© The Rockefeller University Press, 0022-1007/1996/12/2399/ $5.00
The Journal of Experimental Medicine, Volume 184, Number 6, December 1, 1996 2399-2404
Proteolytic Activation of Protein Kinase C
by an ICE/CED 3-like Protease Induces Characteristics of Apoptosis
Tariq Ghayur*,
Margaret Hugunin*,
Robert V. Talanian*,
Sheldon Ratnofsky*,
Christopher Quinlan*,
Yutaka Emoto
,
Pramod Pandey
,
Rakesh Datta
,
Yinyin Huang
,
Surender Kharbanda
,
Hamish Allen*,
Robert Kamen*,
Winnie Wong*, and
Donald Kufe
From * BASF Bioresearch Corporation, Worcester, Massachusetts 01605; and
Division of Cancer Pharmacology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115
Recent studies have shown that protein kinase C (PKC)
is proteolytically activated at the onset of apoptosis induced by DNA-damaging agents, tumor necrosis factor, and anti-Fas antibody. However, the relationship of PKC
cleavage to induction of apoptosis is unknown. The present studies demonstrate that full-length PKC
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 PKC
or a kinase inactive PKC
fragment had no detectable effect. The findings suggest that proteolytic activation of PKC
by a CPP32-like protease contributes to phenotypic changes associated with apoptosis.
Address correspondence to Donald W. Kufe, Division of Cancer Pharmacology, Dana-Farber Cancer Institute, 44 Binney St., Boston, MA 02115.
This investigation was supported by Public Health Service grants CA66996, CA55241, and CA29431 awarded by the National Cancer Institute, DHHS.

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