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Papers In Press, published online ahead of print November 12, 2002
Department of Pathology, The University of Tennessee, Knoxville, TN 37996
Corresponding Author: cuim{at}utk.edu
Thrombin plays a critical role in hemostasis, thrombosis and inflammation. However, the responsible intracellular signaling pathways triggered by thrombin are still not well defined. We report here that thrombin rapidly and transiently induces activation of protein kinase D (PKD) in aortic smooth muscle cells. Our data demonstrate that PKC inhibitors completely block thrombin-induced PKD activation, suggesting that thrombin induces PKD activation, via a PKC-dependent pathway. Furthermore, our results show that thrombin rapidly induces PKCdelta phosphorylation and that PKCdelta-specific inhibitor rottlerin blocks thrombin-induced PKD activation, suggesting that PKCdelta mediates the thrombin-induced PKD activation. Using dominant negative approaches, we demonstrated that expression of a dominant negative PKCdelta inhibits the phosphorylation and activation of PKD induced by thrombin, whereas neither PKCepsilon nor PKCzeta affected thrombin-induced PKD activation. In addition, our results of co-immunoprecipitaion assay showed that PKD forms a complex with PKCdelta in smooth muscle cells. Taken together, the present study demonstrates that thrombin induces activation of PKD and reveals a novel role of PKCdelta in mediating thrombin-induced PKD activation in vascular smooth muscle cells.
J. Biol. Chem, 10.1074/jbc.M211523200
Submitted on November 12, 2002
Revised on November 12, 2002
Accepted on November 12, 2002
Thrombin rapidly induces protein kinase D phosphorylation and protein kinase C delta mediates the activation
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