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Papers In Press, published online ahead of print May 19, 2005
Cardiovascular Research Center, Temple University School of Medicine, Philadelphia, PA 19140
Corresponding Author: seguchi{at}temple.edu
A G-protein-coupled receptor agonist, angiotensin II (AngII), induces epidermal growth factor receptor (EGFR) transactivation possibly through a metalloprotease-dependant heparin-binding EGF (HB-EGF) shedding. Here, we have investigated signal transduction of this process by using COS7 cells expressing an AngII receptor, AT1. In these cells, AngII-induced EGFR transactivation was completely inhibited by pretreatment with CRM197, a selective HB-EGF inhibitor, or with a metalloprotease inhibitor. We also developed a COS7 cell line permanently expressing a HB-EGF construct tagged with alkaline phoshatase, which enabled us to measure HB-EGF shedding quantitatively. In the COS7 cell line expressing the AT1 receptor, AngII stimulated release of HB-EGF. This effect was mimicked by treatment either with a phosholipase C (PLC) activator, a Ca2+ ionophore, a metalloprotease activator, or H2O2. Conversely, pretreatment with an intracellular Ca2+ antagonist or an antioxidant blocked AngII-induced HB-EGF shedding. Moreover, infection of adenovirus encoding an inhibitor of Gq or pretreatment of a pharmacological Gq inhibitor markedly reduced EGFR transactivation and HB-EGF shedding through AT1. In this regard, AngII-stimulated HB-EGF shedding was abolished in an AT1 mutant that lacks Gq protein coupling. However, in cells expressing AT1 mutants that retain Gq protein coupling, AngII is still able to induce HB-EGF shedding. Finally, the AngII-induced EGFR transactivation was attenuated in COS7 cells over-expressing catalytically inactive mutant of ADAM17. From these data, we conclude that AngII stimulates a metalloprotease ADAM17-dependent HB-EGF shedding through AT1/Gq/PLC-mediated elevation of intracellular Ca2+ and reactive oxygen species production, representing a key mechanism indispensable for EGFR transactivation.
J. Biol. Chem, 10.1074/jbc.M502906200
Submitted on March 16, 2005
Revised on May 10, 2005
Accepted on May 19, 2005
G protein coupling and second messenger generation are indispensable for a metalloprotease-dependent HB-EGF shedding through angiotensin II type-1 receptor
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