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Volumn 98, Issue 11, 1996, Pages 2462-2468

Interaction between the insulin-like growth factor family and the integrin receptor family in tissue repair processes: Evidence in a rabbit ear dermal ulcer model

Author keywords

extracellular matrix; growth factors; insulin like growth factor I; integrins; wound healing

Indexed keywords

BINDING PROTEIN; GROWTH FACTOR RECEPTOR; INTEGRIN; SOMATOMEDIN B;

EID: 0029826177     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI119064     Document Type: Article
Times cited : (71)

References (57)
  • 1
    • 1542692267 scopus 로고
    • Mediators of wound healing, including the role of growth factors
    • R.C. Lee, T.A. Mustoe, and J.W. Siebert, editors. World Medical Press, New York
    • Mustoe, T.A., and R.D. Galiano. 1993. Mediators of wound healing, including the role of growth factors. In Advances in Wound Healing and Tissue Repair. Vol. 4. R.C. Lee, T.A. Mustoe, and J.W. Siebert, editors. World Medical Press, New York. 27-55.
    • (1993) Advances in Wound Healing and Tissue Repair , vol.4 , pp. 27-55
    • Mustoe, T.A.1    Galiano, R.D.2
  • 2
    • 0011088676 scopus 로고
    • Role of cytokines in wound repair
    • A. Gearting, J. Rossio, and J. Oppenheim, editors. Oxford University, New York
    • Jyung, R.W., and T.A. Mustoe. 1993. Role of cytokines in wound repair. In Clinical Applications of Cytokines. A. Gearting, J. Rossio, and J. Oppenheim, editors. Oxford University, New York. 307-329.
    • (1993) Clinical Applications of Cytokines , pp. 307-329
    • Jyung, R.W.1    Mustoe, T.A.2
  • 3
    • 0025835670 scopus 로고
    • Requirement of heparan sulfate for bFGF-mediated fibroblast growth and myoblast differentiation
    • Rapraeger, A.C., A. Krufka, and B.B. Olwin. 1991. Requirement of heparan sulfate for bFGF-mediated fibroblast growth and myoblast differentiation. Science (Wash. DC). 252:1705-1707.
    • (1991) Science (Wash. DC) , vol.252 , pp. 1705-1707
    • Rapraeger, A.C.1    Krufka, A.2    Olwin, B.B.3
  • 4
    • 0026080765 scopus 로고
    • Proteoglycans as modulators of growth factor activities
    • Ruoslahti, E., and Y. Yamaguchi. 1991. Proteoglycans as modulators of growth factor activities. Cell. 64:867-869.
    • (1991) Cell , vol.64 , pp. 867-869
    • Ruoslahti, E.1    Yamaguchi, Y.2
  • 6
    • 0027976511 scopus 로고
    • Betaglycan can act as a dual modulator of TGF-β access to signaling receptors. Mapping of ligand binding and GAG attachment sites
    • Lopez-Casillas, F., H.M. Payne, J.L. Andres, and J. Massague. 1994. Betaglycan can act as a dual modulator of TGF-β access to signaling receptors. Mapping of ligand binding and GAG attachment sites. J. Cell Biol. 124:557-568.
    • (1994) J. Cell Biol. , vol.124 , pp. 557-568
    • Lopez-Casillas, F.1    Payne, H.M.2    Andres, J.L.3    Massague, J.4
  • 7
    • 0027230170 scopus 로고
    • Regulation of development and differentiation by the extracellular matrix
    • Adams, J.C., and F.M. Watt. 1993. Regulation of development and differentiation by the extracellular matrix. Development (Cambridge). 117:1183-1198.
    • (1993) Development (Cambridge) , vol.117 , pp. 1183-1198
    • Adams, J.C.1    Watt, F.M.2
  • 10
    • 0026647096 scopus 로고
    • Gene expression of insulin-like growth factor-I and IGF-I receptor during wound healing in rats
    • Steenfos, H.H., and J.Q. Janssen. 1992. Gene expression of insulin-like growth factor-I and IGF-I receptor during wound healing in rats. Eur. J. Surg. 158:327-331.
