The Journal of Experimental Medicine
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J. Exp. Med.
© The Rockefeller University Press
0022-1007/96/12/2399/06 $2.00
Volume 184 December 1996 2399-2404

BRIEF DEFINITIVE REPORT:
Proteolytic Activation of Protein Kinase C delta  by an ICE/CED 3-like Protease Induces Characteristics of Apoptosis

By Tariq Ghayur,* Margaret Hugunin,* Robert V. Talanian,* Sheldon Ratnofsky,* Christopher Quinlan,* Yutaka Emoto,Dagger Pramod Pandey,Dagger Rakesh Datta,Dagger Yinyin Huang,Dagger Surender Kharbanda,Dagger Hamish Allen,* Robert Kamen,* Winnie Wong,* and Donald KufeDagger

From * BASF Bioresearch Corporation, Worcester, Massachusetts 01605; and Dagger  Division of Cancer Pharmacology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115

Recent studies have shown that protein kinase C (PKC) delta  is proteolytically activated at the onset of apoptosis induced by DNA-damaging agents, tumor necrosis factor, and anti-Fas antibody. However, the relationship of PKCdelta cleavage to induction of apoptosis is unknown. The present studies demonstrate that full-length PKCdelta is cleaved at DMQD330N to a catalytically active fragment by the cysteine protease CPP32. The results also demonstrate that overexpression of the catalytic kinase fragment in cells is associated with chromatin condensation, nuclear fragmentation, induction of sub-G1 phase DNA and lethality. By contrast, overexpression of full-length PKCdelta or a kinase inactive PKCdelta fragment had no detectable effect. The findings suggest that proteolytic activation of PKCdelta by a CPP32-like protease contributes to phenotypic changes associated with apoptosis.


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