TY - JOUR
T1 - Resistance to EGFR-TKI can be mediated through multiple signaling pathways converging upon cap-dependent translation in EGFR-wild type NSCLC
AU - Patel, Manish R
AU - Jay-Dixon, Joe
AU - Sadiq, Ahad A.
AU - Jacobson, Blake A
AU - Kratzke, Robert A
N1 - Funding Information:
This work was funded, in part, by the National Institutes of Health (5 T32 HL07062).
PY - 2013/9
Y1 - 2013/9
N2 - Introduction: For the majority of patients with non-small-cell lung cancer (NSCLC), response to epidermal growth factor receptor tyrosine kinase inhibitors (EGFR-TKIs) is suboptimal. In models of acquired resistance to EGFR-TKI, activation of Akt phosphorylation is frequently observed. Because Akt activation results in downstream initiation of cap-dependent protein translation, we hypothesized that a strategy of targeting cap-dependent translation in combination with erlotinib might enhance therapy. Methods: NSCLC cells that are wild type for EGFR were assayed for sensitivity to erlotinib. Serum-starved NSCLC cells were assayed for EGFR signaling and downstream pathway activation by immunoblot after stimulation with epidermal growth factor. EGFR signaling and signaling mediators of cap-dependent translation were assayed by immunoblot under serum-replete conditions 24 hours after treatment with erlotinib. Finally, combination treatment with erlotinib and two different cap-dependent translation inhibitors were done to assess the effect on cell viability. Results: EGFR signaling is coupled to activation of cap-dependent translation in EGFR wild-type cells. Erlotinib inhibits EGFR phosphorylation in EGFR-TKI resistant cells, however, results in activation of downstream signaling molecules including Akt and extracellular regulated kinase, ERK 1/2, resulting in maintenance of eukaryotic initiation factor 4F (eIF4F) activation. eIF4F cap-complex formation is maintained in erlotinib-resistant cells, but not in erlotinib-sensitive cells. Finally, using an antisense oligonucleotide against eukaryotic translation initiation factor 4E and a small-molecule inhibitor to disrupt eIF4F formation, we show that cap-dependent translation inhibition can enhance sensitivity to erlotinib. Conclusion: The results of these studies support further clinical development of translation inhibitors for treatment of NSCLC in combination with erlotinib.
AB - Introduction: For the majority of patients with non-small-cell lung cancer (NSCLC), response to epidermal growth factor receptor tyrosine kinase inhibitors (EGFR-TKIs) is suboptimal. In models of acquired resistance to EGFR-TKI, activation of Akt phosphorylation is frequently observed. Because Akt activation results in downstream initiation of cap-dependent protein translation, we hypothesized that a strategy of targeting cap-dependent translation in combination with erlotinib might enhance therapy. Methods: NSCLC cells that are wild type for EGFR were assayed for sensitivity to erlotinib. Serum-starved NSCLC cells were assayed for EGFR signaling and downstream pathway activation by immunoblot after stimulation with epidermal growth factor. EGFR signaling and signaling mediators of cap-dependent translation were assayed by immunoblot under serum-replete conditions 24 hours after treatment with erlotinib. Finally, combination treatment with erlotinib and two different cap-dependent translation inhibitors were done to assess the effect on cell viability. Results: EGFR signaling is coupled to activation of cap-dependent translation in EGFR wild-type cells. Erlotinib inhibits EGFR phosphorylation in EGFR-TKI resistant cells, however, results in activation of downstream signaling molecules including Akt and extracellular regulated kinase, ERK 1/2, resulting in maintenance of eukaryotic initiation factor 4F (eIF4F) activation. eIF4F cap-complex formation is maintained in erlotinib-resistant cells, but not in erlotinib-sensitive cells. Finally, using an antisense oligonucleotide against eukaryotic translation initiation factor 4E and a small-molecule inhibitor to disrupt eIF4F formation, we show that cap-dependent translation inhibition can enhance sensitivity to erlotinib. Conclusion: The results of these studies support further clinical development of translation inhibitors for treatment of NSCLC in combination with erlotinib.
KW - Cap-dependent translation
KW - Epidermal growth factor receptor
KW - Erlotinib
KW - Eukaryotic translation initiation factor 4E
KW - Non-small-cell lung cancer
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U2 - 10.1097/JTO.0b013e31829ce963
DO - 10.1097/JTO.0b013e31829ce963
M3 - Article
C2 - 23883783
AN - SCOPUS:84883453155
SN - 1556-0864
VL - 8
SP - 1142
EP - 1147
JO - Journal of Thoracic Oncology
JF - Journal of Thoracic Oncology
IS - 9
ER -