    • (1992) Eur. J. Surg. , vol.158 , pp. 327-331
    • Steenfos, H.H.1    Janssen, J.Q.2
  • 11
    • 0026680779 scopus 로고
    • Insulin-like growth factors I and II expression in the healing wound
    • Gartner, M.H., J.D. Benson, and M.D. Caldwell. 1992. Insulin-like growth factors I and II expression in the healing wound. J. Surg. Res. 52:389-394.
    • (1992) J. Surg. Res. , vol.52 , pp. 389-394
    • Gartner, M.H.1    Benson, J.D.2    Caldwell, M.D.3
  • 12
    • 0026466175 scopus 로고
    • Insulin-like growth factor-I reverses the impairment of wound healing induced by corticosteroids in rats
    • Suh, D.Y., T.K. Hunt, and E.M. Spencer. 1992. Insulin-like growth factor-I reverses the impairment of wound healing induced by corticosteroids in rats. Endocrinology. 131:2399-2403.
    • (1992) Endocrinology , vol.131 , pp. 2399-2403
    • Suh, D.Y.1    Hunt, T.K.2    Spencer, E.M.3
  • 13
    • 0026879441 scopus 로고
    • IGF binding proteins: Regulation of cellular actions
    • Clemmons, D. R. 1992. IGF binding proteins: regulation of cellular actions. Growth Regul. 2:80-87.
    • (1992) Growth Regul. , vol.2 , pp. 80-87
    • Clemmons, D.R.1
  • 14
    • 0026879641 scopus 로고
    • Insulin-like growth factor binding proteins: Gene structure and expression
    • Rechler, M.M., and A.L. Brown. 1992. Insulin-like growth factor binding proteins: gene structure and expression. Growth Regul. 2:55-68.
    • (1992) Growth Regul. , vol.2 , pp. 55-68
    • Rechler, M.M.1    Brown, A.L.2
  • 15
    • 0028958031 scopus 로고
    • Insulin-like growth factors and their binding proteins: Biological actions
    • Jones, J.I., and D.R. Clemmons. 1995. Insulin-like growth factors and their binding proteins: biological actions. Endocr. Rev. 16:3-34.
    • (1995) Endocr. Rev. , vol.16 , pp. 3-34
    • Jones, J.I.1    Clemmons, D.R.2
  • 16
    • 0027515722 scopus 로고
    • Insulin-like growth factor binding protein-1 stimulates cell migration and binds to the alpha 5 beta 1 integrin by means of its Arg-Gly-Asp sequence
    • Jones, J.I., A. Gockerman, W.H. Busby, G. Wright, and D.R. Clemmons. 1993. Insulin-like growth factor binding protein-1 stimulates cell migration and binds to the alpha 5 beta 1 integrin by means of its Arg-Gly-Asp sequence. Proc. Natl. Acad. Sci. USA. 90:10553-10557.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10553-10557
    • Jones, J.I.1    Gockerman, A.2    Busby, W.H.3    Wright, G.4    Clemmons, D.R.5
  • 17
    • 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., G.L. Francis, L. Szabo, J.C. Wallace, and F.J. Ballard. 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
  • 18
    • 0024465961 scopus 로고
    • Insulin-like growth factor binding proteins from cultured endothelial cells: Purification, characterization and intrinsic biologic activities
    • Bar, R.S., B.A. Booth, M. Bowes, and B.L. Drake. 1989. Insulin-like growth factor binding proteins from cultured endothelial cells: purification, characterization and intrinsic biologic activities. Endocrinology. 125:1910-1920.
