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Originally published In Press as doi:10.1074/jbc.M211523200 on November 12, 2002

J. Biol. Chem., Vol. 278, Issue 5, 2824-2828, January 31, 2003
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Thrombin Rapidly Induces Protein Kinase D Phosphorylation, and Protein Kinase C delta  Mediates the Activation*

Mingqi TanDagger , Xuemin XuDagger , Motoi Ohba§, Wataru Ogawa, and Mei-Zhen CuiDagger ||

From the Dagger  Department of Pathology, University of Tennessee, Knoxville, Tennessee 37996, the § Institute of Molecular Oncology, Showa University, Shinagawa-ku, Tokyo 142-8555, Japan, and the  Department of Clinical Molecular Medicine, Kobe University, Kobe 650-0017, Japan

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 protein kinase C (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 the 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 affects thrombin-induced PKD activation. In addition, our results of co-immunoprecipitation assays showed that PKD forms a complex with PKCdelta in smooth muscle cells. Taken together, the findings of the present study demonstrate that thrombin induces activation of PKD and reveal a novel role of PKCdelta in mediating thrombin-induced PKD activation in vascular smooth muscle cells.

* This work was supported by American Heart Association Scientist Development Grant 9730039N (to M.-Z. C.) and National Institutes of Health Grant NS42314 (to X. X.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed: Dept. of Pathology, University of Tennessee, College of Veterinary Medicine, 2407 River Dr., Knoxville, TN 37996. Tel.: 865-974-8212; Fax: 865-974-5616; E-mail: cuim@utk.edu.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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