Stoichiometry, Kinetic and Binding Analysis of the Interaction between Epidermal Growth Factor (EGF) and the Extracellular Domain of the EGF Receptor

References

• Alroy I., Yarden Y. The ErbB signaling network in embryogenesis and oncogenesis: signal diversification through combinatorial ligand - receptor interactions. FEBS Letters 1997; 410: 83–86
   PubMed Web of Science ®Google Scholar
• Bellot F., Moolenaar W., Kris R., Mirakhur B., Verlaan I., Ullrich A., Schlessinger J., Felder S. High-affinity epidermal growth factor binding is specifically reduced by a monoclonal antibody, and appears necessary for early responses. J. Cell Biol 1990; 110: 491–502
   PubMed Web of Science ®Google Scholar
• Brown P. M., Debanne M. T., Grothe S., Bergsma D., Caron M., Kay C., O'Connor-McCourt M. D. The extracellular domain of the epidermal growth factor receptor. Eur. J. Biochem 1994; 225: 223–233
   PubMedGoogle Scholar
• Burgess A. W., Knesel J., Sparrow L. G., Nicola N. A., Nice E. C. Two forms of murine epidermal growth factor: rapid separation by using reverse-phase HPLC. Proc. Natl. Acad. Sci. USA 1982; 79: 5753–5757
   PubMedGoogle Scholar
• Catimel B., Nerrie M., Lee F. T., Scott A. M., Ritter G., Welt S., Old L. J., Burgess A. W., Nice E. C. Kinetic analysis of the interaction between the monoclonal antibody A33 and its colonic epithelial antigen by the use of an optical biosensor. A comparison of immobilisation strategies. J. Chromatogr. A 1997; 776: 15–30
   Google Scholar
• Chatelier R. C., Ashcroft R. G., Lloyd C. J., Nice E. C., Whitehead R. H., Sawyer W. H., Burgess A. W. Binding of fluoresceinated epidermal growth factor to A431 cell sub-populations studied using a model-independent analysis of flow cytometric fluorescence data. EMBO. J 1986; 5: 1181–1186
   PubMed Web of Science ®Google Scholar
• Crothe S. BIA symposium 1992: Meeting reviews. Pharmacia Biosensor, Piscataway, NJ 1992; 32–33
   Google Scholar
• Cunningham B. C., Ultsch M., de Vos A. M., Mulkerrin M. G., Clauser K. R., Wells J. A. Dimerization of the extracellular domain of the human growth receptor by a single hormone molecule. Science 1991; 254: 821–825
   PubMed Web of Science ®Google Scholar
• de Vos A. M., Ultsch M., Kossiakoff A. A. Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science 1992; 255: 306–312
   PubMed Web of Science ®Google Scholar
• Defize L. H.K., Boonstra J., Meisenhelder J., Kruijer W., Tertoolen L. G.J., Tilly B. C., Hunter T., van Bergen en Heenegouwen P. M.P., Moolenaar W. H., de Laat S. W. Signal transduction by epidermal growth factor occurs through the subclass of high affinity receptors. J. Cell Biol 1989; 109: 2495–2507
   PubMed Web of Science ®Google Scholar
• Degenhardt M., Weber W., Eschenburg S., Dierks K., Funari S. S., Rapp G., Betzel C. Crystallisation and preliminary X-ray crystallographic analysis of the EGF receptor ectodomain. Acta Cryst 1998; 54: 999–1001
   PubMed Web of Science ®Google Scholar
• Garrett T. P., McKern N. M., Lou M., Frenkel M. J., Bentley J. D., Lovrecz G. O., Elleman T. C., Cosgrove L. J., Ward C. W. Crystal structure of the first three domains of the type-1 insulin-like growth factor receptor. Nature 1998; 394: 395–399
   PubMed Web of Science ®Google Scholar
• Glaser R. W. Antigen-antibody binding and mass transport by convection and diffusion to a surface: a two dimensional computer model of binding and dissociation kinetics. Anal. Biochem 1993; 213: 152–161
   PubMed Web of Science ®Google Scholar
• Greenfield C., Hiles I., Waterfield M. D., Federwisch M., Wollmer A., Blundell T. L., McDonald N. Epidermal growth factor binding induces a conformational change in the external domain of its receptor. EMBO J 1989; 8: 4115–4123
   PubMed Web of Science ®Google Scholar