    • (1989) Endocrinology , vol.125 , pp. 1910-1920
    • Bar, R.S.1    Booth, B.A.2    Bowes, M.3    Drake, B.L.4
  • 19
    • 0026502260 scopus 로고
    • Cloning and sequence determination of bovine insulin-like growth factor binding protein-2 (IGFBP-2): Comparison of its structural and functional properties with IGFBP-1
    • Bourner, M.J., W.H. Busby, N.R. Seigel, G.G. Krivi, R.H. McCusker, and D.R. Clemmons. 1992. Cloning and sequence determination of bovine insulin-like growth factor binding protein-2 (IGFBP-2): comparison of its structural and functional properties with IGFBP-1. J. Cell. Biochem. 48:215-226.
    • (1992) J. Cell. Biochem. , vol.48 , pp. 215-226
    • Bourner, M.J.1    Busby, W.H.2    Seigel, N.R.3    Krivi, G.G.4    McCusker, R.H.5    Clemmons, D.R.6
  • 20
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark, E.A., and J.S. Brugge. 1995. Integrins and signal transduction pathways: the road taken. Science (Wash. DC). 268:233-239.
    • (1995) Science (Wash. DC) , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 21
    • 0027744501 scopus 로고
    • Regulation of extracellular matrix proteins and integrin cell substratum adhesion receptors on epithelium during cutaneous human wound healing in vivo
    • Juhasz, I., G.F. Murphy, H.C. Yan, M. Herlyn, and S.M. Albelda. 1993. Regulation of extracellular matrix proteins and integrin cell substratum adhesion receptors on epithelium during cutaneous human wound healing in vivo. Am. J. Pathol. 143:1458-1469.
    • (1993) Am. J. Pathol. , vol.143 , pp. 1458-1469
    • Juhasz, I.1    Murphy, G.F.2    Yan, H.C.3    Herlyn, M.4    Albelda, S.M.5
  • 22
    • 0027990415 scopus 로고
    • Wound repair in the context of extracellular matrix
    • Gailit, J., and R.A.F. Clark. 1994. Wound repair in the context of extracellular matrix. Curr Opin. Cell Biol. 6:717-725.
    • (1994) Curr Opin. Cell Biol. , vol.6 , pp. 717-725
    • Gailit, J.1    Clark, R.A.F.2
  • 23
    • 0027217908 scopus 로고
    • Expression of integrins and basement membrane components by wound keratinocytes
    • Larjava, H., T. Salo, K. Haapasalmi, R.H. Kramer, and J. Heino. 1993. Expression of integrins and basement membrane components by wound keratinocytes. J. Clin. Invest. 92:1425-1435.
    • (1993) J. Clin. Invest. , vol.92 , pp. 1425-1435
    • Larjava, H.1    Salo, T.2    Haapasalmi, K.3    Kramer, R.H.4    Heino, J.5
  • 24
    • 0027517680 scopus 로고
    • Distinctive integrin expression in the newly forming epidermis during wound healing in humans
    • Cavani, A., G. Zambruno, A. Marconi, V. Manca, M. Marchetti, and A. Giannetti. 1993. Distinctive integrin expression in the newly forming epidermis during wound healing in humans. J. Invest. Dermatol. 101:600-604.
    • (1993) J. Invest. Dermatol. , vol.101 , pp. 600-604
    • Cavani, A.1    Zambruno, G.2    Marconi, A.3    Manca, V.4    Marchetti, M.5    Giannetti, A.6
  • 25
    • 0028987192 scopus 로고
    • Transforming growth factor-β1 modulates β1 and β5 integrin receptors and induces the de novo expression of the αvβ6 heterodimer in normal human keratinocytes. Implications for wound healing
    • Zambruno, G., P.C. Marchisio, A. Marconi, C. Vaschieri, A. Melchiori, A. Giannetti, and M. De Luca. 1995. Transforming growth factor-β1 modulates β1 and β5 integrin receptors and induces the de novo expression of the αvβ6 heterodimer in normal human keratinocytes. Implications for wound healing. J. Cell Biol. 129:853-865.
