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J. Biol. Chem., Vol. 269, Issue 51, 32043-32046, 12, 1994
AJ Darmon, N Ehrman, A Caputo, J Fujinaga and RC Bleackley
Murine granzyme B (cytotoxic cell proteinase-1 (CCP1)) is a member of a
family of seven serine proteases found in cytoplasmic granules of cytotoxic
T lymphocytes (CTLs). Evidence has suggested that it is involved in target
cell DNA fragmentation during CTL-mediated cytotoxicity, although
intracellular substrates for granzyme B have not yet been identified. The
substrate specificity of granzyme B, requiring an aspartic acid residue at
site P1, is unique among eukaryotic serine proteases and is shared with
only one other known eukaryotic protease, interleukin-1 beta-converting
enzyme (ICE). ICE is responsible for processing pro-interleukin-1 beta to
produce biologically active interleukin-1 beta and is itself synthesized as
an inactive precursor. Recent evidence has suggested a role for ICE in
programmed cell death, which led to a model for CTL-mediated cytotoxicity.
In this proposal granzyme B activates ICE in the target cell by
proteolytically processing the ICE precursor, resulting in active ICE
heterodimer that induces apoptosis in the target cell. We have isolated the
cDNA encoding murine ICE and generated in vitro translated ICE precursor.
Using lysates from COS cells expressing granzyme B we show that ICE
precursor is not a substrate for granzyme B and propose an alternate
mechanism for CTL-mediated cytotoxicity.
The cytotoxic T cell proteinase granzyme B does not activate interleukin-1 beta-converting enzyme
Department of Biochemistry, University of Alberta, Edmonton, Canada.
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