• Groenen L. C., Nice E. C., Burgess A. W. Structure-function relationships for the EGF/TGF-α Family of Mitogens. Growth Factors 1994; 11: 235–257
   PubMed Web of Science ®Google Scholar
• Gunther N., Betzel C., Weber W. The secreted form of the epidermal growth factor receptor. J. Biol. Chem 1990; 265: 22082–22085
   PubMed Web of Science ®Google Scholar
• Hammacher A., Simpson R. J., Nice E. C. The interleukin-6 (IL-6) partial antagonist (Q159E, T162P) IL6 interacts with the IL-6 receptor and gp130 but fails to induce a stable hexameric receptor complex. J. Biol. Chem 1996; 271: 5464–5413
   Google Scholar
• Han Y., Caday C. G., Nanda A., Cavenee W. K., Huang H.-J. S. Tyrphostin AG 1478 preferentially inhibits human glioma cells expressing truncated rather than wild-type epidermal growth factor receptors. Cancer Re-search 1996; 56: 3859–3861
   PubMed Web of Science ®Google Scholar
• Heldin C.-H. Dimerization of cell surface receptors in signal transduction. Cell 1995; 80: 213–223
   PubMed Web of Science ®Google Scholar
• Hoyt D. W., Harkins R. N., Debanne M. T., O'Connor-McCourt M., Sykes B. D. Interaction of transforming growth factor α with the epidermal growth factor receptor: binding kinetics and differential mobility within the bound TGFα. Biochemistry 1994; 33(15)283–15292
   Google Scholar
• Hurwitz D. R., Emanuel S. L., Nathan M. H., Sarver N., Ullrich A., Felder S., Lax I., Schlessinger J. EGF induces increased ligand binding affinity and dimerization of soluble epidermal growth factor (EGF) receptor extracellular domain. J. Biol. Chem 1991; 266: 22035–22043
   PubMed Web of Science ®Google Scholar
• Hynes N. E., Stern D. F. The biology of erbB2/neu/HER2 and its role in cancer. Biochim. Biophys. Acta 1994; 1198: 165–184
   PubMed Web of Science ®Google Scholar
• Karlsson R. Real-time competitive kinetic analysis of interactions between low-molecular-weight ligands in solution and surface immobilized receptors. Anal. Biochem 1994; 221: 142–451
   PubMed Web of Science ®Google Scholar
• Karlsson R., Roos H., Fagerstam L., Persson B. Kinetic and concentration analysis using BIA technology Methods. A Companion to Methods in Enzymology 1994; 6: 99–110
   Google Scholar
• Karlsson R., Falt A. Experimental design for the kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors. J. Immunol. Methods 1997; 200: 121–133
   PubMed Web of Science ®Google Scholar
• Kawamoto T., Sato J. D., Le A., Polikoff J., Sato G. H., Mendelson J. Growth stimulation of A431 cells by epidermal growth factor: identification of high-affinity receptors for epidermal growth factor by an anti-receptor monoclonal antibody. Prot. Natl. Acad. Sci. USA 1983; 80: 1337–1341
   PubMed Web of Science ®Google Scholar
• King A. C., Cuatrecasas P. Resolution of high and low affinity epidermal growth factor receptor. Inhibition of high affinity component by low temperature, cycloheximide and phorbol esters. J. Biol. Chem 1982; 257: 3053–3060
   PubMed Web of Science ®Google Scholar
• Kohda D., Odaka M., Lax I., Kawasaki H., Suzuki K., Ullrich A., Schlessinger J., Inagaki F. A 40-kDa epidermal growth factor/transforming growth factor α-binding domain produced by limited proteolysis of the extracellular domain of the epidermal growth factor receptor. J. Biol. Chem 1993; 268: 1976–1981
   PubMed Web of Science ®Google Scholar
• Kuziemko G. M., Stroh M., Stevens R. C. Cholera toxin binding affinity and specificity for gangliosides determined by surface plasmon resonance. Biochemistry 1996; 35: 6375–6384
   PubMed Web of Science ®Google Scholar
• Laue T. M., Shah B. D., Ridgeway T. M., Pelletier S. L. Analytical Ultracentrifugation in Biochemistry and Polymer Science, S. E. Harding, A. J. Rowe, J. C. Horton. Royal Society of Chemistry, Cambridge 1992; 90
   Google Scholar
• Lax I., Bellot F., Howk R., Ullrich A., Givol D., Schlessinger J. Functional analysis of the ligand binding site of the EGF-receptor utilizing chimeric chicken/human receptor molecules. EMBO J 1989; 8: 421–427
