Abstract
Abstract Transforming growth factor beta (TGF-β) is a secreted protein that controls cellular proliferation, differentiation, apoptosis, migration, adhesion, immune response, and other functions in most cells. The binding of TGF-β to its receptor, TGFβRII, can lead to activation of both the SMAD-dependent canonical pathway as well as the SMAD-independent non-canonical pathways (such as PI3K/Akt, ERK, JNK, and p38). The TGF-β signaling pathway is coordinately regulated by phosphorylation and understanding the role of this pathway in normal physiological processes and in diseases such as cancer and diabetes requires the ability to simultaneously measure phosphorylation status of multiple protein targets. In recent years, bead-based assays, such as those using Luminex xMAP technology, have enabled the measurement of phosphorylation levels of up to 12 proteins simultaneously. Using the TGF-β Signaling Pathway multiplex panel, we observed increased levels of phosphorylated Smad2 and Smad3, but not phosphorylated ERK or Akt in TGF-β treated cells when compared to their unstimulated counterparts. Modifications in phosphorylation levels were confirmed by the treatment of cells with specific inhibitors against TGFβRI, which blocked phosphorylation of Smad2 and Smad3 in TGF-β treated HepG2 cells. Furthermore, significant increase in phosphorylated Smad3 was observed in human breast cancer versus matched breast normal tissues. The TGF-β Signaling Pathway multiplex panel allowed for simultaneous detection of multiple analytes in both the SMAD-dependent canonical pathway as well as the SMAD-independent non-canonical pathways in a specific, sensitive, and reproducible manner. Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 103rd Annual Meeting of the American Association for Cancer Research; 2012 Mar 31-Apr 4; Chicago, IL. Philadelphia (PA): AACR; Cancer Res 2012;72(8 Suppl):Abstract nr 1237. doi:1538-7445.AM2012-1237
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