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Volumn 136, Issue 5, 2004, Pages 643-649

Design, expression and characterization of collagen-like proteins based on the cell adhesive and crosslinking sequences derived from native collagens

Author keywords

Cell adhesion; Collagen; Cross linking; Genetic engineering; Recombinant protein

Indexed keywords

COLLAGEN; COLLAGEN LIKE PROTEIN; COLLAGEN TYPE 1; COLLAGEN TYPE 3; GLYCYLPROLYLPROLYLGLYCYLPROLYLCYSTEINYLCYTEINYLGLYCYLGLYCYLGLYCINE; PROTEIN; UNCLASSIFIED DRUG;

EID: 14944361263     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvh172     Document Type: Article
Times cited : (36)

References (38)
  • 1
    • 0035912971 scopus 로고    scopus 로고
    • Biomedical applications of collagen
    • Lee, C.H., Singla, A., and Lee, Y. (2001) Biomedical applications of collagen. Int. J. Pharm. 221, 1-22
    • (2001) Int. J. Pharm. , vol.221 , pp. 1-22
    • Lee, C.H.1    Singla, A.2    Lee, Y.3
  • 2
    • 0037131510 scopus 로고    scopus 로고
    • Genetic engineering of fibrous proteins: Spider dragline silk and collagen
    • Wong Po Foo, C. and Kaplan, D.L. (2002) Genetic engineering of fibrous proteins: Spider dragline silk and collagen. Adv. Drug Delivery Rev. 54, 1131-1143
    • (2002) Adv. Drug Delivery Rev. , vol.54 , pp. 1131-1143
    • Wong Po Foo, C.1    Kaplan, D.L.2
  • 3
    • 0021338291 scopus 로고
    • The immunogenicity of injectable collagen. I. A 1-year prospective study
    • Cooperman, L. and Michaeli, D. (1984) The immunogenicity of injectable collagen. I. A 1-year prospective study. J. Amer. Acad. Dermatol. 10, 638-646
    • (1984) J. Amer. Acad. Dermatol. , vol.10 , pp. 638-646
    • Cooperman, L.1    Michaeli, D.2
  • 4
    • 0034830878 scopus 로고    scopus 로고
    • Complete primary structure of rainbow trout type I collagen of 1 (I) 2 (I) 3 (I) heterotrimers
    • Saito, M., Takenouchi, Y., Kunisaki, N., and Kimura, S. (2001) Complete primary structure of rainbow trout type I collagen of 1 (I) 2 (I) 3 (I) heterotrimers. Eur. J. Biochem. 268, 2817-2827
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2817-2827
    • Saito, M.1    Takenouchi, Y.2    Kunisaki, N.3    Kimura, S.4
  • 5
    • 0034607263 scopus 로고    scopus 로고
    • Sequence-specific liquid crystallinity of collagen model peptides. I. Transmission electron microscopy studies of interfacial collagen gels
    • Valluzzi, R. and Kaplan, D.L. (2000) Sequence-specific liquid crystallinity of collagen model peptides. I. Transmission electron microscopy studies of interfacial collagen gels. Biopolymers 53, 350-362
    • (2000) Biopolymers , vol.53 , pp. 350-362
    • Valluzzi, R.1    Kaplan, D.L.2
  • 6
    • 0002565653 scopus 로고
    • Cartilage-specific collagens: Structural studies
    • (Kuettner, K.E., Schleyrenbach, R., Peyron, J.G., and Hascall, V.C., eds.) Raven Press, New York
    • Eyre, D.R., Wu, J.J., and Woods, P. (1992) Cartilage-specific collagens: structural studies in Articular Cartilage and Osteoarthritis (Kuettner, K.E., Schleyrenbach, R., Peyron, J.G., and Hascall, V.C., eds.) pp. 119-131, Raven Press, New York
    • (1992) Articular Cartilage and Osteoarthritis , pp. 119-131
    • Eyre, D.R.1    Wu, J.J.2    Woods, P.3
  • 7
    • 0040358808 scopus 로고    scopus 로고
    • 15GPCCG forms pH-dependent covalently linked triple helical trimers
    • 15GPCCG forms pH-dependent covalently linked triple helical trimers. J. Biol. Chem. 275, 14532-14536
    • (2000) J. Biol. Chem. , vol.275 , pp. 14532-14536
    • Mechling, D.E.1    Bächinger, H.P.2
  • 8
    • 0027717709 scopus 로고
    • Molecular mechanisms of neural crest cell attachment and migration on types I and IV collagen
    • Perris, R., Syfrig, J., Paulsson, M., and Bronner-Fraser, M. (1993) Molecular mechanisms of neural crest cell attachment and migration on types I and IV collagen. J. Cell Sci. 106, 1357-1368
    • (1993) J. Cell Sci. , vol.106 , pp. 1357-1368
    • Perris, R.1    Syfrig, J.2    Paulsson, M.3    Bronner-Fraser, M.4
  • 9
    • 0029098293 scopus 로고
    • Cytokines modulate phagocytosis and intracellular digestion of collagen fibrils by fibroblasts in rabbit periosteal explants. Inverse effects on procollagenase production and collagen phagocytosis
    • van der Zee, E., Everts, V., Hoeben, K., and Beertsen W. (1995) Cytokines modulate phagocytosis and intracellular digestion of collagen fibrils by fibroblasts in rabbit periosteal explants. Inverse effects on procollagenase production and collagen phagocytosis. J. Cell Sci. 108, 3307-3315
    • (1995) J. Cell Sci. , vol.108 , pp. 3307-3315
    • Van Der Zee, E.1    Everts, V.2    Hoeben, K.3    Beertsen, W.4
  • 10
    • 0025264295 scopus 로고
    • The alpha 2 beta 1 integrin cell surface collagen receptor binds to the alpha 1 (I)-CB3 peptide of collagen
    • Staatz, W.D., Walsh, J.J., Pexton, T., and Santoro, S.A. (1990) The alpha 2 beta 1 integrin cell surface collagen receptor binds to the alpha 1 (I)-CB3 peptide of collagen. J. Biol. Chem. 265, 4778-4781
    • (1990) J. Biol. Chem. , vol.265 , pp. 4778-4781
    • Staatz, W.D.1    Walsh, J.J.2    Pexton, T.3    Santoro, S.A.4
  • 11
    • 0027189862 scopus 로고
    • Integrin and Arg-Gly-Asp dependence of cell adhesion to the native and unfolded triple helix of collagen type VI
    • Pfaff, M., Aumailley, M., Specks, U., Knolle, J., Hans Zerwes, G., and Timpl R. (1993) Integrin and Arg-Gly-Asp dependence of cell adhesion to the native and unfolded triple helix of collagen type VI. Exp. Cell Res. 206, 167-176
    • (1993) Exp. Cell Res. , vol.206 , pp. 167-176
    • Pfaff, M.1    Aumailley, M.2    Specks, U.3    Knolle, J.4    Hans Zerwes, G.5    Timpl, R.6
  • 12
    • 0025872761 scopus 로고
    • Sequence specific thermal stability of the collagen triple helix
    • Bächinger, H.P. and Davis, J.M. (1991) Sequence specific thermal stability of the collagen triple helix. Int. J. Biol. Macromol. 13, 152-156
    • (1991) Int. J. Biol. Macromol. , vol.13 , pp. 152-156
    • Bächinger, H.P.1    Davis, J.M.2
  • 14
    • 0042733495 scopus 로고    scopus 로고
    • Angiogenesis in collagen I requires α2β1 ligation of a GFP*GER sequence and possibly p38 MAPK activation and focal adhesion disassembly
    • Sweeney, S.M., DiLullo, G., Slater, S.J., Martinez, J., Iozzo, R.V., Lauer-Fields, J.L., Fields, G.B., and San Antonio JD. (2003) Angiogenesis in collagen I requires α2β1 ligation of a GFP*GER sequence and possibly p38 MAPK activation and focal adhesion disassembly. J. Biol. Chem. 278, 30516-30524
    • (2003) J. Biol. Chem. , vol.278 , pp. 30516-30524
    • Sweeney, S.M.1    DiLullo, G.2    Slater, S.J.3    Martinez, J.4    Iozzo, R.V.5    Lauer-Fields, J.L.6    Fields, G.B.7    San Antonio, J.D.8
  • 15
    • 17544375225 scopus 로고    scopus 로고
    • Promotion of fibroblast adhesion by triple-helical peptide models of type I collagen-derived sequences
    • Grab, B., Miles, A.J., Furcht, L.T., and Fields, G.B. (1996) Promotion of fibroblast adhesion by triple-helical peptide models of type I collagen-derived sequences. J. Biol. Chem. 271, 12234-12240
    • (1996) J. Biol. Chem. , vol.271 , pp. 12234-12240
    • Grab, B.1    Miles, A.J.2    Furcht, L.T.3    Fields, G.B.4
  • 16
