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Volumn 13, Issue 3-4, 1996, Pages 261-272

Design and characterisation of long-r3-insulin-like growth factor-I muteins which show resistance to pepsin digestion

Author keywords

Biological activity; IGF I muteins; Kinetics of degradation; Pepsin resistance; Receptor binding; Site directed mutagenesis

Indexed keywords

MUTANT PROTEIN; PEPSIN A; SOMATOMEDIN C; SOMATOMEDIN C DERIVATIVE;

EID: 0029862348     PISSN: 08977194     EISSN: None     Source Type: Journal    
DOI: 10.3109/08977199609003227     Document Type: Article
Times cited : (5)

References (28)
  • 1
    • 0023898621 scopus 로고
    • Structural analogs of human insulin-like growth factor I with reduced affinity for serum binding proteins and the type 2 insulin-like growth factor receptor
    • Bayne, M. L., Applebaum, J., Chicchi, G.G., Hayes, N. S., Green, B. G. and Cascieri, M. A. (1988) Structural analogs of human insulin-like growth factor I with reduced affinity for serum binding proteins and the type 2 insulin-like growth factor receptor. J. Biol. Chem. 263, 6233-6239.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6233-6239
    • Bayne, M.L.1    Applebaum, J.2    Chicchi, G.G.3    Hayes, N.S.4    Green, B.G.5    Cascieri, M.A.6
  • 2
    • 0025113224 scopus 로고
    • The roles of tyrosines 24, 31 and 60 in the high affinity binding of insulin-like growth factor-I to the type 1 insulin-like growth factor receptor
    • Bayne, M. L., Applebaum, J., Chicchi, G. G., Miller, R. E. and Cascieri, M. A. (1990) The roles of tyrosines 24, 31 and 60 in the high affinity binding of insulin-like growth factor-I to the type 1 insulin-like growth factor receptor. J. Biol. Chem. 265, 15648-15652.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15648-15652
    • Bayne, M.L.1    Applebaum, J.2    Chicchi, G.G.3    Miller, R.E.4    Cascieri, M.A.5
  • 3
    • 0025969881 scopus 로고
    • Suggestions for "safe" residue substitutions in site-directed mutagenesis
    • Bordo, D. and Argos, P. (1991) Suggestions for "safe" residue substitutions in site-directed mutagenesis. J. Mol. Biol. 217, 721-729.
    • (1991) J. Mol. Biol. , vol.217 , pp. 721-729
    • Bordo, D.1    Argos, P.2
  • 4
    • 0024581918 scopus 로고
    • Structural analogs of human insulin-like growth factor (IGF) I with altered affinity for type 2 IGF receptors
    • Cascieri, M. A., Chicchi, G. G., Applebaum, J., Green, B. G., Hayes, N. S. and Bayne, M. L. (1989) Structural analogs of human insulin-like growth factor (IGF) I with altered affinity for type 2 IGF receptors. J. Biol. Chem. 264, 2199-2202.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2199-2202
    • Cascieri, M.A.1    Chicchi, G.G.2    Applebaum, J.3    Green, B.G.4    Hayes, N.S.5    Bayne, M.L.6
  • 6
    • 0025985470 scopus 로고
    • Characterisation of the biological activity of IGF I analogs with reduced affinity for the IGF receptors and binding proteins
    • Raizada, M. K. and LeRoith, D., ed., Plenum Press, New York
    • Cascieri, M. A., Chicchi, G. G. and Bayne, M. L. (1991) Characterisation of the biological activity of IGF I analogs with reduced affinity for the IGF receptors and binding proteins. In Molecular Biology and Physiology of Insulin and Insulin-like Growth Factors (Raizada, M. K. and LeRoith, D., ed.), pp. 23-30, Plenum Press, New York.
    • (1991) Molecular Biology and Physiology of Insulin and Insulin-like Growth Factors , pp. 23-30
    • Cascieri, M.A.1    Chicchi, G.G.2    Bayne, M.L.3
