English Version
Cancer cells may acquire the capacity for autonomous and dys regulated proliferation through the uncontrolled production of specif ic molecules that promote cell growth (growth factors) or through abnormal, enhanced expression of specfic proteins (growthfactor receptors) on the cell membranes to which growth factors selectively bind. Both processes trigger a series of intracellular signals that ultimately lead to the proliferation of cancer cells, induction of angiogenesis, and metastasis. The majority of human epithelial cancers are marked by functional activation of growth factors and receptors of the epidermal growth factor receptor (EGFR) family. Given this phenomenon, EGFR was the first growth factor receptor to be proposed as a target for cancer therapy. Af ter 20 years of drug development, four EGFR antagonists are currently available for the treatment of four metastat ic epithelial cancers: non–small-cell lung cancer, squamous-cell carcinoma of the head and neck, colorectal cancer, and pancreatic cancer. Less informat ion is avai lable about the use of EGFR antagonists in the treatment of earlier stages of cancer. This article summarizes the mechanisms of action of EGFR inhibitors, presents the clinical evidence of their anticancer activity, and considers the current, and controversial, clinical issues with respect to their optimal use in the treatment of patients with cancer.
EGFR in Human Carcinogenesis
EGFR is a transmembrane receptor belonging to a family of four related proteins (Fig. 1). Ten different ligands can selectively bind to each receptor. After a ligand binds to a single chain EGFR, the receptor forms a dimer3 that signals within the cell by activating receptor autophosphorylation through tyrosine kinase activity. Autophosphorylation triggers a series of intracellular pathways that may result in cancer-cell proliferation, blocking apoptosis, activating invasion and metastasis, and stimulating tumor-induced neovascularization.
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EGFR is a transmembrane receptor belonging to a family of four related proteins (Fig. 1). Ten different ligands can selectively bind to each receptor. After a ligand binds to a single chain EGFR, the receptor forms a dimer3 that signals within the cell by activating receptor autophosphorylation through tyrosine kinase activity. Autophosphorylation triggers a series of intracellular pathways that may result in cancer-cell proliferation, blocking apoptosis, activating invasion and metastasis, and stimulating tumor-induced neovascularization.
Journals for full download on the link below
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