EGFR Inhibition in Non-Small Cell Lung Cancer Resistance, Once Again, Rears Its Ugly Head 英文参考文献.docVIP

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EGFR Inhibition in Non-Small Cell Lung Cancer Resistance, Once Again, Rears Its Ugly Head 英文参考文献.doc

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EGFR Inhibition in Non-Small Cell Lung Cancer Resistance, Once Again, Rears Its Ugly Head 英文参考文献

Open access, freely available online Perspectives EGFR Inhibition in Non-Small Cell Lung Cancer: Resistance, Once Again, Rears Its Ugly Head Jennifer Clark, Jan Cools, D. Gary Gilliland* Kinase Inhibition for Treatment of Cancer tyrosine kinases. As a consequence, there have been additional dividends from the United States Federal Drug Administration approval of imatinib for treatment of BCR-ABL-positive CML. For example, imatinib is effective in treatment of chronic myelomonocytic leukemia with gene rearrangements More recently, this paradigm has been extended to treatment of non- small cell lung cancer (NSCLC). Several mutations have been identi?ed in the context of epidermal growth factor receptor (EGFR) in patients with NSCLC that are associated with clinical response to the small-molecule EGFR inhibitors ge?tinib (Iressa) or erlotinib (Tarceva) [7,8,9], including in-frame deletions such as del L747–E749;A750P in exon 19, or L858R in exon 21. Although responses are often dramatic, most responding patients ultimately develop clinical resistance and relapse of disease [7,8,9]. The basis for Uncontrolled proliferation of tumor cells is a hallmark of cancer. In many types of cancer, mutations in genes that activate cellular signal transduction pathways contribute to enhanced proliferation and survival of cancer cells. One well-characterized example is mutation in tyrosine kinases, enzymes that regulate the growth and survival of cells. Tyrosine kinase activity is tightly regulated in normal cells, but is dysregulated due to mutation in some cancers, including lung cancer, resulting in enhanced proliferation and survival of cancer cells. The tyrosine kinases are attractive candidates for molecularly targeted therapy in cancer, because cancers become dependent on growth signals from the mutant tyrosine kinases. Tyrosine kinases require ATP for their enzymic activity, and thus small molecules that mimic ATP can bind to mutant kinases and inactivate them. The pa