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- W2000560765 abstract "Rationale: Currently approved therapies, including EGFR inhibitors, have minimal effect on survival in pancreatic cancer (PC). HSP90 is a molecular chaperone that specifically enables activity of numerous protein kinases, including EGFR and other signaling proteins. We have reported that simultaneous inhibition of EGFR and HSP90 may be additive in inhibiting cell viability in PC cell lines. Here we report possible molecular mechanisms underlying HSP90 and EGFR inhibition. Methods: MiaPaCa-2 and PANC-1 were treated with EGFR inhibitor, compound 56 (CMP56) (5 − 35 μmol), and HSP90 inhibitor geldanamycin (250 nmol − 1μmol). Growth inhibition was evaluated using the MTT assay, and apoptosis was evaluated by caspase-3 and PARP cleavage. The effect on relevant cell signaling proteins was assessed by immunoblotting with specific antibodies directed against EGFR and effectors such as AKT, STAT-3 and JNK. Results: Growth inhibition was significantly (p Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 101st Annual Meeting of the American Association for Cancer Research; 2010 Apr 17-21; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2010;70(8 Suppl):Abstract nr 1657." @default.
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- W2000560765 date "2010-04-15" @default.
- W2000560765 modified "2023-09-25" @default.
- W2000560765 title "Abstract 1657: HSP90 inhibition down regulates EGFR and its effector signaling proteins in pancreatic cancer cell lines" @default.
- W2000560765 doi "https://doi.org/10.1158/1538-7445.am10-1657" @default.
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