Skip to main content

The Membrane Receptor for Epidermal Growth Factor

Structural and Functional Studies

  • Chapter
  • 43 Accesses

Part of the book series: New Horizons in Therapeutics ((NHTH))

Abstract

A useful model system for exploring the molecular mechanisms underlying the proliferation of eucaryotic cells is the mode of action of the cellular mitogen epidermal growth factor (EGF). Epidermal growth factor is a small protein containing 53 amino acid residues (Carpenter and Cohen, 1980). It binds tightly to a specific membrane receptor. The occupation of the receptor molecule leads to activation of the pleiotropic response culminating in DNA synthesis and cell proliferation (Carpenter and Cohen, 1980; Schlessinger 1983).

This is a preview of subscription content, log in via an institution.

Buying options

Chapter
USD   29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD   39.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD   54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Learn about institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Bishop, M. J., 1983, Cell oncogenes and retroviruses, Annu. Rev. Biochem. 52: 301–354.

    Article  PubMed  CAS  Google Scholar 

  • Carpenter, G., and Cohen, S., 1979, Epidermal growth factor, Annu. Rev. Biochem. 48:193– 216.

    Article  PubMed  Google Scholar 

  • Carpenter, G., King, L., Jr., and Cohen, S., 1978, Epidermal growth factor stimulates phosphorylation in membrane preparation in vitro, Nature 276: 409–410.

    Article  CAS  Google Scholar 

  • Carpenter, G., King, L., Jr., and Cohen, S., 1979, Rapid enhancement of protein phosphorylation in A-431 cell membrane preparations by epidermal growth factor, J. Biol. Chem. 254: 4884–4891.

    PubMed  CAS  Google Scholar 

  • Chinkers, M., and Cohen, M. S., 1981, Purified EGF receptor-kinase interacts specifically with antibodies to Rous sarcoma virus transforming protein, Nature 290: 516–519.

    Article  PubMed  CAS  Google Scholar 

  • Cohen, S., Carpenter, G., and King, L., Jr., 1980, Epidermal growth factor-receptor protein kinase interactions. Co-purification of receptor and epidermal growth factor-enhanced phosphorylation activity, J. Biol. Chem. 255: 4834–4842.

    PubMed  CAS  Google Scholar 

  • Cohen, S., Hiroshi, U., Christa, S., and Michael, C., 1982, A native 170,000 epidermal growth factor receptor-kinase complex from shed plasma membrane vesicles, J. Biol. Chem. 257: 1523–1531.

    PubMed  CAS  Google Scholar 

  • Collett, M. S., Erikson, E., Purchio, A. F., Brugge, J. S., and Erikson, R. L., 1979, A normal cell protein similar in structure and function to avian sarcoma virus transforming gene product, Proc. Natl. Acad. Sci. U.S.A. 76: 3159–3163.

    Article  PubMed  CAS  Google Scholar 

  • Collett, M. S., Purchio, A. F., and Erikson, R. L., 1980, Avian sarcoma virus transforming protein, PP60src, shows protein kinase activity specific for tyrosine, Nature 285: 167–169.

    Article  PubMed  CAS  Google Scholar 

  • Downward, J., Yarden, Y., Mayes, E., Scrace, G., Totty, N., Stockwell, P., Ullrich, A., Schlessinger, J., and Waterfield, M., 1984, Close similarity of epidermal growth factor receptor and V-erb-B oncogene protein sequences, Nature 307: 521–526.

    Article  PubMed  CAS  Google Scholar 

  • Ek, B., Westermark, B., Wasteson, A., and Heldin, C.-H., 1982, Stimulation of tyrosine- specific phosphorylation by plateled-derived growth factor, Nature 295: 419–420, 1982.

    Article  PubMed  CAS  Google Scholar 

  • Gentry, L. E., Rohrschneider, L. R., Casnellie, J. E., and Krebs, E. G., 1983, Antibodies to defined region of PP60src neutralize the tyrosine specific kinase activity, J. Biol. Chem. 258: 11219–11228.

    PubMed  CAS  Google Scholar 

  • Gooi, H. C., Schlessinger, J., Lax, I., Yarden, Y., Libermann, T. A., and Feizi, T., 1983, Monoclonal antibody reactive with the human epidermal growth factor receptor recognizes the blood group A antigen, Biosci. Rep. 3: 1045–1052.

    Article  PubMed  CAS  Google Scholar 

  • Hapgood, J., Liberman, T. A., Lax, I., Yarden, Y., Schreiber, A. B., Naor, Z., and Schlessinger, J., 1983, Monoclonal antibodies against EGF receptor induce prolactin synthesis in cultured rat pituitary cells (GH3), Proc. Natl. Acad. Sci. U.S.A. 80: 6451–6455.

    Article  PubMed  CAS  Google Scholar 

  • Hortsch, M., Schlessinger, J., Gootwine, E., and Webb, C. G., 1983, appearance of a functional EGF-receptor kinase during rodent embryogenesis, EMBO J. 2: 1937–1941.

    PubMed  CAS  Google Scholar 

  • Hunter, T., and Sefton, B. M., 1980, The transforming gene product of Rous sarcoma virus phosphorylates tyrosine, Proc. Natl. Acad. Sci. U.S.A. 77: 1311–1315.

    Article  PubMed  CAS  Google Scholar 

  • Kasuga, M., Zick, Y., Blithe, D. L., Crettaz, M., and Kahan, C. R., 1982, Insulin stimulates tyrosine phosphorylation of insulin receptor in a cell free system, Nature 298: 667–669.

