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Volumn 17, Issue 4, 1999, Pages 385-389

Expression of an engineered form of recombinant procollagen in mouse milk

Author keywords

Protein engineering; Recombinant procollagen; Transgenic animals

Indexed keywords

COMPLEMENTARY DNA; PROCOLLAGEN; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; RECOMBINANT PROTEIN;

EID: 0032892683     PISSN: 10870156     EISSN: None     Source Type: Journal    
DOI: 10.1038/7945     Document Type: Article
Times cited : (82)

References (32)
  • 1
    • 0029176870 scopus 로고
    • Extracellular matrix 1: Fibril-forming collagens
    • Kadler, K.E. Extracellular matrix 1: fibril-forming collagens. Protein Profile 2, 491-619 (1995).
    • (1995) Protein Profile , vol.2 , pp. 491-619
    • Kadler, K.E.1
  • 2
    • 0029006974 scopus 로고
    • Collagens: Molecular biology, diseases and potential for therapy
    • Prockop, D.J. & Kivirikko, K.I. Collagens: molecular biology, diseases and potential for therapy. Ann. Rev. Biochem. 64, 403-434 (1995).
    • (1995) Ann. Rev. Biochem. , vol.64 , pp. 403-434
    • Prockop, D.J.1    Kivirikko, K.I.2
  • 4
    • 0015624009 scopus 로고
    • The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilising the triple helix of collagen
    • Berg, R.A. & Prockop, D.J. The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilising the triple helix of collagen. Biochem. Biophys. Res. Comrmn. 52, 115-120 (1973).
    • (1973) Biochem. Biophys. Res. Comrmn. , vol.52 , pp. 115-120
    • Berg, R.A.1    Prockop, D.J.2
  • 5
    • 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 co-expression with collagen and assembly of a stable collagen requires co-expression with prolyl 4-hydroxylase
    • Vuorela, A., Myllyharju, J., Nissi, R., Pihlajaniemi, T. & Kivirikko, K.I. Assembly of human prolyl 4-hydroxylase and type III collagen in the yeast Pichia pastoris: formation of a stable enzyme tetramer requires co-expression with collagen and assembly of a stable collagen requires co-expression with prolyl 4-hydroxylase. EMBO J. 18, 6702-6712 (1997).
    • (1997) EMBO J. , vol.18 , pp. 6702-6712
    • Vuorela, A.1    Myllyharju, J.2    Nissi, R.3    Pihlajaniemi, T.4    Kivirikko, K.I.5
  • 6
    • 0028137729 scopus 로고
    • Synthesis of recombinant human procollagen II in a stably transfected tumour cell line (HT1080)
    • Fertala, A. et al. Synthesis of recombinant human procollagen II in a stably transfected tumour cell line (HT1080). Biochem. J. 298, 31-37 (1994).
    • (1994) Biochem. J. , vol.298 , pp. 31-37
    • Fertala, A.1
  • 7
    • 0030613853 scopus 로고    scopus 로고
    • Human recombinant α1(V) collagen chain - Homotrimeric assembly and subsequent processing
    • Fichard, A., Tillet, E., Delacoux, F., Garrone, R. & Ruggiero, F. Human recombinant α1(V) collagen chain - homotrimeric assembly and subsequent processing. J. Biol. Chem. 272, 30083-30087 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 30083-30087
    • Fichard, A.1    Tillet, E.2    Delacoux, F.3    Garrone, R.4    Ruggiero, F.5
  • 8
    • 0030931450 scopus 로고    scopus 로고
    • A cDNA cassette system for the synthesis of recombinant procollagens. Variants of procollagen II lacking a D-period are secreted as triple-helical monomers
    • Arnold, W.V. et al. A cDNA cassette system for the synthesis of recombinant procollagens. Variants of procollagen II lacking a D-period are secreted as triple-helical monomers. Matrix Biol. 16, 105-116 (1997).
    • (1997) Matrix Biol. , vol.16 , pp. 105-116
    • Arnold, W.V.1
  • 9
    • 0026725853 scopus 로고
    • Characterization of the human prolyl 4-hydroxylase tetramer and its multifunctional protein disulphide isomerase subunit synthesized in a baculovirus expression system
    • Vuori, K., Pihlajaniemi, T., Marttila, M. & Kivirikko, K.I. Characterization of the human prolyl 4-hydroxylase tetramer and its multifunctional protein disulphide isomerase subunit synthesized in a baculovirus expression system. Proc. Natl. Acad. Sci. USA 89, 7467-7470 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7467-7470
    • Vuori, K.1    Pihlajaniemi, T.2    Marttila, M.3    Kivirikko, K.I.4
  • 10
    • 0029940986 scopus 로고    scopus 로고
    • Characterization of human type III collagen expressed in a baculovirus system - Production of a protein with a stable triple helix requires coexpression with the two types of recombinant prolyl 4-hydroxylase subunit
    • Lamberg, A. et al. Characterization of human type III collagen expressed in a baculovirus system - production of a protein with a stable triple helix requires coexpression with the two types of recombinant prolyl 4-hydroxylase subunit. J. Biol. Chem. 271, 11988-11995 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 11988-11995
    • Lamberg, A.1
  • 11
    • 0031606150 scopus 로고    scopus 로고
    • Production of therapeutic proteins in the milk of transgenic livestock
    • Colman, A. Production of therapeutic proteins in the milk of transgenic livestock. Biochemical Society Symp. 63, 141-147 (1998).
    • (1998) Biochemical Society Symp. , vol.63 , pp. 141-147
    • Colman, A.1
  • 12
    • 0027521818 scopus 로고
    • Transgenic livestock as bioreactors - Stable expression of human alpha-1-antitrypsin by a flock of sheep
    • Carver, A.S. et al. Transgenic livestock as bioreactors - stable expression of human alpha-1-antitrypsin by a flock of sheep. Bio/Technology 11, 1263-1270 (1993).
    • (1993) Bio/Technology , vol.11 , pp. 1263-1270
    • Carver, A.S.1
  • 13
    • 0029895384 scopus 로고    scopus 로고
    • High level expression of recombinant human fibrinogen in the milk of transgenic mice
    • Prunkard, D. et al. High level expression of recombinant human fibrinogen in the milk of transgenic mice. Nat. Biotechnol. 14, 867-871 (1996).
    • (1996) Nat. Biotechnol. , vol.14 , pp. 867-871
    • Prunkard, D.1
  • 14
    • 0030970789 scopus 로고    scopus 로고
    • Secretion of unprocessed human surfactant protein B in milk of transgenic mice
    • Yarus, S. et al. Secretion of unprocessed human surfactant protein B in milk of transgenic mice. Transgenic Res. 6, 51-57 (1997).
    • (1997) Transgenic Res. , vol.6 , pp. 51-57
    • Yarus, S.1
  • 15
    • 0031193334 scopus 로고    scopus 로고
    • Recombinant human extracellular superoxide dismutase produced in milk of transgenic rabbits
    • Stromqvist, M. et al. Recombinant human extracellular superoxide dismutase produced in milk of transgenic rabbits. Transgenic Res. 6, 271-278 (1997).
    • (1997) Transgenic Res. , vol.6 , pp. 271-278
    • Stromqvist, M.1
  • 16
    • 0030771837 scopus 로고    scopus 로고
    • Transgenic pigs produce functional human factor VIII in milk
    • Paleyanda, R.K. et al. Transgenic pigs produce functional human factor VIII in milk. Nat. Biotechnol. 15, 971-975 (1997).
    • (1997) Nat. Biotechnol. , vol.15 , pp. 971-975
    • Paleyanda, R.K.1
  • 17
    • 0030225322 scopus 로고    scopus 로고
    • Affinity purification of biologically active and inactive forms of recombinant human protein C produced in porcine mammary gland
    • Van-Cott, K.E. et al. Affinity purification of biologically active and inactive forms of recombinant human protein C produced in porcine mammary gland. J Mol Recognit. 9, 407-414 (1996).
    • (1996) J Mol Recognit. , vol.9 , pp. 407-414
    • Van-Cott, K.E.1
  • 18
    • 2642705886 scopus 로고    scopus 로고
    • Human factor IX transgenic sheep produced by transfer of nuclei from transfected fetal fibroblasts
    • Schnieke, A.E. et al. 1997. Human factor IX transgenic sheep produced by transfer of nuclei from transfected fetal fibroblasts. Science 278, 2130-2133.
    • (1997) Science , vol.278 , pp. 2130-2133
    • Schnieke, A.E.1
  • 19
    • 0031055069 scopus 로고    scopus 로고
    • Identification of the molecular recognition sequence which determines the type-specific assembly of procollagen
    • Lees, J.F., Tasab, M. & Bulleid. N.J. Identification of the molecular recognition sequence which determines the type-specific assembly of procollagen. EMBO J. 16, 908-916 (1997).
    • (1997) EMBO J. , vol.16 , pp. 908-916
    • Lees, J.F.1    Tasab, M.2    Bulleid, N.J.3
  • 20
    • 0019880195 scopus 로고