   PubMed Web of Science ®Google Scholar
• Lax I., Burgess W. H., Bellot F., Ullrich A., Schlessinger J., Givol D. Localization of a major receptor-binding domain for epidermal growth factor by affinity labeling. Mol. Cell. Biol 1988a; 8: 1831–1834
   PubMedGoogle Scholar
• Lax I., Johnson A., Howk R., Sap J., Bellot F., Winkler M., Ullrich A., Vennstrom B., Schlessinger J., Givol D. Chicken epidermal growth factor (EGF) receptor: cDNA cloning, expression in mouse cells and differential binding of EGF and transforming growth factor alpha. Mol. Cell Biol 1988b; 8: 1970–1978
   PubMed Web of Science ®Google Scholar
• Lax I., Fischer R., Ng C., Serge J., Ullrich A., Givol D., Schlessinger J. Noncontiguous regions in the extracellular domain of EGF receptor define ligand-binding specificity. Cell Regul 1991a; 2: 337–345
   PubMedGoogle Scholar
• Lax I., Mitra A. L., Ravera C., Hurwitz D. R., Rubinstein M., Ullrich A., Stroud R. M., Schlessinger J. Epidermal growth factor (EGF) induces oligomerization of soluble, extracellular, ligand-binding domain of EGF Receptor. J. Biol. Chem 1991b; 266: 13828–13833
   PubMed Web of Science ®Google Scholar
• Lemmon M. A., Schlessinger J. Regulation of signal transduction and signal diversity by receptor oligomerization. Trends Biochem. Sci 1994; 11: 459–463
   Google Scholar
• Lemmon M. A., Bu Z., Ladbury J. E., Zhou M., Pinchasi D., Lax I., Engelman D. M., Schlessinger J. Two EGF molecules contribute additively to stabilization of the EGFR dimer. EMBO J 1997; 16: 281–294
   PubMed Web of Science ®Google Scholar
• Lofas S., Johnsson B. A novel hydrogel matrix on gold surfaces in surface plasmon resonance sensors for fast efficient covalent immobilization of ligands. J. Chem. Soc. Chem. Commun 1990; 21: 1526–1528
   Google Scholar
• Mendelsohn J. Potential clinical applications of anti-EGF receptor monoclonal antibodies. Cancer Cells, M. Furth, M. Greaves. Cold Spring Harbor Laboratory press, New York 1989; 395–462
   Google Scholar
• Mendelsohn J. The epidermal growth factor receptor as a target for therapy with antireceptor monoclonal antibodies. Semin. Cancer Biol 1990; 1: 339–344
   PubMedGoogle Scholar
• Minton A. P. Modern Analytical Ultracentrifugation: Acquisition and Interpretation of Data for Biological and Synthetic Polymer Systems, T. M. Schuster, T. M. Laue. Birkhauser, Boston 1994; 81
   Google Scholar
• Morton T. A., Myszka D. G. Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors. Methods Enzymol 1998; 295: 268–294
   PubMed Web of Science ®Google Scholar
• Morton T. A., Myszka D. G., Chaiken I. M. Interpreting complex binding kinetics from optical biosensors: a comparison of analysis by linearization, the inter-grated rate equation, and numerical intergration. Anal. Biochem 1995; 227: 176–185
   PubMed Web of Science ®Google Scholar
• Munson P. J., Rodbard D. Ligand: a versatile computerized approach for characterization of ligand-binding systems. Anal. Biochem 1980; 107: 220–239
   PubMed Web of Science ®Google Scholar
• Nice E. C., Fabri L., Hammacher A., Holden J., Simpson R. J., Burgess A. W. The purification of a Rap1 GTPase-activating protein from bovine brain cytosol. J. Biol. Chem 1992; 267: 1546–1553
   PubMedGoogle Scholar
• Nice E., Lackmann M., Symth F., Fabri L., Burgess A. W. Synergies between micropreparative high-performance liquid chromatography and an instrumental optical biosensor. J. Chromatogr. A 1994; 660: 169–185
   PubMedGoogle Scholar
• Nice E. C., McInerney T. L., Jackson D. C. Analysis of the interaction between a synthetic peptide of influenza virus hemagglutinin and monocolonal antibodies using an optical biosensor. Molecular Immunology 1996a; 33: 659–670
   Google Scholar
