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EGFR SIGNALING
Epidermal growth factor receptor is a cell surface receptor family containing four structurally related members (erb1/EGFR, erb2/HER2, erb3/HER3 and erb4/HER4). There are three basic components that make up this single polypeptide chain receptor: the extracellular ligand binding domain, the transmembrane segment and an intracellular protein tyrosine kinase (PTK) domain comprising the catalytic core and the regulatory sequences.
Upon binding of an extracellular ligand the receptor transforms the inactive monomers into homodimers (exception: the tetrametric insulin receptor) that activate its intracellular tyrosine kinase domain and autophosphorylate its C-terminal tyrosine residues. This stabilizes the active receptor conformation and creates phosphotyrosine-docking sites for proteins that transduce signals within the cell.
Transduction by activated EGFR leads to downstream effect on proteins including phosphatidyl 3-kinase (PI3K), Phospholipase (PL) C-g1, Akt, Ras, Raf and mitogen-activated protein kinase (MAPK); entities that are associated with cell proliferation, motility and survival.
REVIEW ARTICLES
- EGFR inhibitors as first-line therapy in EGFR mutation-positive patients with NSCLC, Kimberly J Gorden, Parvin Mesbah, and Jill M Kolesar. Journal of Oncology Pharmacy Practice, Jun 2012; 18: 245 – 249.
- Anti-EGFR Monoclonal Antibodies for Treatment of Colorectal Cancers: Development of Cetuximab and Panitumumab., Benoit You and Eric X. Chen. J. Clin. Pharmacol., Feb 2012; 52: 128 - 155.
- Targeting the HER/EGFR/ErbB Family to Prevent Breast Cancer., Louise R. Howe and Powel H. Brown. Cancer Prevention Research, Aug 2011; 4: 1149 - 1157.
- Risk of venous and arterial thromboembolic events associated with anti-EGFR agents: a meta-analysis of randomized clinical trials., F. Petrelli, M. Cabiddu, K. Borgonovo, and S. Barni. Ann. Onc., Jul 2012; 23: 1672 - 1679.
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