    • (1995) J. Cell Biol. , vol.129 , pp. 853-865
    • Zambruno, G.1    Marchisio, P.C.2    Marconi, A.3    Vaschieri, C.4    Melchiori, A.5    Giannetti, A.6    De Luca, M.7
  • 26
  • 27
    • 0028168899 scopus 로고
    • TGF-beta1 stimulates expression of keratinocyte integrins during re-epithelialization of cutaneous wounds
    • Gailit, J., M.P. Welch, and R.A.F. Clark. 1994. TGF-beta1 stimulates expression of keratinocyte integrins during re-epithelialization of cutaneous wounds. J. Invest. Dermatol. 103:221-227.
    • (1994) J. Invest. Dermatol. , vol.103 , pp. 221-227
    • Gailit, J.1    Welch, M.P.2    Clark, R.A.F.3
  • 28
    • 0028013215 scopus 로고
    • Increased wound-breaking strength induced by insulin-like growth factor I in combination with insulin-like growth factor binding protein-1
    • Jyung, R.W., T.A. Mustoe, W.H. Busby, and D.R. Clemmons. 1994. Increased wound-breaking strength induced by insulin-like growth factor I in combination with insulin-like growth factor binding protein-1. Surgery (St. Louis). 115:233-239.
    • (1994) Surgery (St. Louis) , vol.115 , pp. 233-239
    • Jyung, R.W.1    Mustoe, T.A.2    Busby, W.H.3    Clemmons, D.R.4
  • 29
    • 84989028108 scopus 로고
    • Effects of insulin-like growth factor-I and insulin-like growth factor binding protein-1 on wound healing in a dermal ulcer model
    • Zhao, L.L., R.D. Galiano, G.N. Cox, S.I. Roth, and T.A. Mustoe. 1995. Effects of insulin-like growth factor-I and insulin-like growth factor binding protein-1 on wound healing in a dermal ulcer model. Wound Repair Regen. 3: 316-321.
    • (1995) Wound Repair Regen. , vol.3 , pp. 316-321
    • Zhao, L.L.1    Galiano, R.D.2    Cox, G.N.3    Roth, S.I.4    Mustoe, T.A.5
  • 30
    • 0024592852 scopus 로고
    • A comparison of the biological activity of the recombinant intact and truncated insulin-like growth factor I (IGF-I)
    • Carlsson-Skwirut, C., M. Lake, M. Hartmanis, K. Hall, and V.R. Sara. 1989. A comparison of the biological activity of the recombinant intact and truncated insulin-like growth factor I (IGF-I). Biochim. Biophys. Acta. 1011: 192-197.
    • (1989) Biochim. Biophys. Acta , vol.1011 , pp. 192-197
    • Carlsson-Skwirut, C.1    Lake, M.2    Hartmanis, M.3    Hall, K.4    Sara, V.R.5
  • 31
    • 0026674156 scopus 로고
    • Competition for binding to insulin-like growth factor (IGF) binding protein-2, 3, 4, and 5 by the IGFs and IGF analogs
    • Clemmons, D.R., M.L. Dehoff, W.H. Busby, M.L. Bayne, and M.A. Cascieri. 1992. Competition for binding to insulin-like growth factor (IGF) binding protein-2, 3, 4, and 5 by the IGFs and IGF analogs. Endocrinology. 131:890-895.
    • (1992) Endocrinology , vol.131 , pp. 890-895
    • Clemmons, D.R.1    Dehoff, M.L.2    Busby, W.H.3    Bayne, M.L.4    Cascieri, M.A.5
  • 32
    • 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., H.L. Muller, D.Y. Lee, P.J. Fielder, and R.G. Rosenfeld. 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    Muller, H.L.2    Lee, D.Y.3    Fielder, P.J.4    Rosenfeld, R.G.5
  • 33
    • 0026019087 scopus 로고
    • Growth factor-induced acceleration of tissue repair through direct and inductive activities in a rabbit dermal ulcer model
    • Mustoe, T.A., G.F. Pierce, C. Morishima, and T.F. Deuel. 1991. Growth factor-induced acceleration of tissue repair through direct and inductive activities in a rabbit dermal ulcer model. J. Clin. Invest. 87:694-703.
