Tyrphostins inhibit the epidermal growth factor receptor-mediated breakdown of phosphoinositides.
In response to epidermal growth factor (EGF) and the Ca2+ ionophore A23187, the total phosphatidylinositides ( IPT) increased in A431 human epidermoid carcinoma cells 1.8- and 2.0-fold and in the EGF-dependent A431/Clone 15-2 cells 3.0- and 8.0-fold, respectively, over basal levels. Both responses were inhibited by the antiproliferative agents tyrphostins, but the EGF- induced increase in IPT was inhibited to a much greater extent than that induced by the ionophore. Tyrphostins which are potent EGF-receptor kinase inhibitors were also potent in blocking the EGF-induced production of phosphoinositides. The less potent tyrphostins were found to inhibit the EGF-dependent IPT formation more weakly. These results support the notion that phospholipase C is activated through its phosphorylation by the EGF receptor.[1]References
- Tyrphostins inhibit the epidermal growth factor receptor-mediated breakdown of phosphoinositides. Posner, I., Gazit, A., Gilon, C., Levitzki, A. FEBS Lett. (1989) [Pubmed]
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