  • 7
    • 0024418033 scopus 로고
    • Protein estimation by the product of integrated peak area and flow rate
    • Buck, M. A., Olah, T. A., Weitzmann, C. J. and Cooperman, B. S. (1989) Protein estimation by the product of integrated peak area and flow rate. Anal. Biochem. 182, 295-299.
    • (1989) Anal. Biochem. , vol.182 , pp. 295-299
    • Buck, M.A.1    Olah, T.A.2    Weitzmann, C.J.3    Cooperman, B.S.4
  • 8
    • 0025822851 scopus 로고
    • Solution structure of human insulin-like growth factor I: A nuclear magnetic resonance and restrained molecular dynamics study
    • Cooke, R. M., Harvey, T. S. and Campbell, I. D. (1991) Solution structure of human insulin-like growth factor I: A nuclear magnetic resonance and restrained molecular dynamics study. Biochemistry 30, 5484-5491.
    • (1991) Biochemistry , vol.30 , pp. 5484-5491
    • Cooke, R.M.1    Harvey, T.S.2    Campbell, I.D.3
  • 11
    • 0028208349 scopus 로고
    • Novel oral drug formulations. Their potential in modulating adverse effects
    • Florence, A. T. and Jani, P. U. (1994) Novel oral drug formulations. Their potential in modulating adverse effects. Drug Safety 10, 233-266.
    • (1994) Drug Safety , vol.10 , pp. 233-266
    • Florence, A.T.1    Jani, P.U.2
  • 12
    • 0024997961 scopus 로고
    • Separation and characterization of modified variants of recombinant human insulin-like growth factor I derived from a fusion protein secreted from Escherichia coli
    • Forsberg, G., Palm, G., Ekebacke, A., Josephson, S. and Hartmanis, M. (1990) Separation and characterization of modified variants of recombinant human insulin-like growth factor I derived from a fusion protein secreted from Escherichia coli. Biochem. J. 271, 357-363.
    • (1990) Biochem. J. , vol.271 , pp. 357-363
    • Forsberg, G.1    Palm, G.2    Ekebacke, A.3    Josephson, S.4    Hartmanis, M.5
  • 14
    • 0026696046 scopus 로고
    • Novel recombinant fusion protein analogues of insulin-like growth factor (IGF)-I indicate the relative importance of IGF-binding protein and receptor binding for enhanced biological activity
    • Francis, G. L., Ross, M., Ballard, F. J., Milner, S. J., Senn, C. McNeil, K. A., Wallace, J. C., King, R. and Wells, J. R. E. (1992) Novel recombinant fusion protein analogues of insulin-like growth factor (IGF)-I indicate the relative importance of IGF-binding protein and receptor binding for enhanced biological activity. J. Mol. Endocrinol. 8, 213-223.
    • (1992) J. Mol. Endocrinol. , vol.8 , pp. 213-223
    • Francis, G.L.1    Ross, M.2    Ballard, F.J.3    Milner, S.J.4    Senn, C.5    McNeil, K.A.6    Wallace, J.C.7    King, R.8    Wells, J.R.E.9
  • 16
    • 0028958031 scopus 로고
    • Insulin-like growth factors and their binding proteins: Biological actions
    • Jones, J. I. and Clemmons, D. R. (1995) Insulin-like growth factors and their binding proteins: biological actions. Endocrine Reviews 16, 3-34.
    • (1995) Endocrine Reviews , vol.16 , pp. 3-34
    • Jones, J.I.1    Clemmons, D.R.2
  • 18
    • 0024394536 scopus 로고
    • Identification of the types of insulin-like growth factor binding proteins that are secreted by muscle cells in vitro
    • McCusker, R. H., Cacacho-Hubner, C. and Clemmons, D. R. (1989) Identification of the types of insulin-like growth factor binding proteins that are secreted by muscle cells in vitro. J. Biol. Chem. 264, 7795-7800.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7795-7800
    • McCusker, R.H.1    Cacacho-Hubner, C.2    Clemmons, D.R.3
  • 19
