of polyethylene glycol for antibiofouling. Acta Biomater 3 (2007) 1024-1032
    • (2007) Acta Biomater , vol.3 , pp. 1024-1032
    • Ito, Y.1    Hasuda, H.2    Sakuragi, M.3    Tsuzuki, S.4
  • 21
    • 2942516314 scopus 로고    scopus 로고
    • An in vitro outgrowth culture system for normal human keratinocytes
    • Ura H., Takeda F., and Okochi H. An in vitro outgrowth culture system for normal human keratinocytes. J Dermatol Sci 35 (2004) 19-28
    • (2004) J Dermatol Sci , vol.35 , pp. 19-28
    • Ura, H.1    Takeda, F.2    Okochi, H.3
  • 22
    • 0021003169 scopus 로고
    • Supplementary factors required for serum-free culture of rat kidney cells of line NRK-49F
    • Bradshaw G.L., and Dubes G.R. Supplementary factors required for serum-free culture of rat kidney cells of line NRK-49F. In Vitro 19 (1983) 735-742
    • (1983) In Vitro , vol.19 , pp. 735-742
    • Bradshaw, G.L.1    Dubes, G.R.2
  • 23
    • 0023624729 scopus 로고
    • Cell migration is essential for sustained growth of keratinocyte colonies: the roles of transforming growth factor-alpha and epidermal growth factor
    • Barrandon Y., and Green H. Cell migration is essential for sustained growth of keratinocyte colonies: the roles of transforming growth factor-alpha and epidermal growth factor. Cell 50 (1987) 1131-1137
    • (1987) Cell , vol.50 , pp. 1131-1137
    • Barrandon, Y.1    Green, H.2
  • 24
    • 0242406634 scopus 로고    scopus 로고
    • A novel role of fibrin in epidermal healing: plasminogen-mediated migration and selective detachment of differentiated keratinocytes
    • Geer D.J., and Andreadis S.T. A novel role of fibrin in epidermal healing: plasminogen-mediated migration and selective detachment of differentiated keratinocytes. J Invest Dermatol 121 (2003) 1210-1216
    • (2003) J Invest Dermatol , vol.121 , pp. 1210-1216
    • Geer, D.J.1    Andreadis, S.T.2
  • 25
    • 0344394522 scopus 로고    scopus 로고
    • Matrix-fibrinogen enhances wound closure by increasing both cell proliferation and migration
    • Rybarczyk B.J., Lawrence S.O., and Simpson-Haidaris P.J. Matrix-fibrinogen enhances wound closure by increasing both cell proliferation and migration. Blood 102 (2003) 4035-4043
    • (2003) Blood , vol.102 , pp. 4035-4043
    • Rybarczyk, B.J.1    Lawrence, S.O.2    Simpson-Haidaris, P.J.3
  • 26
    • 37149053488 scopus 로고    scopus 로고
    • Covalently immobilized biosignal molecule materials for tissue engineering
    • Ito Y. Covalently immobilized biosignal molecule materials for tissue engineering. Soft Matter 4 (2008) 46-56
    • (2008) Soft Matter , vol.4 , pp. 46-56
    • Ito, Y.1
  • 27
    • 43049153109 scopus 로고    scopus 로고
    • The use of N-terminal immobilization of PTH(1-34) on PLGA to enhance bioactivity
    • Sharon J.L., and Puleo D.L. The use of N-terminal immobilization of PTH(1-34) on PLGA to enhance bioactivity. Biomaterials 29 (2008) 3137-3142
    • (2008) Biomaterials , vol.29 , pp. 3137-3142
    • Sharon, J.L.1    Puleo, D.L.2
  • 28
    • 42949146918 scopus 로고    scopus 로고
    • Multivalency of sonic hedgehog conjugated to linear polymer chains modulates protein potency
    • Wall S.T., Saha K., Ashton R.S., Kam K.R., Schaffer D.V., and Healy K.E. Multivalency of sonic hedgehog conjugated to linear polymer chains modulates protein potency. Bioconjug Chem 19 (2008) 806-812
    • (2008) Bioconjug Chem , vol.19 , pp. 806-812
    • Wall, S.T.1    Saha, K.2    Ashton, R.S.3    Kam, K.R.4    Schaffer, D.V.5    Healy, K.E.6
  • 29
    • 33644997107 scopus 로고    scopus 로고
    • Construction of epidermal growth factor fusion protein with cell adhesive activity
    • Elloumi I., Kobayashi R., Funabashi H., Mie M., and Kobatake E. Construction of epidermal growth factor fusion protein with cell adhesive activity. Biomaterials 27 (2006) 3451-3458
    • (2006) Biomaterials , vol.27 , pp. 3451-3458
    • Elloumi, I.1    Kobayashi, R.2    Funabashi, H.3    Mie, M.4    Kobatake, E.5
  • 30
    • 0032499796 scopus 로고    scopus 로고
    • Collagen-binding growth factors: production and characterization of functional fusion proteins having a collagen-binding domain
    • Nishi N., Matsushita O., Yuube K., Miyanaka H., Okabe A., and Wada F. Collagen-binding growth factors: production and characterization of functional fusion proteins having a collagen-binding domain. Proc Natl Acad Sci USA 95 (1998) 7018-7023
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7018-7023
    • Nishi, N.1    Matsushita, O.2    Yuube, K.3    Miyanaka, H.4    Okabe, A.5    Wada, F.6
  • 31
    • 0034540910 scopus 로고    scopus 로고
    • Design, expression, and renaturation of a lesion-targeted recombinant epidermal growth factor-von Willebrand factor fusion protein: efficacy in an animal model of experimental colitis
