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New insights into novel mechanisms of action of Genmab's HuMax-EGFr

14 Mar 2007 - Genmab A/S announced new insights into the novel mechanisms of action of its antibody HuMax-EGFr(TM) (zalutumumab). By using Protein Tomography(TM), a relatively new technology which uses an electron microscope to view the three dimensional structure of proteins on the surface of cells, HuMax-EGFr was shown to lock the EGF receptor in an inactive conformation which prevents receptor activation and the binding of growth factors. Furthermore, HuMax-EGFr was shown to inhibit EGF receptor signaling by preventing receptor dimerization, the pairing of two receptor molecules which starts the signaling cascade. All of these mechanisms have the potential to interfere with cancer cell growth.
 
"Coupled with previous findings that HuMax-EGFr is able to induce potent ADCC and block growth factor binding to EGF receptors, these studies have given us greater insight into the novel way HuMax-EGFr works," said Lisa N. Drakeman, Ph.D., Chief Executive Officer of Genmab.