• Nice E. C., Smyth F., Domagala T., Fabri L., Catimel B., Burgess A. W. Synergies between micropreparative HPLC and an optical biosensor: Applications to structure function studies. Science Tools 1996b; 3: 3–5
   Google Scholar
• Odaka M., Kodha D., Lax I., Schlessinger J., Inagaki F. Ligand-binding enhances the affinity of dimerization of the extracellular domain of the epidermal growth factor receptor. J. Biochem 1997; 122: 116–121
   PubMed Web of Science ®Google Scholar
• O'Shannessy D. J., Brigham-Burke M., Soneson K. K., Hensley P., Brooks I. Determination of rate and equilibrium binding constants for macromolecular interactions using surface plasmon resonance: use of nonlinear least squares analysis methods. Anal. Biochem 1993; 212: 457–468
   PubMed Web of Science ®Google Scholar
• Panayotou G., Gish G., End P., Troung O., Gout I., Dhand R., Fry M. J., Hiles I., Pawson T., Waterfield M. D. Interactions between SH2 domains and tyrosine-phosphorylated platelet-derived growth factor beta-receptor sequences: analysis of kinetic parameters by a novel biosensor-based approach. Mol. Cell Biol 1993; 13: 3567–3576
   PubMedGoogle Scholar
• Payne G., Shoelson S. E., Gish G. D., Pawson T., Walsh C. T. Kinetics of p561ck and p60src Src homology 2 domain binding to tyrosine-phosphorylated peptides determined by a competition assay or surface plasmon resonance. Proc. Natl. Acad. Sci. USA 1993; 90: 4902–4909
   PubMedGoogle Scholar
• Riese D. J., Stern D. F. Specificity within the EGF family/ErbB receptor family signaling network. BioEssays 1998; 20: 41–48
   PubMed Web of Science ®Google Scholar
• Rousseau D. L., Staros J. V., Beechem J. M. The interaction of epidermal growth factor with its receptor in A431 cell membranes: a stopped-flow fluorescence anisotropy study. Biochemistry 1995; 34: 14508–14518
   PubMed Web of Science ®Google Scholar
• Salomon D. S., Brandt R., Ciardiello F., Normanno N. Epidermal growth factor-related peptides and their receptors in human malignancies. Crit. Rev. Oncol. Hematol 1995; 19: 183–232
   PubMed Web of Science ®Google Scholar
• Scatchard G. The attraction of proteins for small molecules and ions. Ann. N. Y. Acad. Sci 1949; 51: 660–672
   Web of Science ®Google Scholar
• Schlessinger J., Schreiber A. B., Levi A., Lax I., Libermann T., Yarden Y. Regulation of cell proliferation by epidermal growth factor. CRC Crit. Rev. Biochem 1983; 14: 93–111
   PubMed Web of Science ®Google Scholar
• Schuck P., Minton A. P. Kinetic analysis of biosensor data: elementary tests for self consistency. Trends Biochem. Sci 1996; 21: 458–460
   PubMed Web of Science ®Google Scholar
• Simpson R. J., Moritz R. L., Begg G. S., Rubira M. R., Nice E. C. Micropreparative procedures for high sensitivity sequencing of peptides and proteins. Anal. Biochem 1989; 177: 221–236
   PubMed Web of Science ®Google Scholar
• Sizeland A. M., Burgess A. W. Anti-sense transforming growth factor alpha oligonucleotides inhibit autocrine stimulated proliferation of a colon carcinoma cell line. Mol. Biol. Cell 1992; 3: 1235–1243
   PubMed Web of Science ®Google Scholar
• Smith K. D., Davies M. J., Bailey D., Renouf D. V., Hounsell E. F. Analysis of the glycosylation patterns of the extracellular domain of the epidermal growth factor receptor expressed in Chinese hamster ovary fibroblasts. Growth Factors 1996; 13: 121–132
   PubMed Web of Science ®Google Scholar
• Summerfield A. E., Hudnall A. K., Lukas T. J., Guyer C. A., Staros J. V. Identification of residues of the epidermal growth factor receptor proximal to residue 45 of bound epidermal growth factor. J. Biol. Chem 1996; 271: 19656–19659
   PubMed Web of Science ®Google Scholar
• Tzahar E., Pinkas-Kramarski R., Moyer J. D., Klapper L. N., Alroy I., Levkowitz G., Shelly M., Henis S., Eisenstein M., Ratzkin B. J., Sela M., Andrews G. C., Yarden Y. Bivalence of EGF-like ligands drives the ErbB signaling network. EMBO J 1997; 16: 4938–4950