    • 0018400235 scopus 로고
    • Chain conformation in the collagen molecule
    • Fraser, R.D.B., MacRae, T.P., and Suzuki, E. (1979) Chain conformation in the collagen molecule. J. Mol. Biol. 129, 463-481
    • (1979) J. Mol. Biol. , vol.129 , pp. 463-481
    • Fraser, R.D.B.1    MacRae, T.P.2    Suzuki, E.3
  • 17
    • 84985666220 scopus 로고
    • Evidence for the role of 4-hydroxyproline localized in the third position of the triplet (Gly-XY) in adaptational changes of thermostability of a collagen molecule and collagen fibrils
    • Burjanadze, T.V. (1982) Evidence for the role of 4-hydroxyproline localized in the third position of the triplet (Gly-XY) in adaptational changes of thermostability of a collagen molecule and collagen fibrils. Biopolymers 21, 1489-1501
    • (1982) Biopolymers , vol.21 , pp. 1489-1501
    • Burjanadze, T.V.1
  • 18
    • 0036290657 scopus 로고    scopus 로고
    • Nucleation and propagation of the collagen triple helix in single-chain and trimerized peptides: Transition from third to first order kinetics
    • Boudko, S., Frank, S., Kammerer, R.A., Stetefeld, J., Schulthess, T., Landwehr, R., Lustig, A., Bachinger, H.P., and Engel, J. (2002) Nucleation and propagation of the collagen triple helix in single-chain and trimerized peptides: Transition from third to first order kinetics. J. Mol. Biol. 317, 459-470
    • (2002) J. Mol. Biol. , vol.317 , pp. 459-470
    • Boudko, S.1    Frank, S.2    Kammerer, R.A.3    Stetefeld, J.4    Schulthess, T.5    Landwehr, R.6    Lustig, A.7    Bachinger, H.P.8    Engel, J.9
  • 20
    • 0037287423 scopus 로고    scopus 로고
    • Synthesis and structural characterization of silk-like materials incorporated with elastic motif
    • Yao, J. and Asakura, T. (2003) Synthesis and structural characterization of silk-like materials incorporated with elastic motif. J. Biochem. 133, 147-154
    • (2003) J. Biochem. , vol.133 , pp. 147-154
    • Yao, J.1    Asakura, T.2
  • 21
    • 0242320979 scopus 로고    scopus 로고
    • Production and characterization of a silk-like hybrid protein, based on the polyalanine region of Samia cynthia ricini silk fibroin and a cell adhesive region derived from fibronectin
    • Asakura, T., Tanaka, C., Yang, M., Yao, J., and Kurokawa, M. (2004) Production and characterization of a silk-like hybrid protein, based on the polyalanine region of Samia cynthia ricini silk fibroin and a cell adhesive region derived from fibronectin. Biomaterials 25, 617-624
    • (2004) Biomaterials , vol.25 , pp. 617-624
    • Asakura, T.1    Tanaka, C.2    Yang, M.3    Yao, J.4    Kurokawa, M.5
  • 23
    • 0028474211 scopus 로고
    • Fibroblast growth on polymer surfaces and biosynthesis of collagen
    • Tamada, Y. and Ikada, Y. (1994) Fibroblast growth on polymer surfaces and biosynthesis of collagen. J. Biomed. Mater. Res. 28, 783-789
    • (1994) J. Biomed. Mater. Res. , vol.28 , pp. 783-789
    • Tamada, Y.1    Ikada, Y.2
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • Pierschbacher, M.D. and Ruoslahti, E. (1984) Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 309, 30-33
    • (1984) Nature , vol.309 , pp. 30-33
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 28
    • 0022133419 scopus 로고
    • Complete amino acid sequence of human vitronectin deduced from cDNA. Similarity of cell attachment sites in vitronectin and fibronectin
    • Suzuki, S., Oldberg, A., Hayman, E.G., Pierschbacher, M.D., and Ruoslahti, E. (1985) Complete amino acid sequence of human vitronectin deduced from cDNA. Similarity of cell attachment sites in vitronectin and fibronectin. EMBO J. 4, 2519-2524
