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Originally published In Press as doi:10.1074/jbc.M205997200 on August 26, 2002

J. Biol. Chem., Vol. 277, Issue 44, 41850-41856, November 1, 2002
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Proteolytic Activation of Protein Kinase C-epsilon by Caspase-mediated Processing and Transduction of Antiapoptotic Signals*

Alakananda BasuDagger , Dongmei Lu, Baohua Sun§, Andrea N. Moor, Giridhar Rao Akkaraju, and Jie Huang

From the Department of Molecular Biology and Immunology, University of North Texas Health Science Center, Fort Worth, Texas 76107

Several novel protein kinase C (PKC) isozymes have been identified as substrates for caspase-3. We have previously shown that novel PKCepsilon is cleaved during apoptosis in MCF-7 cells that lack any functional caspase-3. In the present study, we show that in vitro-translated PKCepsilon is processed by human recombinant caspase-3, -7, and -9. Tumor necrosis factor-alpha (TNF) triggered processing of PKCepsilon to a 43-kDa carboxyl-terminal fragment, and cell-permeable caspase inhibitors prevented TNF-induced processing of PKCepsilon in MCF-7 cells. PKCepsilon was cleaved primarily at the SSPDdown-arrow G site to generate two fragments with an approximate molecular mass of 43 kDa. It was also cleaved at the DDVDdown-arrow C site to generate two fragments with molecular masses of 52 and 35 kDa. Treatment of MCF-7 cells with TNF resulted in the activation of PKCepsilon , and mutation at the SSPDdown-arrow G (D383A) site inhibited proteolytic activation of PKCepsilon . Overexpression of wild-type but not dominant-negative PKCepsilon in MCF-7 cells delayed TNF-induced apoptosis, and mutation at the D383A site prevented antiapoptotic activity of PKCepsilon . These results suggest that cleavage of PKCepsilon by caspase-7 at the SSPDdown-arrow G site results in the activation of PKCepsilon . Furthermore, activation of PKCepsilon was associated with its antiapoptotic function.

* This work was supported by Grants CA71727 (to A. B.) and CA85682 (to A. B.) from the NCI, National Institutes of Health.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.

Dagger To whom correspondence should be addressed: Dept. of Molecular Biology and Immunology, University of North Texas Health Science Center, 3500 Camp Bowie Blvd., Fort Worth, TX 76107. Tel.: 817-735-2487; Fax: 817-735-2118; E-mail: abasu@hsc.unt.edu.

§ Present address: Departments of Surgery and Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030.

Present address: Dept. of Biology, Texas Christian University, Forth Worth, TX 76129.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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