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Epidermal growth factor receptor (EGFR); heat shock protein 90 (Hsp90)

In vitro studies identified a peptide fragment from EGFR that could help treat cancer. EGFR is stabilized by Hsp90 through binding at an eight-amino-acid segment on the receptor. In EGFR-dependent head and neck cancer cells, an EGFR peptide fragment that competes with EGFR binding to Hsp90 caused specific degradation of EGFR. In head and neck cancer cells and non-small cell lung cancer (NSCLC) cells, the peptide inhibited a dimerization process required for EGFR activation and decreased cancer cell survival compared with a scrambled control peptide. Next steps could include testing the peptide in animal models of cancer.
Synta Pharmaceuticals Corp.'s Hsp90 inhibitor, ganetespib, is in Phase III testing to treat NSCLC.
At least 13 other companies have Hsp90 inhibitors in Phase II testing or earlier to treat various cancers.

SciBX 6(34); doi:10.1038/scibx.2013.920
Published online Sept. 5, 2013

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Ahsan, A. et al. J. Biol. Chem.; published online July 29, 2013;
Contact: Mukesh K. Nyati,
The University of Michigan Medical School, Ann Arbor, Mich.