    • (1991) J. Clin. Invest. , vol.87 , pp. 694-703
    • Mustoe, T.A.1    Pierce, G.F.2    Morishima, C.3    Deuel, T.F.4
  • 34
    • 0026718378 scopus 로고
    • Platelet-derived growth factor (BB homodimer), transforming growth factor-b1 and basic fibroblast growth factor in dermal wound healing
    • Pierce, G.F., J.E. Tarpley, D. Yanagihara, T.A. Mustoe, G.M. Fox, and A. Thomason. 1992. Platelet-derived growth factor (BB homodimer), transforming growth factor-b1 and basic fibroblast growth factor in dermal wound healing. Am. J. Pathol. 140:1375-1388.
    • (1992) Am. J. Pathol. , vol.140 , pp. 1375-1388
    • Pierce, G.F.1    Tarpley, J.E.2    Yanagihara, D.3    Mustoe, T.A.4    Fox, G.M.5    Thomason, A.6
  • 35
    • 0028037490 scopus 로고
    • Effect of hyperbaric oxygen and growth factors on rabbit ear ischemic ulcers
    • Zhao, L., J. Davidson, S. Wee, S. Roth, and T. Mustoe. 1994. Effect of hyperbaric oxygen and growth factors on rabbit ear ischemic ulcers. Arch Surg. 129:1043-1049.
    • (1994) Arch Surg. , vol.129 , pp. 1043-1049
    • Zhao, L.1    Davidson, J.2    Wee, S.3    Roth, S.4    Mustoe, T.5
  • 36
    • 0342476502 scopus 로고
    • An insulin-like growth factor (IGF) binding protein enhances the biologic response to IGF-I
    • Elgin, R.G., W.H. Busby, and D.R. Clemmons. 1987. An insulin-like growth factor (IGF) binding protein enhances the biologic response to IGF-I. Proc. Natl. Acad. Sci. USA. 84:3254-3258.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3254-3258
    • Elgin, R.G.1    Busby, W.H.2    Clemmons, D.R.3
  • 37
    • 0023693399 scopus 로고
    • Growth hormone dependent insulin-like growth factor binding protein both inhibits and potentiates IGF-I stimulated DNA synthesis in skin fibroblasts
    • DeMellow, J.S.M., and R.C. Baxter. 1988. Growth hormone dependent insulin-like growth factor binding protein both inhibits and potentiates IGF-I stimulated DNA synthesis in skin fibroblasts. Biochem. Biophys. Res. Commun. 156:199-204.
    • (1988) Biochem. Biophys. Res. Commun. , vol.156 , pp. 199-204
    • DeMellow, J.S.M.1    Baxter, R.C.2
  • 38
    • 0024401780 scopus 로고
    • Insulin-like growth factor I (IGF-I) binding protein complex is a better mitogen than free IGF-I
    • Blum, W.F., E.W. Jenne, F. Reppin, K. Kietzmann, M.B. Ranke, and J.R. Bierich. 1989. Insulin-like growth factor I (IGF-I) binding protein complex is a better mitogen than free IGF-I. Endocrinology. 125:766-772.
    • (1989) Endocrinology , vol.125 , pp. 766-772
    • Blum, W.F.1    Jenne, E.W.2    Reppin, F.3    Kietzmann, K.4    Ranke, M.B.5    Bierich, J.R.6
  • 39
    • 0026656777 scopus 로고
    • Effect of recombinant IGF binding protein-1 on primary cultures of human keratinocytes and fibroblasts: Selective enhancement of IGF-1 but not IGF-2-induced cell proliferation
    • Kratz, G., M. Lake, K. Ljungstrom, G. Forsberg, A. Haegerstrand, and M. Gidlund. 1992. Effect of recombinant IGF binding protein-1 on primary cultures of human keratinocytes and fibroblasts: selective enhancement of IGF-1 but not IGF-2-induced cell proliferation. Exp. Cell Res. 202:381-385.
