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Am J Physiol Cell Physiol (March 27, 2002). doi:10.1152/ajpcell.00261.2001
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Articles in PresS, published online ahead of print March 27, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00261.2001
Submitted on June 12, 2001
Accepted on March 20, 2002

TRANSACTIVATION OF EGF RECEPTOR IS AN OBLIGATORY EVENT FOR STIMULATION OF PROTEIN SYNTHESIS BY G PROTEIN-COUPLED RECEPTORS IN VASCULAR SMOOTH MUSCLE

Laure Voisin1, Sylvain Foisy1, Edith Giasson1, Chantal Lambert2, Pierre Moreau3, and Sylvain Meloche4*

1 Institut de recherches cliniques de Montreal, Montreal, Quebec, Canada
2 Pharmacology, University of Montreal, Montreal, Quebec, Canada
3 Faculty of Pharmacy, University of Montreal, Montreal, Quebec, Canada
4 Institut de recherches cliniques de Montreal, Montreal, Quebec, Canada; Pharmacology, University of Montreal, Montreal, Quebec, Canada

* To whom correspondence should be addressed. E-mail: melochs{at}ircm.qc.ca.

The epidermal growth factor receptor (EGFR) was recently identified as a signal transducer of G protein-coupled receptors (GPCRs). In this study, we have examined the contribution of EGFR transactivation to the growth-promoting effect of GPCRs on vascular smooth muscle cells. Activation of the Gq-coupled angiotensin II receptor or Gi-coupled lysophosphatidic acid receptor resulted in increased tyrosine phosphorylation and activation of EGFR. Specific inhibition of EGFR kinase activity by tyrphostin AG1478 or expression of a dominant-negative EGFR mutant abolished this response. Importantly, inhibition of EGFR function strongly attenuated the global stimulation of protein synthesis by GPCR agonists in vitro in cultured aortic smooth muscle cells and in vivo in the rat aorta and in small resistance arteries. The growth inhibition was associated with a marked reduction of extracellular signal-regulated kinase and phosphoinositide 3-kinase pathways activity, and the resulting suppression of eukaryotic translation initiation factor 4E and 4E-binding protein 1 phosphorylation. Our results demonstrate that EGFR transactivation is a physiologically relevant action of GPCRs linked to translational control and protein synthesis.




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