    • 0027502282 scopus 로고
    • Characterization of the affinities of insulin-like growth factor (IGF) binding proteins 1-4 for IGF-I, IGF-II, IGF-I/ insulin hybrid and IGF-I analogs
    • Oh, Y., Müller, H. L. Lee, D.-Y, Fielder, P. J. and Rosenfeld, R. G. (1993) Characterization of the affinities of insulin-like growth factor (IGF) binding proteins 1-4 for IGF-I, IGF-II, IGF-I/ insulin hybrid and IGF-I analogs. Endocrinology 132, 1337-1344.
    • (1993) Endocrinology , vol.132 , pp. 1337-1344
    • Oh, Y.1    Müller, H.L.2    Lee, D.-Y.3    Fielder, P.J.4    Rosenfeld, R.G.5
  • 21
    • 0026021381 scopus 로고
    • Drug Delivery Systems 5A. Oral drug delivery
    • Ranade, V. V. (1991) Drug Delivery Systems 5A. Oral drug delivery. J. Clin. Pharmacol. 31, 2-16.
    • (1991) J. Clin. Pharmacol. , vol.31 , pp. 2-16
    • Ranade, V.V.1
  • 22
    • 0026719008 scopus 로고
    • Insulin-like growth factor-I and its N-terminal modified analogues induce marked gut growth in dexamethasone-treated rats
    • Read, L. C., Tomas, F. M., Howarth, G. S., Martin, A. A., Edson, K. J., Gillespie, C. M., Owens, P. C. and Ballard, F. J. (1992) Insulin-like growth factor-I and its N-terminal modified analogues induce marked gut growth in dexamethasone-treated rats. J. Endocrinol. 133, 421-432.
    • (1992) J. Endocrinol. , vol.133 , pp. 421-432
    • Read, L.C.1    Tomas, F.M.2    Howarth, G.S.3    Martin, A.A.4    Edson, K.J.5    Gillespie, C.M.6    Owens, P.C.7    Ballard, F.J.8
  • 23
    • 0024603050 scopus 로고
    • Insulin-like growth factor (IGF)-binding proteins inhibit the biological activities of IGF-I and IGF-II, but not des(1-3)IGF-I
    • Ross, M., Francis, G. L., Szabo, L., Wallace, J. C. and Ballard, F. J. (1989) Insulin-like growth factor (IGF)-binding proteins inhibit the biological activities of IGF-I and IGF-II, but not des(1-3)IGF-I. Biochem. J. 258, 267-272.
    • (1989) Biochem. J. , vol.258 , pp. 267-272
    • Ross, M.1    Francis, G.L.2    Szabo, L.3    Wallace, J.C.4    Ballard, F.J.5
  • 26
    • 0028225790 scopus 로고
    • Prolonged administration of IGF peptides enhances growth of gastrointestinal tissues in normal rats
    • Steeb, C.-B., Trahair, J. F., Tomas, F. M. and Read, L. C. (1994) Prolonged administration of IGF peptides enhances growth of gastrointestinal tissues in normal rats. Am. J. Physiol. 266, G1090-G1098.
    • (1994) Am. J. Physiol. , vol.266
    • Steeb, C.-B.1    Trahair, J.F.2    Tomas, F.M.3    Read, L.C.4
  • 27
    • 0026684906 scopus 로고
    • Production and characterization of recombinant chicken insulin-like growth factor-I from Escherichia coli
    • Upton, Z., Francis, G. L., Ross, M., Wallace, J. C. and Ballard, F. J. (1992) Production and characterization of recombinant chicken insulin-like growth factor-I from Escherichia coli. J. Mol. Endocrinol. 9, 83-92.
    • (1992) J. Mol. Endocrinol. , vol.9 , pp. 83-92
    • Upton, Z.1    Francis, G.L.2    Ross, M.3    Wallace, J.C.4    Ballard, F.J.5
  • 28
    • 0029122580 scopus 로고
    • Degradation of IGF-I in the adult rat gastrointestinal tract is limited by a specific antiserum or the dietary protein casein
    • Xian, C. J., Shoubridge, C. A. and Read, L. C. (1995) Degradation of IGF-I in the adult rat gastrointestinal tract is limited by a specific antiserum or the dietary protein casein. J. Endocrinol. 146, 215-225.
    • (1995) J. Endocrinol. , vol.146 , pp. 215-225
    • Xian, C.J.1    Shoubridge, C.A.2    Read, L.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.