    • Hall F.L., Kaiser A., Liu L., Chen Z.H., Hu J., Nimni M.E., et al. Design, expression, and renaturation of a lesion-targeted recombinant epidermal growth factor-von Willebrand factor fusion protein: efficacy in an animal model of experimental colitis. Int J Mol Med 6 (2000) 635-643
    • (2000) Int J Mol Med , vol.6 , pp. 635-643
    • Hall, F.L.1    Kaiser, A.2    Liu, L.3    Chen, Z.H.4    Hu, J.5    Nimni, M.E.6
  • 32
    • 0037331130 scopus 로고    scopus 로고
    • Delivery of a growth factor fusion protein having collagen-binding activity to wound tissues
    • Ishikawa T., Terai H., Yamamoto K., Harada K., and Kitajima T. Delivery of a growth factor fusion protein having collagen-binding activity to wound tissues. Artif Organs 27 (2003) 147-154
    • (2003) Artif Organs , vol.27 , pp. 147-154
    • Ishikawa, T.1    Terai, H.2    Yamamoto, K.3    Harada, K.4    Kitajima, T.5
  • 33
    • 15044342932 scopus 로고    scopus 로고
    • Responses of keratinocytes to substrate-bound vitronectin: growth factor complexes
    • Erratum in: Exp Cell Res 308:236-40
    • Hollier B., Harkin D.G., Leavesley D., and Upton Z. Responses of keratinocytes to substrate-bound vitronectin: growth factor complexes. Exp Cell Res 305 (2005) 221-232 Erratum in: Exp Cell Res 308:236-40
    • (2005) Exp Cell Res , vol.305 , pp. 221-232
    • Hollier, B.1    Harkin, D.G.2    Leavesley, D.3    Upton, Z.4
  • 34
    • 40849085396 scopus 로고    scopus 로고
    • Substrate-bound insulin-like growth factor (IGF)-I-IGF binding protein-vitronectin-stimulated breast cell migration is enhanced by coactivation of the phosphatidylinositide 3-kinase/AKT pathway by v-integrins and the IGF-I receptor
    • Hollier B.G., Kricker J.A., Van Lonkhuyzen D.R., Leavesley D.I., and Upton Z. Substrate-bound insulin-like growth factor (IGF)-I-IGF binding protein-vitronectin-stimulated breast cell migration is enhanced by coactivation of the phosphatidylinositide 3-kinase/AKT pathway by v-integrins and the IGF-I receptor. Endocrinology 149 (2008) 1075-1090
    • (2008) Endocrinology , vol.149 , pp. 1075-1090
    • Hollier, B.G.1    Kricker, J.A.2    Van Lonkhuyzen, D.R.3    Leavesley, D.I.4    Upton, Z.5
  • 35
    • 43749097878 scopus 로고    scopus 로고
    • Vitronectin: growth factor complexes hold potential as a wound therapy approach
    • Upton Z., Cuttle L., Noble A., Kempf M., Topping G., Malda J., et al. Vitronectin: growth factor complexes hold potential as a wound therapy approach. J Invest Dermatol 128 (2008) 1535-1544
    • (2008) J Invest Dermatol , vol.128 , pp. 1535-1544
    • Upton, Z.1    Cuttle, L.2    Noble, A.3    Kempf, M.4    Topping, G.5    Malda, J.6
  • 36
    • 33748761927 scopus 로고    scopus 로고
    • Three-dimensional culture for expansion and differentiation of mouse embryonic stem cells
    • Liu H., Collins S.F., and Suggs L.J. Three-dimensional culture for expansion and differentiation of mouse embryonic stem cells. Biomaterials 27 (2006) 6004-6014
    • (2006) Biomaterials , vol.27 , pp. 6004-6014
    • Liu, H.1    Collins, S.F.2    Suggs, L.J.3
  • 37
    • 33748775190 scopus 로고    scopus 로고
    • Optimization of fibrin scaffolds for differentiation of murine embryonic stem cells into neural lineage cells
    • Willerth S.M., Arendas K.J., Gottlieb D.I., and Sakiyama-Elbert S.E. Optimization of fibrin scaffolds for differentiation of murine embryonic stem cells into neural lineage cells. Biomaterials 27 (2006) 5990-6003
    • (2006) Biomaterials , vol.27 , pp. 5990-6003
    • Willerth, S.M.1    Arendas, K.J.2    Gottlieb, D.I.3    Sakiyama-Elbert, S.E.4
  • 38
    • 14944353409 scopus 로고    scopus 로고
    • A new method for manufacturing cardiac cell sheets using fibrin-coated dishes and its electrophysiological studies by optical mapping
    • Itabashi Y., Miyoshi S., Kawaguchi H., Yuasa S., Tanimoto K., Furuta A., et al. A new method for manufacturing cardiac cell sheets using fibrin-coated dishes and its electrophysiological studies by optical mapping. Artif Organs 29 (2005) 95-103
    • (2005) Artif Organs , vol.29 , pp. 95-103
    • Itabashi, Y.1    Miyoshi, S.2    Kawaguchi, H.3    Yuasa, S.4    Tanimoto, K.5    Furuta, A.6
  • 39
    • 0036897164 scopus 로고    scopus 로고
    • A novel approach to increase human islet cell mass while preserving beta-cell function
    • Beattie G.M., Montgomery A.M., Lopez A.D., Hao E., Perez B., Just M.L., et al. A novel approach to increase human islet cell mass while preserving beta-cell function. Diabetes 51 (2002) 3435-3439
    • (2002) Diabetes , vol.51 , pp. 3435-3439
    • Beattie, G.M.1    Montgomery, A.M.2    Lopez, A.D.3    Hao, E.4    Perez, B.5    Just, M.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.