   PubMed Web of Science ®Google Scholar
• Ullrich A., Coussens L., Hayflick J. S., Dull T. J., Gray A., Tam A. J., Yarden Y., Libermann T. A., Schlessinger J., Downward J., Mayes E. L.V., Whittle N., Waterfield M. D., Seeburg P. H. Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells. Nature 1984; 309: 418–425
   PubMed Web of Science ®Google Scholar
• Walker F., Burgess A. W. Reconstitution of the high affinity epidermal growth factor receptor on cell-free membranes after transmodulation by platelet-derived growth factor. J. Biol. Chem 1991; 266: 2746–2752
   PubMed Web of Science ®Google Scholar
• Ward L. D., Howlett G. J., Hammacher A., Weinstock J., Yasukawa K., Simpson R. J., Winzor D. J. Use of a biosensor with surface plasmon resonance detection for the determination of binding constants: measurement of interleukin-6 binding to the soluble interleukin-6 receptor. Biochemistry 1995; 34: 2901–2907
   PubMedGoogle Scholar
• Weber W., Bertics P. J., Gill G. N. Immunoaffinity purification of the epidermal growth factor receptor. J. Biol. Chem 1984; 259: 14631–14636
   PubMedGoogle Scholar
• Weber W., Wenisch E., Gunther N., Marnitz U., Betzel C., Righetti P. G. Protein microheterogeneity and crystal habits: the case of epidermal growth factor receptor isoforms as isolated in a multicompartment electrolyzer with isoelectric membranes. J. Chromatogr. A 1994; 679: 181–189
   PubMed Web of Science ®Google Scholar
• Wenisch E., Righetti P. G., Weber W. Purification to single isoforms of a sectreted epidermal growth factor receptor in a multicompartment electrolyzer with isoelectric membranes. Electrophoresis 1992; 13: 668–673
   Google Scholar
• Winzor D. J., Sawyer W. Quantitative Characterizalion of ligund binding. Wiley-Liss, Inc., New York 1995
   Google Scholar
• Wofsy C., Goldstein B., Lund K., Wiley H. S. Implications of epidermal growth factor (EGF) induced EGF receptor aggregation. Biophys. J 1992; 63: 98–110
   Google Scholar
• Wu D., Wang L., Sat G. H., West K. A., Harris W. R., Crabb J. W., Sato J. D. Human epidermal growth factor (EGF) receptor sequence recognized by EGF competitive monoclonal antibodies. J. Biol. Chem 1989; 264: 17469–17475
   Google Scholar
• Yarden Y., Schlessinger J. Self-phosphorylation of epidermal growth factor receptor: evidence for a model of intermolecular allosteric activation. Biochemistry 1987a; 26: 1434–1442
   PubMed Web of Science ®Google Scholar
• Yarden Y., Schlessinger J. Epidermal growth factor, M. Zhou, S. Felder, M. Rubinstein, D. R. Hurwitz, A. Ullrich, 1987b
   Google Scholar
• Lax I., Schlessinger J. Real-time measurements of growth factor receptor. Biochemistry 1993; 26: 1443–1451, induces rapid, reversible aggregation of the purified epidermal, kinetics of EGF binding to soluble EGF receptor monomers
   Google Scholar
• Yarden Y., Harari I., Schlessinger J. Purification of and dimers support the dimerization model for receptor and active EGF receptor kinase with monoclonal antireceptor activation. Biochemistry 1985; 32: 8193–8198, antibodies. J. Biol. Chem 260, 315–319
   Google Scholar
• Yarden Y., Schlessinger J. Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptor. Biochemistry 1987b; 26: 1443–1451
   PubMed Web of Science ®Google Scholar
• Yarden Y., Harari I., Schlessinger J. Purification of and active EGF receptor kinase with monoclonal antireceptor antibodies. J. Biol. Chem 1985; 260: 315–319
   PubMedGoogle Scholar
• Zhou M., Felder S., Rubinstein M., Hurwitz D. R., Ullrich A., Lax I., Schlessinger J. Real-time measurements of kinetics of EGF binding to soluble EGF receptor monomers and dimers support the dimerization model for receptor activation. Biochemistry 1993; 32: 8193–8198
   PubMed Web of Science ®Google Scholar