Advertisement

Epidermal Growth Factor (EGF) as a Potential Targeting Agent for Delivery of Boron to Malignant Gliomas

  • Jacek Capala
  • Rolf F. Barth
  • Dianne M. Adams
  • Michael Q. Bailey
  • Albert H. Soloway
  • Jörgen Carlsson

Abstract

The majority of high grade gliomas express an amplified epidermal growth factor receptor (EGFR) gene, and this often is associated with an increase in cell surface receptor expression1,2.

Keywords

Epidermal Growth Factor Receptor Glioma Cell Malignant Glioma Boron Atom Intratumoral Injection 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. I. H. Modjtahedi and C. Dean, The receptor for EGF and its ligands: expression, prognostic value and target for therapy in cancer (Review), Int. J. Oncol. 4: 227–296, 1994.Google Scholar
  2. 2.
    S.H. Trop, E.Helseth, A. Dalen and G. Unsgaard, Epidermal growth factor receptor expression in human gliomas, Cancer Immunol. Immunother 33: 61–63, 1991.CrossRefGoogle Scholar
  3. 3.
    J. Capala, R.F. Barth, D.M. Adams, A.H. Soloway and J. Carlsson. Epidermal growth factor as a potential targeting agent for delivery of 10B to malignant gliomas, in “Advances of Neutron capture Therapy” A.H. Soloway, R.F. Barth, D.E. Carpenter, eds. Plenum Press, N.Y., 1993, pp. 371–375.Google Scholar
  4. 4.
    R.A. Fenstermaker, J. Capala, R.F. Barth, A. Hujer, H.-J. Kung and D.M. Kaetzel Jr., The effect of epidermal growth factor receptor (EGFR) expression on in vivo growth of rat 3’6 glioma cells. Leulemia A. Suppl. L 5106–5112, 1995.Google Scholar
  5. 5.
    R.F. Barth, D.M. Adams, A.H. Soloway, F. Alam and M.V. Darby, Boronated starburst dendrimer-monoclonal antibody immunoconjugates: evaluation as a potential delivery system for neutron capture therapy. Bioconjug. Chem. 5: 58–66, 1994.PubMedCrossRefGoogle Scholar
  6. 6.
    B.A. Bidlingmeyer, S.A. Cohen and T.L. Tarvin Rapid analysis of amino acids using pre-column derivatization, J. Chromatography 336: 93–104, 1984.Google Scholar
  7. 7.
    S.A. Cohen, T.L. Tarvin and B.A. Bidlingmeycr, Amino acid analysis using pre-column derivatization with phenylisothiocyanate: Matrix effects and tryptophan analysis, in: “Proteins: Structure and Function”, J.J. L’Italien ed. Plenum Press, NY, 1987, pp. 207–213.Google Scholar
  8. 8.
    P.J. Munson, Heterogenous receptors and binding curve analysis in neurobiology, in: “Brain Receptor Methodologies, Part A: General Methods and Concepts. Amines and Acetylcholine”, P.J. Marangos, I.C.Campbell and R.M. Cohen, eds. Academic Press, Inc., New York, NY, 1954, pp. 33–45.Google Scholar
  9. 9.
    B.A. Rhodes, Direct labeling of proteins with “”’Tc, Nucl.: tied. Biol. 18: 667–676, 1991.Google Scholar
  10. 10.
    O.A. Oredipe, R.F. Barth, J.H. Rotaru and Z. Steplewski, Lack of effect of recombinant human interferon-2b on expression of 17–1A antigen on human colon cancer cells, Ilrhridorna l. 1: 607–615, 1992.Google Scholar

Copyright information

© Springer Science+Business Media New York 1996

Authors and Affiliations

  • Jacek Capala
    • 1
  • Rolf F. Barth
    • 1
  • Dianne M. Adams
    • 1
  • Michael Q. Bailey
    • 2
  • Albert H. Soloway
    • 3
  • Jörgen Carlsson
    • 4
  1. 1.Department of PathologyThe Ohio State UniversityColumbusUSA
  2. 2.Department of Veterinary Clinical ScienceThe Ohio State UniversityColumbusUSA
  3. 3.College of PharmacyThe Ohio State UniversityColumbusUSA
  4. 4.Department of Radiation SciencesUppsala UniversityUppsalaSweden

Personalised recommendations