메뉴 건너뛰기




Volumn 15, Issue 11, 2009, Pages 3589-3596

Collagen-binding human epidermal growth factor promotes cellularization of collagen scaffolds

Author keywords

[No Author keywords available]

Indexed keywords

BIOACTIVITY; BIOLOGICAL MATERIALS; CELL CULTURE; LEAKAGE (FLUID); PEPTIDES; SCAFFOLDS;

EID: 72649101231     PISSN: 19373341     EISSN: 1937335X     Source Type: Journal    
DOI: 10.1089/ten.tea.2008.0648     Document Type: Article
Times cited : (33)

References (31)
  • 1
    • 0022843166 scopus 로고
    • Nobel lecture. Epidermal growth factor
    • Cohen, S. Nobel lecture. Epidermal growth factor. Biosci Rep 6, 1017, 1986.
    • (1986) Biosci Rep , vol.6 , pp. 1017
    • Cohen, S.1
  • 2
    • 43749094998 scopus 로고    scopus 로고
    • The epidermal growth factor receptor system in skin repair and inflammation
    • Pastore, S., Mascia, F., Mariani, V., and Girolomoni, G. The epidermal growth factor receptor system in skin repair and inflammation. J Investig Dermatol 128, 1365, 2008.
    • (2008) J Investig Dermatol , vol.128 , pp. 1365
    • Pastore, S.1    Mascia, F.2    Mariani, V.3    Girolomoni, G.4
  • 3
    • 0025347672 scopus 로고
    • Prospects for epidermal growth factor in the management of corneal disorders
    • Tripathi, R.C., Raja, S.C., and Tripathi, B.J. Prospects for epidermal growth factor in the management of corneal disorders. Surv Ophthalmol 34, 457, 1990.
    • (1990) Surv Ophthalmol , vol.34 , pp. 457
    • Tripathi, R.C.1    Raja, S.C.2    Tripathi, B.J.3
  • 4
    • 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., Beart, R.W., Jr., and Gordon, E.M. 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, 635, 2000.
    • (2000) Int J Mol Med , vol.6 , pp. 635
    • Hall, F.L.1    Kaiser, A.2    Liu, L.3    Chen, Z.H.4    Hu, J.5    Nimni, M.E.6    Beart Jr., R.W.7    Gordon, E.M.8
  • 5
    • 0031926865 scopus 로고    scopus 로고
    • Cooperative interaction of autocrine and paracrine mitogens for airway epithelial cells
    • Kumar, R.K., Maronese, S.E., and Hassim, Z. Cooperative interaction of autocrine and paracrine mitogens for airway epithelial cells. Cell Biol Toxicol 14, 293, 1998.
    • (1998) Cell Biol Toxicol , vol.14 , pp. 293
    • Kumar, R.K.1    Maronese, S.E.2    Hassim, Z.3
  • 6
    • 45249103749 scopus 로고    scopus 로고
    • Epidermal growth factor therapy and wound healing-past, present and future perspectives
    • Hardwicke, J., Schmaljohann, D., Boyce, D., and Thomas, D. Epidermal growth factor therapy and wound healing-past, present and future perspectives. Surgeon 6, 172, 2008.
    • (2008) Surgeon , vol.6 , pp. 172
    • Hardwicke, J.1    Schmaljohann, D.2    Boyce, D.3    Thomas, D.4
  • 9
    • 0001413484 scopus 로고    scopus 로고
    • Interactions of cytokines, growth factors, and proteases in acute and chronic wounds
    • Mast, B.A., and Schultz, G.S. Interactions of cytokines, growth factors, and proteases in acute and chronic wounds. Wound Repair Regen 4, 411, 1996.
    • (1996) Wound Repair Regen , vol.4 , pp. 411
    • Mast, B.A.1    Schultz, G.S.2
  • 11
    • 0025905809 scopus 로고
    • EGF and TGF-alpha in wound healing and repair
    • Schultz, G., Rotatori, D.S., and Clark, W. EGF and TGF-alpha in wound healing and repair. J Cell Biochem 45, 346, 1991.
    • (1991) J Cell Biochem , vol.45 , pp. 346
    • Schultz, G.1    Rotatori, D.S.2    Clark, W.3
  • 12
