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- W2331428818 abstract "Transforming growth factor-β (TGF-β) is a multifunctional cytokine that plays important roles in a variety of physiological processes including cell proliferation, differentiation, and apoptosis. Dysregulation of TGF-β signaling has been implicated in the pathogenesis of a variety of diseases including cancer; therefore, pharmacological inhibitors that target the TGF-β signaling pathway might be promising drugs for disease therapy. In this study, we investigated the mechanism of inhibition of TGF-β signaling by the Hsp90 inhibitor geldanamycin (GA). Treatment with GA suppressed TGF-β signaling, as evidenced by inhibition of TGF-β-induced phosphorylation and transcriptional activity of Smad3 and decreased induction of target genes. Western blot analysis revealed that GA induced degradation of TGF-β type I and type II receptors through a proteasome-dependent pathway. Hsp70 interacted directly with TGF-β receptors following GA treatment. Notably, induction of Hsp70 by GA correlated with inhibition of TGF-β signaling. Suppression of Hsp70 expression by Hsp70 siRNA or KNK437, an inhibitor of Hsp70 synthesis, blocked the inhibition of TGF-β signaling by GA. Furthermore, down-regulation of endogenous Hsp70 enhanced TGF-β induced transcriptional activity and cell cycle arrest. These results strongly suggest that GA-induced Hsp70 acts as a negative regulator of TGF-β signaling. 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 3965." @default.
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- W2331428818 date "2010-04-15" @default.
- W2331428818 modified "2023-09-27" @default.
- W2331428818 title "Abstract 3965: Geldanamycin-induced heat shock protein 70 negatively regulates TGF-β signaling through interaction with TGF-β receptors" @default.
- W2331428818 doi "https://doi.org/10.1158/1538-7445.am10-3965" @default.
- W2331428818 hasPublicationYear "2010" @default.
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