    • (1985) EMBO J. , vol.4 , pp. 2519-2524
    • Suzuki, S.1    Oldberg, A.2    Hayman, E.G.3    Pierschbacher, M.D.4    Ruoslahti, E.5
  • 29
    • 0018567093 scopus 로고
    • Amino acid sequence studies on the alpha chain of human fibrinogen. Overlapping sequences providing the complete sequence
    • Watt, K.W., Cottrell, B.A., Strong, D.D., and Doolittle, R.F. (1979) Amino acid sequence studies on the alpha chain of human fibrinogen. Overlapping sequences providing the complete sequence. Biochemistry 18, 5410-5416
    • (1979) Biochemistry , vol.18 , pp. 5410-5416
    • Watt, K.W.1    Cottrell, B.A.2    Strong, D.D.3    Doolittle, R.F.4
  • 30
    • 0025115315 scopus 로고
    • Serum enhancement of human endothelial cell attachment to and spreading on collagens I and IV does not require serum fibronectin or vitronectin
    • Norris, W.D., Steele, J.G., Johnson, G., and Underwood, P.A. (1990) Serum enhancement of human endothelial cell attachment to and spreading on collagens I and IV does not require serum fibronectin or vitronectin. J. Cell Sci. 95, 255-262
    • (1990) J. Cell Sci. , vol.95 , pp. 255-262
    • Norris, W.D.1    Steele, J.G.2    Johnson, G.3    Underwood, P.A.4
  • 32
    • 0026333465 scopus 로고
    • A model for interstitial collagen catabolism by mammalian collagenases
    • Fields, G.B. (1991) A model for interstitial collagen catabolism by mammalian collagenases. J. Theor. Biol. 153, 585-602
    • (1991) J. Theor. Biol. , vol.153 , pp. 585-602
    • Fields, G.B.1
  • 33
    • 0028227278 scopus 로고
    • Promotion of human platelet adhesion and aggregation by a synthetic, triple-helical "mini-collagen"
    • Rao, G.H., Fields, C.G., White, J.G., and Fields, G.B. (1994) Promotion of human platelet adhesion and aggregation by a synthetic, triple-helical "mini-collagen". J. Biol. Chem. 269, 13899-13903
    • (1994) J. Biol. Chem. , vol.269 , pp. 13899-13903
    • Rao, G.H.1    Fields, C.G.2    White, J.G.3    Fields, G.B.4
  • 35
    • 0030732364 scopus 로고    scopus 로고
    • Assembly of human prolyl 4-hydroxylase and type III collagen in the yeast Pichia pastoris: Formation of a stable enzyme tetramer requires coexpression with collagen and assembly of a stable collagen requires coexpression with prolyl 4-hydroxylase
    • Vuorela, A., Myllyharju, J., Nissi, R., Pihlajaniemi, T., and Kivirikko, K.I. (1997) Assembly of human prolyl 4-hydroxylase and type III collagen in the yeast Pichia pastoris: formation of a stable enzyme tetramer requires coexpression with collagen and assembly of a stable collagen requires coexpression with prolyl 4-hydroxylase. EMBO J. 16, 6702-6712
    • (1997) EMBO J. , vol.16 , pp. 6702-6712
    • Vuorela, A.1    Myllyharju, J.2    Nissi, R.3    Pihlajaniemi, T.4    Kivirikko, K.I.5
  • 38
    • 0033662393 scopus 로고    scopus 로고
    • Functional analysis of bone sialoprotein: Identification of the hydroxyapatite-nucleating and cell-binding domains by recombinant peptide expression and site-directed mutagenesis
    • Harris, N.L., Rattray, K.R., Tye, C.E., Underbill, T.M., Somerman, M.J., D'Errico, J.A., Chambers, A.F., Hunter, O.K., and Goldberg, H.A. (2000) Functional analysis of bone sialoprotein: identification of the hydroxyapatite-nucleating and cell-binding domains by recombinant peptide expression and site-directed mutagenesis. Bone 27, 795-802
    • (2000) Bone , vol.27 , pp. 795-802
    • Harris, N.L.1    Rattray, K.R.2    Tye, C.E.3    Underbill, T.M.4    Somerman, M.J.5    D'Errico, J.A.6    Chambers, A.F.7    Hunter, O.K.8    Goldberg, H.A.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.