    • 26444587113 scopus 로고    scopus 로고
    • Acceleration of wound healing by gelatin film dressings with epidermal growth factor
    • Tanaka, A., Nagate, T., and Matsuda, H. Acceleration of wound healing by gelatin film dressings with epidermal growth factor. J Vet Med Sci 67, 909, 2005.
    • (2005) J Vet Med Sci , vol.67 , pp. 909
    • Tanaka, A.1    Nagate, T.2    Matsuda, H.3
  • 13
    • 0035912971 scopus 로고    scopus 로고
    • Biomedical applications of collagen
    • Lee, C.H., Singla, A., and Lee, Y. Biomedical applications of collagen. Int J Pharm 221, 1, 2001.
    • (2001) Int J Pharm , vol.221 , pp. 1
    • Lee, C.H.1    Singla, A.2    Lee, Y.3
  • 14
    • 22044437561 scopus 로고    scopus 로고
    • Engineered skin substitutes: Practices and potentials
    • Supp, D.M., and Boyce, S.T. Engineered skin substitutes: practices and potentials. Clin Dermatol 23, 403, 2005.
    • (2005) Clin Dermatol , vol.23 , pp. 403
    • Supp, D.M.1    Boyce, S.T.2
  • 15
    • 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, 7018, 1998.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7018
    • Nishi, N.1    Matsushita, O.2    Yuube, K.3    Miyanaka, H.4    Okabe, A.5    Wada, F.6
  • 16
    • 0026751189 scopus 로고
    • Collagen binding site in collagenase can be determined using the concept of sense-antisense peptide interactions
    • de Souza, S.J., and Brentani, R. Collagen binding site in collagenase can be determined using the concept of sense-antisense peptide interactions. J Biol Chem 267, 13763, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 13763
    • De Souza, S.J.1    Brentani, R.2
  • 17
    • 33846301419 scopus 로고    scopus 로고
    • Activation of demineralized bone matrix by genetically engineered human bone morphogenetic protein-2 with a collagen binding domain derived from von Willebrand factor propolypeptide
    • Chen, B., Lin, H., Zhao, Y., Wang, B., Liu, Y., Liu, Z., and Dai, J. Activation of demineralized bone matrix by genetically engineered human bone morphogenetic protein-2 with a collagen binding domain derived from von Willebrand factor propolypeptide. J Biomed Mater Res A 80, 428, 2007.
    • (2007) J Biomed Mater Res A , vol.80 , pp. 428
    • Chen, B.1    Lin, H.2    Zhao, Y.3    Wang, B.4    Liu, Y.5    Liu, Z.6    Dai, J.7
  • 18
    • 33748080132 scopus 로고    scopus 로고
    • The effect of collagen-targeting platelet-derived growth factor on cellularization and vascularization of collagen scaffolds
    • Lin, H., Chen, B., Sun, W., Zhao, W., Zhao, Y., and Dai, J. The effect of collagen-targeting platelet-derived growth factor on cellularization and vascularization of collagen scaffolds. Biomaterials 27, 5708, 2006.
    • (2006) Biomaterials , vol.27 , pp. 5708
    • Lin, H.1    Chen, B.2    Sun, W.3    Zhao, W.4    Zhao, Y.5    Dai, J.6
  • 20
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248, 1976.
    • (1976) Anal Biochem , vol.72 , pp. 248
    • Bradford, M.M.1
  • 21
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H., and von Jagow, G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166, 368, 1987.
    • (1987) Anal Biochem , vol.166 , pp. 368
    • Schagger, H.1    Von Jagow, G.2
  • 22
    • 0017123728 scopus 로고
    • Induction of human fibroblast proliferation by epidermal growth factor (EGF): Enhancement by an EGF-binding arginine esterase and by ascorbate