    Article  PubMed  CAS  Google Scholar 

  • Kudlow, J. E., Buss, J. E., and Gill, G. N., 1981, Anti-PP60src antibodies are substrates for EGF-stimulated protein kinase, Nature 290: 519–521.

    Article  PubMed  CAS  Google Scholar 

  • Laemmli, U. K., 1970, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227: 680–683.

    Article  PubMed  CAS  Google Scholar 

  • Lax, I., Bar-Eli, M., Yarden, Y., Libermann, T. A., and Schlessinger, J., 1984, Antibodies to two defined regions on PP60src interact specifically with the EGF receptor kinase system, Proc. Natl. Acad. Sci. U.S.A. 81: 5911–5915.

    Article  PubMed  CAS  Google Scholar 

  • Levinson, A. D., Oppermann, H., Varmus, H. E., and Bishop, J. M., 1980, The purified product of the transforming gene of avian sarcoma virus phosphorylates tyrosine J. Biol. Chem. 255: 11973–11980.

    PubMed  CAS  Google Scholar 

  • Libermann, T. A., Razon, N., Bartal, A. D., Yarden, Y., Schlessinger, J., and Soreq, M., 1984, Expression of epidermal growth factor receptors in human brain tumors, Cancer Res. 44: 753–760.

    PubMed  CAS  Google Scholar 

  • Linsley, P. S., and Fox, C. F., 1980, Direct linkage of EGF to its receptor. Characterization and biological activity, J. Supramol. Struct. 14:441–.

    Article  PubMed  Google Scholar 

  • Mayes, E. L. V., and Waterfield, M. D., 1984, Biosynthesis of epidermal growth factor receptors in A-431 cells, EMBO J. 3: 531–537.

    PubMed  CAS  Google Scholar 

  • Rubin, J. B., Shia, M. A., and Pilch, P. F., 1983, Stimulation of tyrosine specific phosphorylation in vitro by insulin like growth factor 1, Nature 305: 438–440.

    Article  PubMed  CAS  Google Scholar 

  • Savage, C. R., Jr., and Cohen, S., 1972, Epidermal growth factor and a new derivative, J. Biol. Chem. 247: 7609–7611.

    PubMed  CAS  Google Scholar 

  • Schlessinger, J., Schreiber, A. B., Levi, A., Lax, I., Libermann, T., and Yarden, Y., 1983, Regulation of cell proliferation by epidermal growth factor, CRC Crit. Rev. Biochem. 14: 93–111.

    Article  PubMed  CAS  Google Scholar 

  • Schlessinger, J., Lax, I., Yarden, Y., Kanety, H., and Libermann, T. A., 1984, Monoclonal antibodies against the membrane receptor for epidermal growth factor: A versatile for structural and mechanistic studies, in: Receptors and Recognition (M. Greaves, ed.), Chapman and Hall, London 17: 279–303.

    Google Scholar 

  • Schreiber, A. B., Yarden, Y., and Schlessinger, J., 1981, A non-mitogenic analogue of epidermal growth factor enhances the phosphorylation of endogenous membrane proteins, Biochem. Biophys. Res. Commun. 101: 517–523.

    Article  PubMed  CAS  Google Scholar 

  • Schreiber, A. B., Liberman, T. A., Lax, L, Yarden, Y., and Schlessinger, J., 1983, Biological role of EGF receptor clustering: Investigation with monoclonal anti-EGF receptor antibodies J. Biol. Chem. 258: 846–853.

    PubMed  CAS  Google Scholar 

  • Snyder, M. A., Bishop, J. M., Colby, W. W., and Levinson, A. D., 1983, Phosphorylation of tyrosine 416 is not required for the transforming properties and kinase activity of PP60src, Cell 32: 891–901.

    Article  PubMed  CAS  Google Scholar 

  • Tamura, T., Bauer, H., Birr, C., and Pipkorn, R., 1983, Antibodies against synthetic peptides as a tool for functional analysis of the transforming protein PP60src, Cell 34: 587–596.

    Article  PubMed  CAS  Google Scholar 

  • Ushiro, H., and Cohen, S., 1980, Identification of phosphotyrosine as a product of epidermal growth factor-activated protein kinase in A-431 cell membranes, J. Biol. Chem. 255: 8363–8365.

    PubMed  CAS  Google Scholar 

  • Yarden, Y., Schreiber, A. B., and Schlessinger, J., 1982, A non-mitogenic analogue of EGF induces the early responses mediated by EGF, J. Cell Biol. 92: 687–693.

    Article  PubMed  CAS  Google Scholar 

  • Yarden, Y., Harari, I., and Schlessinger, J., 1985, Purification of EGF receptor from A-431 cells by immunoaffinity chromatography with monoclonal antibody against EGF receptor, J. Biol. Chem. 260: 315–319.

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1985 Plenum Press, New York

About this chapter

Cite this chapter

Schlessinger, J. et al. (1985). The Membrane Receptor for Epidermal Growth Factor. In: Poste, G., Crooke, S.T. (eds) Mechanisms of Receptor Regulation. New Horizons in Therapeutics. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2131-6_3

Download citation

  • DOI: https://doi.org/10.1007/978-1-4613-2131-6_3

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4612-9259-3

  • Online ISBN: 978-1-4613-2131-6

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics