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Updated: Jan 27, 2026

Assessment of Resistance to Tyrosine Kinase Inhibitors by an Interrogation of Signal Transduction Pathways by Antibody Arrays
Published on: September 19, 2018
alpha-Thrombin activates Akt via a nonreceptor tyrosine kinase in IIC9 cells
Polly J Phillips-Mason1, Reema Goel, Joseph J Baldassare
1Departments of Cell and Molecular Biology, and Pharmacological and Physiological Sciences, St. Louis University School of Medicine, St. Louis, Missouri 63104, USA.
Abstract:
Previous data from our laboratory show that PI 3-kinase is required for alpha-thrombin-stimulated G(1) progression in IIC9 cells. In IIC9 cells, PI 3-kinase acts downstream of Ras to activate Akt, in a pathway parallel to ERK1. Here we show that alpha-thrombin does not transactivate either the EGF receptor or the PDGF receptor as measured by tyrosine phosphorylation, suggesting that activation of PI 3-kinase by alpha-thrombin is not the result of an RTK. Interestingly, both genistein and PP1 block alpha-thrombin-stimulated Akt phosphorylation, suggesting the involvement of a member of the Src family of nonreceptor tyrosine kinases.
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