Epidermal Growth Factor Receptor

The epidermal growth factor receptor (EGFR) family consists of four structurally related transmembrane receptors: EGFR (HER-1 or Erb-B1), HER2neu (c-erbB-2),

HER-3, and HER-4. In response to ligand-specific binding, these receptors act by forming hetero- or homodimers and thereby initiate tyrosine kinase activity in the intracellular domain. The oncogenic pathway of some cells is believed to start as a result of HER2neu and/or EGFR mutation, overexpression, structural rearrangements, and/or relief of normal regulatory or inhibitory pathways. Increased expression of HER2-neu and decreased EGFR membranous staining identified an improved disease-free survival and an overall survival in patients with cervical cancer (39,40). On the other hand, other studies have also revealed no correlation with clinical outcome (41,42). The conflicting results may be because of differences in institutional treatment standards and to the variability of immunohistochemical techniques and the "cut-off" used in the statistical analysis.

Recently, many therapeutic agents targeting this receptor have entered the clinical and phase II trials of both small-molecule inhibitors of EGFR and antibody-based inhibitors underway in cervical cancer. However, emerging data suggest that their activity in unselected women with advanced cancer is very modest, raising the possibility that these agents could be highly effective in a small subset of patients whose tumors are dependent on EGFR signaling.

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