    • Proteolytic enzymes as probes for the triple-helical conformation of procollagen
    • Bruckner, P. & Prockop. D.J. Proteolytic enzymes as probes for the triple-helical conformation of procollagen. Anal. Biochem. 110, 360-368 (1981).
    • (1981) Anal. Biochem. , vol.110 , pp. 360-368
    • Bruckner, P.1    Prockop, D.J.2
  • 21
    • 0015624009 scopus 로고
    • The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen
    • Berg, R.A. & Prockop, D.J. The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen. Biochem. Biophys. Res. Commun. 52, 115-119 (1973).
    • (1973) Biochem. Biophys. Res. Commun. , vol.52 , pp. 115-119
    • Berg, R.A.1    Prockop, D.J.2
  • 22
    • 0029893377 scopus 로고    scopus 로고
    • Type III procollagen assembly in semi-intact cells: Chain association, nucleation and triple-helix folding do not require formation of inter-chain disuiphide bonds but triple-helix nucleation does require hydroxylation
    • Bulleid, N.J., Wilson, R. & Lees, J.F. Type III procollagen assembly in semi-intact cells: chain association, nucleation and triple-helix folding do not require formation of inter-chain disuiphide bonds but triple-helix nucleation does require hydroxylation. Biochem J. 317, 195-202 (1996).
    • (1996) Biochem J. , vol.317 , pp. 195-202
    • Bulleid, N.J.1    Wilson, R.2    Lees, J.F.3
  • 23
    • 0023815508 scopus 로고    scopus 로고
    • Cleavage of type-I and type-II procollagens by type-I/II procollagen N-proteinase - Correlation of kinetic constants with the predicted conformations of procollagen substrates
    • Dombrowski, K.E. & Prockop, D.J. Cleavage of type-I and type-II procollagens by type-I/II procollagen N-proteinase - correlation of kinetic constants with the predicted conformations of procollagen substrates. J Biol. Chem. 263, 16545-16552 (1998).
    • (1998) J Biol. Chem. , vol.263 , pp. 16545-16552
    • Dombrowski, K.E.1    Prockop, D.J.2
  • 25
  • 26
    • 0027967277 scopus 로고
    • The role of cysteine residues in the folding and association of the COOH-terminal propeptide of types I and II procollagen
    • Lees, J.F. & Bulleid, N.J. The role of cysteine residues in the folding and association of the COOH-terminal propeptide of types I and II procollagen. J. Biol. Chem. 269, 24354-24360 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 24354-24360
    • Lees, J.F.1    Bulleid, N.J.2
  • 28
    • 0027415488 scopus 로고
    • Cell-free synthesis and assembly of prolyl 4-hydroxylase; the role of the β-subunit (PDI) in preventing misfolding and aggregation of the α-subunit
    • John, D.C.A., Grant, M.E. & Bulleid, N.J. Cell-free synthesis and assembly of prolyl 4-hydroxylase; the role of the β-subunit (PDI) in preventing misfolding and aggregation of the α-subunit. EMBO J. 12, 1587-1595 (1993).
    • (1993) EMBO J. , vol.12 , pp. 1587-1595
    • John, D.C.A.1    Grant, M.E.2    Bulleid, N.J.3
  • 30
    • 0020010851 scopus 로고
    • Preparation and characterisation of different types of collagen
    • Miller, E.J. & Rhodes, R.K. Preparation and characterisation of different types of collagen. Methods Enzymol. 82, 33-64 (1982).
    • (1982) Methods Enzymol. , vol.82 , pp. 33-64
    • Miller, E.J.1    Rhodes, R.K.2
  • 31
    • 0024448684 scopus 로고
    • Selective determination of hydroxyproline in urine by high-performance liquid chromatography using pre-column derivatisation
    • Terlink, T., Tavenier, P. & Netelenbos, J.C. Selective determination of hydroxyproline in urine by high-performance liquid chromatography using pre-column derivatisation. Clinica Chim Acta 183, 309-316 (1989).
    • (1989) Clinica Chim Acta , vol.183 , pp. 309-316
    • Terlink, T.1    Tavenier, P.2    Netelenbos, J.C.3
  • 32
    • 0014086921 scopus 로고
    • Modifications of a specific assay for hydroxyproline in urine
    • Kivirikko, K.I., Laitenen, O. & Prockop, D.J. Modifications of a specific assay for hydroxyproline in urine. Anal. Biochem. 19, 249-255 (1967).
    • (1967) Anal. Biochem. , vol.19 , pp. 249-255
    • Kivirikko, K.I.1    Laitenen, O.2    Prockop, D.J.3


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