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(Received for publication, March 7, 1997)
From Roussel Uclaf, 102 route de Noisy, 93235 Romainville
Cedex, France
Cysteine proteases of the
interleukin-1
-converting enzyme family have been implicated in the
effector process of apoptosis in several systems. Among these, CPP32
has been shown to be processed to active enzyme at the onset of
apoptosis. Here, we show that CPP32 precursor is cleaved into its
active form during phytohaemaglutinin A activation of T
lymphocytes. Maximal processing is observed between day 3 and day 4 following addition of mitogen and is a transient process. Precursor
cleavage is associated with the appearance of a CPP32-like enzymatic
activity in cell lysates. At this time in the culture, almost no
apoptotic cell and no dead cell can be detected, and T lymphocytes are
actively proliferating. CPP32 processing also occurs when lymphocytes
are stimulated through an allogeneic primary mixed lymphocyte reaction.
Our results suggest that proteolytic activation of CPP32 could be a
physiological step during T lymphocyte activation. In addition, these
data indicate that CPP32 activation can occur independently of
programmed cell death in T lymphocytes.
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