    • Lembach, K.J. Induction of human fibroblast proliferation by epidermal growth factor (EGF): enhancement by an EGF-binding arginine esterase and by ascorbate. Proc Natl Acad Sci USA 73, 183, 1976.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 183
    • Lembach, K.J.1
  • 23
    • 0030930661 scopus 로고    scopus 로고
    • Microfibril-associated gly-coprotein-1 (MAGP-1) binds to the pepsin-resistant domain of the alpha3(VI) chain of type VI collagen
    • Finnis, M.L., and Gibson, M.A. Microfibril-associated gly-coprotein-1 (MAGP-1) binds to the pepsin-resistant domain of the alpha3(VI) chain of type VI collagen. J Biol Chem 272, 22817, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 22817
    • Finnis, M.L.1    Gibson, M.A.2
  • 24
    • 0019215155 scopus 로고
    • The molecular organization of collagen and its role in determining the biophysical properties of the connective tissues
    • Nimni, M.E. The molecular organization of collagen and its role in determining the biophysical properties of the connective tissues. Biorheology 17, 51, 1980.
    • (1980) Biorheology , vol.17 , pp. 51
    • Nimni, M.E.1
  • 25
    • 0032488998 scopus 로고    scopus 로고
    • A study of the collagen-binding domain of a 116-kDa Clostridium histolyticum collagenase
    • Matsushita, O., Jung, C.M., Minami, J., Katayama, S., Nishi, N., and Okabe, A. A study of the collagen-binding domain of a 116-kDa Clostridium histolyticum collagenase. J Biol Chem 273, 3643, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 3643
    • Matsushita, O.1    Jung, C.M.2    Minami, J.3    Katayama, S.4    Nishi, N.5    Okabe, A.6
  • 28
    • 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, 627, 2001.
    • (2001) J Biochem , vol.129 , pp. 627
    • Ishikawa, T.1    Terai, H.2    Kitajima, T.3
  • 29
    • 0037331130 scopus 로고    scopus 로고
    • Delivery of a growth factor fusion protein having collagen-binding activity to wound tissues
    • Ishikawa, T., Terai, H., Yamamoto, T., Harada, K., and Kitajima, T. Delivery of a growth factor fusion protein having collagen-binding activity to wound tissues. Artif Organs 27, 147, 2003.
    • (2003) Artif Organs , vol.27 , pp. 147
    • Ishikawa, T.1    Terai, H.2    Yamamoto, T.3    Harada, K.4    Kitajima, T.5
  • 30
    • 17644418377 scopus 로고    scopus 로고
    • The FAXWXXT motif in the carboxyl terminus of Vibrio mimicus metalloprotease is involved in binding to collagen
    • Lee, J.H., Ahn, S.H., Lee, E.M., Jeong, S.H., Kim, Y.O., Lee, S.J., and Kong, I.S. The FAXWXXT motif in the carboxyl terminus of Vibrio mimicus metalloprotease is involved in binding to collagen. FEBS Lett 579, 2507, 2005.
    • (2005) FEBS Lett , vol.579 , pp. 2507
    • Lee, J.H.1    Ahn, S.H.2    Lee, E.M.3    Jeong, S.H.4    Kim, Y.O.5    Lee, S.J.6    Kong, I.S.7
  • 31
    • 58149197766 scopus 로고    scopus 로고
    • Expression of a fusion protein containing human epidermal growth factor and the collagen-binding domain of Vibrio mimicus metalloprotease
    • Kim, D.G., Min, M.K., Ahn, S.C., Kim, J.K., and Kong, I.S. Expression of a fusion protein containing human epidermal growth factor and the collagen-binding domain of Vibrio mimicus metalloprotease. Biotechnol Lett 31, 259, 2009
    • (2009) Biotechnol Lett , vol.31 , pp. 259
    • Kim, D.G.1    Min, M.K.2    Ahn, S.C.3    Kim, J.K.4    Kong, I.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.