    • (1992) Exp. Cell Res. , vol.202 , pp. 381-385
    • Kratz, G.1    Lake, M.2    Ljungstrom, K.3    Forsberg, G.4    Haegerstrand, A.5    Gidlund, M.6
  • 40
    • 0026002202 scopus 로고
    • Insulin-like growth factor (IGF) binding to cell monolayers is directly modulated by the addition of IGF-binding proteins
    • McCusker, R.H., W.H. Busby, M.H. Dehoff, C. Camacho-Hubner, and D.R. Clemmons. 1991. Insulin-like growth factor (IGF) binding to cell monolayers is directly modulated by the addition of IGF-binding proteins. Endocrinology. 129:939-949.
    • (1991) Endocrinology , vol.129 , pp. 939-949
    • McCusker, R.H.1    Busby, W.H.2    Dehoff, M.H.3    Camacho-Hubner, C.4    Clemmons, D.R.5
  • 41
    • 0025641845 scopus 로고
    • Structural and biological characterization of bovine insulin-like growth factor binding protein-3
    • Conover, C.A., M. Ronk, F. Lombana, and D.R. Powell. 1990. Structural and biological characterization of bovine insulin-like growth factor binding protein-3. Endocrinology. 127:2795-2803.
    • (1990) Endocrinology , vol.127 , pp. 2795-2803
    • Conover, C.A.1    Ronk, M.2    Lombana, F.3    Powell, D.R.4
  • 42
    • 0028211185 scopus 로고
    • In vivo proteolysis of serum insulin-like growth factor (IGF) binding protein-3 results in increased availability of IGF to target cells
    • Blat, C., J. Villaudy, and M. Binoux. 1994. In vivo proteolysis of serum insulin-like growth factor (IGF) binding protein-3 results in increased availability of IGF to target cells. J. Clin. Invest. 93:2286-2290.
    • (1994) J. Clin. Invest. , vol.93 , pp. 2286-2290
    • Blat, C.1    Villaudy, J.2    Binoux, M.3
  • 43
    • 0025127106 scopus 로고
    • Insulin-like growth factor (IGF) binding to human fibroblast and glioblastoma cells: The modulating effect of cell released IGF binding proteins (IGFBPs)
    • McCusker, R.H., C. Camacho-Hubner, M.L. Bayne, M.A. Cascieri, and D.R. Clemmons. 1990. Insulin-like growth factor (IGF) binding to human fibroblast and glioblastoma cells: the modulating effect of cell released IGF binding proteins (IGFBPs). J. Cell. Physiol. 144:244-253.
    • (1990) J. Cell. Physiol. , vol.144 , pp. 244-253
    • McCusker, R.H.1    Camacho-Hubner, C.2    Bayne, M.L.3    Cascieri, M.A.4    Clemmons, D.R.5
  • 44
    • 0027162738 scopus 로고
    • In vivo effects of systemic insulin-like growth factor-I alone and complexed with insulin-like growth factor binding protein-3 on corticosteroid suppressed wounds
    • Hamon, G.A., T.K. Hunt, and E.M. Spencer. 1993. In vivo effects of systemic insulin-like growth factor-I alone and complexed with insulin-like growth factor binding protein-3 on corticosteroid suppressed wounds. Growth Regul. 3: 53-56.
    • (1993) Growth Regul. , vol.3 , pp. 53-56
    • Hamon, G.A.1    Hunt, T.K.2    Spencer, E.M.3
  • 46
    • 0025819877 scopus 로고
    • Phosphorylation of insulin-like growth factor (IGF) binding protein 1 in cell culture and in vivo: Effects on affinity for IGF-I
    • Jones, J.I., A.J. D'Ercole, C. Camacho-Hubner, and D.R. Clemmons. 1991. Phosphorylation of insulin-like growth factor (IGF) binding protein 1 in cell culture and in vivo: effects on affinity for IGF-I. Proc. Natl. Acad. Sci. USA. 88:7481-7485.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7481-7485
    • Jones, J.I.1    D'Ercole, A.J.2    Camacho-Hubner, C.3    Clemmons, D.R.4
  • 47
    • 0023785178 scopus 로고
    • Purification of a 31000 dalton insulin like growth factor binding protein from human amniotic fluid
    • Busby, W.H., D.G. Klapper, and D.R. Clemmons. 1988. Purification of a 31000 dalton insulin like growth factor binding protein from human amniotic fluid. J. Biol. Chem. 263:14203-14210.
