Lung cancer is the number one cause of cancer-related death involving excessive cell growth in epithelial tissues lining the lungs. Non-small cell lung cancer (NSCLC) is the most prevalent form of lung cancer. Genome-wide association studies provide insight into NSCLC. Single nucleotide polymorphism variations on chromosomes 15q24 and 15q25 lead to increased risk of NSCLC. Also, two tyrosine kinase receptors, epidermal growth factor receptor (EGFR) and human epidermal growth factor receptor 2 (HER2 / ERBB2), have mutated kinase domains associated with NSCLC. Proteins with Src homology 2 (SH2) and phosphotyrosine domains interact with EGFR and ERBB2, allowing proteins to bind to phosphotyrosine residues. Two of these proteins containing phosphotyrosine residues are vascular endothelial growth factor-A (VEGF-A) and platelet-derived growth factor receptor- ß (PDGFR-ß). These are present in the PI3K/Akt pathway involving angiogenic proteins p85 and p110. There are several drugs that inhibit these signaling pathways. Gefitinib inhibits the phosphorylation of mutant EGFR and ERBB2 receptors. Multiple mutations on kinase domains of EGFR and ERBB2 lead to higher Gefitinib sensitivity. Imatinib decreases phosphorylation of PDGFR-ß and VEGF-A, reducing tumor cell proliferation and cisplatin activates a signal-transduction pathway causing apoptosis of tumor cells involving p53 and p73 signaling pathways.
Eukaryon is published by students at Lake Forest College, who are solely responsible for its content. The views expressed in Eukaryon do not necessarily reflect those of the College. Articles published within Eukaryon should not be cited in bibliographies. Material contained herein should be treated as personal communication and should be cited as such only with the consent of the author.