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Analysis of the Interaction of IGF-I Analogs with the IGF-I Receptor and IGF Binding Proteins

  • Margaret A. Cascieri
  • Marvin L. Bayne
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 343)

Abstract

The characterization of the various species of IGF binding proteins (IGFBPs) by molecular cloning has revealed a large family of highly homologous soluble proteins with high affinity for both IGF-I and IGF-II. The type 1 IGF receptor and the IGFBPs appear to form a complex regulatory system for transducing and modulating the activity of IGF-I and IGF-II. The determination of the roles of these proteins in IGF action has been facilitated by the use of IGF-I analogs that selectively bind to either the receptor or to IGFBPs.

Keywords

Helical Domain Receptor Binding Domain Ternary Complex Formation Poor Affinity Normal Affinity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    Bayne, M.L., Cascieri, M.A., Kelder, B., Applebaum, J., Chicchi, G., Shapiro, J.A., Pasleau, F., and Kopchick, J.J. (1987) Proc. Natl. Acad. Sci. USA 84:2638–2642.PubMedCrossRefGoogle Scholar
  2. 2.
    Bayne, M.L., Applebaum, J., Chicchi, G.G., Hayes, N.S., Green, B.G., and Cascieri, M.A. (1988) Gene 66:235–244.PubMedCrossRefGoogle Scholar
  3. 3.
    Blundell, T.L., Bedarker, S., Rinderknecht, E., and Humbel, R.E. (1978) Proc. Natl. Acad. Sci., USA 75:180–184.PubMedCrossRefGoogle Scholar
  4. 4.
    Blundell, T.L., Bedarker, S., and Humbel, R.E. (1983) Fed. Proc., Fed. Am. Soc. Exp. Biol. 42:2592–2597.Google Scholar
  5. 5.
    Cooke, R.M., Harvey, T.S., Campbell, I.D. (1991) Biochemistry 30:5484–5491.PubMedCrossRefGoogle Scholar
  6. 6.
    Tager, H., Thomas, N., Assoian, R., Rubenstein, A., Solkow, M., Olefsky, J., and Kaiser, E.T. (1980) Proc. Natl. Acad. Sci., USA 77:3181–3185.PubMedCrossRefGoogle Scholar
  7. 7.
    Kobayashi, M., Ohgaku, S., Iwasaki, M., Maegawa, H., Shigeta, Y., and Inouye, K. (1982) Biochem. J. 206:597–603.PubMedGoogle Scholar
  8. 8.
    Cascieri, M.A., Chicchi, G.G., Applebaum, J., Hayes, N.S., Green, B.G., and Bayne, M.L. (1988) Biochemistry 27:3229–3223.PubMedCrossRefGoogle Scholar
  9. 9.
    Bayne, M.L., Applebaum, J., Underwood, D., Chicchi, G.G., Green, B.G., Hayes, N.S., and Cascieri, M.A. (1988) J. Biol. Chem. 264:11004–11008.Google Scholar
  10. 10.
    Bayne, M.L., Applebaum, J., Chicchi, G.G., Miller, R.E., and Cascieri, M.A. (1990) J. Biol. Chem. 26:15648–15652.Google Scholar
  11. 11.
    Morgan, D.O., Edman, J.C., Standring, D.N., Fried, V.A., Smith, M.C., Roth, R.A., and Rutter, W.J. (1987) Nature 329:301–307.PubMedCrossRefGoogle Scholar
  12. 12.
    Cascieri, M.A., Chicchi, G.G., Applebaum, J., Green, B.G., Hayes, N.S., and Bayne, M.L. (1989) J. Biol. Chem. 264:2199–2202.PubMedGoogle Scholar
  13. 13.
    Beukers, M.W., Oh, Y., Shang, H., Ling, N., and Rosenfeld, R.G. (1991) Endocrinology 128:1201–1203.PubMedCrossRefGoogle Scholar
  14. 14.
    Sakano, K., Enjoh, T., Numata, F., Fujiwara, H., Marumoto, Y., Higashihashi, N., Sato, Y., Perdue, J.F., and Fujita-Yamaguchi, Y. (1991) J. Biol. Chem. 266:20626–20635.PubMedGoogle Scholar
  15. 15.
    Burgisser, D.M., Roth, B.V., Giger, R., Luthi, C., Weigl, S., Zarn, J., and Humbel, R.E. (1991) J. Biol. Chem. 266:1029–1033.PubMedGoogle Scholar
  16. 16.
    Bäýne, M.L., Applebaum, J., Chicchi, G.G., Hayes, N.S., Green, B.G., and Cascieri, M.A. (1988) J. Biol. Chem. 263:6233–6239.PubMedGoogle Scholar
  17. 17.
    Cascieri, M.A., Hayes, N.S., and Bayne, M.L. (1989) J. Cell. Physiol. 139:181–188.PubMedCrossRefGoogle Scholar
  18. 18.
    Baxter, R.C., Bayne, M.L., and Cascieri, M.A. (1992) J. Biol. Chem. 267:60–65.PubMedGoogle Scholar
  19. 19.
    Clemmons, D.R., Cascieri, M.A., Camacho-Hubner, C, McCusker, R.H., and Bayne, M.L. (1990) J. Biol. Chem. 265:12210–12216.PubMedGoogle Scholar
  20. 20.
    Clemmons, D.R., Dehoff, M.L., Busby, W.H., Bayne, M.L. and Cascieri, M.A. (1992) Endocrinology 131:890–895.PubMedCrossRefGoogle Scholar
  21. 21.
    Baxtéîr, R.C., Martin, J.C., and Beniac, V.A. (1989) J. Biol. Chem. 264:11843–11848.Google Scholar
  22. 22.
    Cascieri, M.A., Saperstein, R., Hayes, N.S., Green, B.G., Chicchi, G.G. ,Applebaum, J., and Bayne, M.L. (1988) Endocrinology 123:373–381.PubMedCrossRefGoogle Scholar
  23. 23.
    Tollefson, S.E., Heath-Monnig, E., Cascieri, M.A., Bayne, M.L., and Daughaday, W.H. (1991) J. Clin. Inv. 87:1241–1250.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1994

Authors and Affiliations

  • Margaret A. Cascieri
    • 1
  • Marvin L. Bayne
    • 1
  1. 1.Department of Molecular Pharmacology and BiochemistryMerck Research LaboratoriesRahwayUSA

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