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- W2026306857 abstract "The central domain interface of the HGF referred to as the hinge region is critical for proper ligand (HGF) dimerization and activation. A peptide sequence representing the hinge region acts as a hinge region mimic, by binding directly to HGF and blocking its dimerization. Ligand dimerization is a critical step in activating the HGF/c-Met signaling pathway. And the interference of this unique structure with HGF dimerization translates into inhibition of HGF-dependent signaling, proliferation, and scattering in multiple cell types at concentrations reaching down into the picomolar range. Not only was the hinge peptide sequence capable of inhibiting HGF in-vitro, but it also showed anti-c-Met/anti-cancer activity in an in-vivo study. As expected, it significantly suppresses pulmonary colonization by B16-F10 murine melanoma cells (in C57BL/6 mice), which are characterized by an overactive HGF/c-Met system. This leads to the conclusion that the hinge peptide sequence exerts its anti-cancerous activity through interfering with the HGF/c-Met system, and that more effective HGF/c-Met antagonists can be designed using the hinge region peptide as the parent compound template. The project was funded by Autzen foundation. Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 102nd Annual Meeting of the American Association for Cancer Research; 2011 Apr 2-6; Orlando, FL. Philadelphia (PA): AACR; Cancer Res 2011;71(8 Suppl):Abstract nr 1356. doi:10.1158/1538-7445.AM2011-1356" @default.
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- W2026306857 date "2011-04-15" @default.
- W2026306857 modified "2023-09-26" @default.
- W2026306857 title "Abstract 1356: The Hinge (linker) region of the Hepatocyte Growth Factor (HGF) peptide sequence can act as Hepatocyte Growth Factor/c-Met inhibitor" @default.
- W2026306857 doi "https://doi.org/10.1158/1538-7445.am2011-1356" @default.
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