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Am J Physiol Cell Physiol (January 26, 2005). doi:10.1152/ajpcell.00499.2004
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Submitted on October 12, 2004
Accepted on January 18, 2005

PKC{delta}-DEPENDENT PATHWAYS CONTRIBUTE TO PDGF-STIMULATED ERK1/2 ACTIVATION IN VASCULAR SMOOTH MUSCLE

Roman Ginnan1 and Harold A. Singer1*

1 Cardiovascular Sciences, Albany Medical College, Albany, NY, USA

* To whom correspondence should be addressed. E-mail: singerh{at}mail.amc.edu.

Platelet derived growth factor (PDGF) is an important regulator of vascular smooth muscle cell growth and migration and has been identified as a key mediator of neointima formation resulting from vascular injury. PDGF exerts its effects, in part, through activation of ERK1/2. Previously, we reported that PKC{delta}, specifically compared to PKC{alpha}, mediated phorbol ester- and ATP-dependent activation of ERK1/2 in VSM cells. The purpose of this study was to determine whether PKC{delta} was involved in PDGF-dependent activation of ERK1/2 in VSM cells. Addition of PDGF resulted in the activation, and src family kinase-dependent tyrosine phosphorylation, of PKC{delta}. Treatment with rottlerin (0.1-10 µM), a selective PKC{delta} inhibitor, or adenoviral overexpression of kinase-negative PKC{delta} significantly attenuated PDGF-induced activation of ERK1/2. Effects of the PKC{delta} inhibitors decreased with increasing concentrations of activator PDGF. Interestingly, treatment with Go6976 (0.1-3 µM), a selective inhibitor of cPKCs, or adenoviral overexpression of kinase-negative PKC{alpha} also inhibited PDGF-stimulated ERK1/2. Furthermore, inhibition of cPKC activity with Go6976 or overexpression of kinase-negative PKC{alpha} attenuated PKC{delta} activation and tyrosine phosphorylation in response to PDGF. These studies indicate involvement of both PKC{delta} and PKC{alpha} isozymes in PDGF-stimulated signaling in VSM and suggest an unexpected role for PKC{alpha} in the regulation of PKC{delta} activity.




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