    • (1988) J. Biol. Chem. , vol.263 , pp. 14203-14210
    • Busby, W.H.1    Klapper, D.G.2    Clemmons, D.R.3
  • 48
    • 0029867915 scopus 로고    scopus 로고
    • Ligand occupancy of the aVb3 integrin is necessary for smooth muscle cells to migrate in response to insulin-like growth factor 1
    • Jones, J., T. Prevette, A. Gockerman, and D. Clemmons. 1996. Ligand occupancy of the aVb3 integrin is necessary for smooth muscle cells to migrate in response to insulin-like growth factor 1. Proc. Natl. Acad. Sci. USA. 93:2482-2487.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2482-2487
    • Jones, J.1    Prevette, T.2    Gockerman, A.3    Clemmons, D.4
  • 49
    • 0029125685 scopus 로고
    • Insulin-like growth factor binding protein-2 inhibits smooth muscle cell migration response to IGF-I
    • Gockerman, A., J. Jones, T. Prevette, and D. Clemmons. 1995. Insulin-like growth factor binding protein-2 inhibits smooth muscle cell migration response to IGF-I. Endocrinology. 136:4168-4173.
    • (1995) Endocrinology , vol.136 , pp. 4168-4173
    • Gockerman, A.1    Jones, J.2    Prevette, T.3    Clemmons, D.4
  • 50
    • 0028641601 scopus 로고
    • Association of insulin receptor substrate-1 with integrins
    • Vuori, K., and E. Ruoslahti. 1994. Association of insulin receptor substrate-1 with integrins. Science (Wash. DC). 266:1576-1578
    • (1994) Science (Wash. DC) , vol.266 , pp. 1576-1578
    • Vuori, K.1    Ruoslahti, E.2
  • 51
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
    • Schlaepfer, D.D., S.K. Hanks, T. Hunter, and P. van der Geer. 1994. Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature (Lond.). 372:786-791.
    • (1994) Nature (Lond.) , vol.372 , pp. 786-791
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    Van Der Geer, P.4
  • 52
    • 0027939187 scopus 로고
    • Integrin-mediated cell adhesion activates mitogen-activated protein kinases
    • Chen, Q., M.S. Kinch, T.H. Lin, K. Burridge, and R.L. Juliano. 1994. Integrin-mediated cell adhesion activates mitogen-activated protein kinases. J. Biol. Chem. 269:26602-26605.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26602-26605
    • Chen, Q.1    Kinch, M.S.2    Lin, T.H.3    Burridge, K.4    Juliano, R.L.5
  • 54
    • 0028018178 scopus 로고
    • Signalling through the insulin receptor and the insulin-like growth faclor-I receptor
    • Obberghen, E.V. 1994. Signalling through the insulin receptor and the insulin-like growth faclor-I receptor. Diabetologia. 37(Suppl. 2):S125-S134.
    • (1994) Diabetologia , vol.37 , Issue.2 SUPPL.
    • Obberghen, E.V.1
  • 55
    • 0028817908 scopus 로고
    • Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex
    • Plopper, G.E., H.P. McNamee, L.E. Dike, K. Bojanowski, and D.E. Ingber. 1995. Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex. Mol. Biol. Cell. 6: 349-1356.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 349-1356
    • Plopper, G.E.1    McNamee, H.P.2    Dike, L.E.3    Bojanowski, K.4    Ingber, D.E.5
  • 57
    • 0028362351 scopus 로고
    • Integrating with integrins
    • Schwartz, M., and D. Ingber. 1994. Integrating with integrins. Mol. Biol. Cell. 5:389-393.
    • (1994) Mol. Biol. Cell. , vol.5 , pp. 389-393
    • Schwartz, M.1    Ingber, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.