Individualized Tissue Analysis for EGFR-dependent Phosphoproteomic Signature in Non-small-cell Lung Cancer

摘要

The abnormal protein kinase activity with its corresponding change in protein phosphorylation states has been implicated in tumor formation and cancer progression. The discovery of aberrant phosphorylation can lead to the design of kinase inhibitor, such as gefitinibtargeting mutated EGFR for cancer treatment. A sensitive quantitative phosphoproteomicsignature analysis is helpful to find such tissue signature for different EGFR-dependent cancer subtypes, which may subsequently facilitate the identification of drug target candidate.in attempt to discover an alternative drug target, the patient tissue samples of wild-type EGFR or different mutation status, Del19-EGFR and L858R-EGFR are analyzed for the phosphorylation-mediated signaling networks and their interplay.