Abstract
GPCRs (G-protein coupled receptor) activation of extracellular signal- regulated kinases (ERK) has been extensively explored the last decade and showed a multitude of intracellular pathways involved including the activation of PKC, Ras, raf-1, etc [1]. Recently, it has been demonstrated that some GPCRs such as the lysophosphatidic acid, thrombin, bombesin and angiotensin receptor can activate ERK through the phosphorylation of the epidermal growth factor (EGF) receptor [[2]]. This was mainly done using selective inhibitors of the tyrosine kinase activity of the EGF receptor such as the tyrphostin AG1478. Also, direct demonstration of the phosphorylation of the receptor of EGF in response to these different ligands has been demonstrated [[3]].
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Gallet, C., Blaie, S., Lévy-Toledano, S., Habib, A. (2003). Thromboxane-Induced Erk Phosphorylation in Human Aortic Smooth Muscle Cells. In: Yazici, Z., Folco, G.C., Drazen, J.M., Nigam, S., Shimizu, T. (eds) Advances in Prostaglandin, Leukotriene, and other Bioactive Lipid Research. Advances in Experimental Medicine and Biology, vol 525. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-9194-2_14
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DOI: https://doi.org/10.1007/978-1-4419-9194-2_14
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