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Evidence for CPP32 Activation in the Absence of Apoptosis during T Lymphocyte Stimulation
Cysteine proteases of the interleukin-1β-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...
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Published in: | The Journal of biological chemistry 1997-05, Vol.272 (21), p.13459-13462 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Cysteine proteases of the interleukin-1β-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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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1074/jbc.272.21.13459 |