| Autor: |
Tohru Ohmori, Toshio Kuroki, Tsuyoki Kadofuku, Kazuto Nishio, Tomoko Kanome |
| Rok vydání: |
2009 |
| Předmět: |
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| Zdroj: |
New Trends in the Molecular and Biological Basis for Clinical Oncology ISBN: 9784431886624 |
| DOI: |
10.1007/978-4-431-88663-1_14 |
| Popis: |
Non-small cell lung cancer cells expressed mutant EGFR are more sensitive to gefitinib (Iressa) than that expressed wild type EGFR. To elucidate the mechanism of the hypersensitivity to gefitinib in the mutant EGFR, we explored the difference of EGFR-binding proteins between wild type and a 15 bp deletion mutant EGFR using respective stable transfectant cells. EGFR-binding proteins in respective transfectant cells were collected by co-precipitation with polyclonal anti-.EGFR and the co-precipitate proteins were separated by two-dimensional polyacrylamide gel electrophoresis (2D-PAGE). Both co-precipitate proteins showed a similar 2D-PAGE pattern, however, several proteins differed between both transfectant cells. Among these proteins, one protein, detected to high concentration in mutant EGFR tranfectant cells, was identified as heat shock protein 70 (HSP 70) by peptide mass finger printing. Much binding of HSP 70 to mutant EGFR was also confirmed by Western blotting. There was no significant difference of HSP 70 protein expression between both transfectant cells. These results suggest that the difference of HSP70 binding to EGFR may modify the EGFR-downstream signaling and influence the sensitivity to gefitinib. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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