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J Biol Chem, Vol. 273, Issue 12, 6916-6920, March 20, 1998
From the Burnham Institute, Program on Apoptosis and Cell Death
Research, La Jolla, California 92037
Recently it has been reported that caspase-3
activation occurs in stimulated T-lymphocytes without associated
apoptosis (Miossec, C., Dutilleul, V., Fassy, F., and Diu-Hercend, A. (1997) J. Biol. Chem. 272, 13459-13462). To explore
this phenomenon, human peripheral blood lymphocytes (PBLs) were
stimulated with mitogenic lectins or anti-CD3 antibody, and the
proteolytic processing of different caspases and caspase substrates was
analyzed by immunoblotting. Proteolytic processing of caspases-3 and -7 and the caspase substrates poly(ADP-ribose) polymerase, GDP
dissociation inhibitor, and PKC
was observed when PBLs were
activated in vitro, and lysates were prepared using RIPA
buffer which contains 1% Nonidet P-40, 0.5% deoxycholate, and 0.1%
SDS. In contrast, when a lysis buffer containing 2% SDS was used, the
caspases remained in their zymogen pro-forms, and no proteolytic
processing of caspase substrates was detected. Moreover, in experiments
using intact cells and a cell-permeable fluorigenic caspase substrate,
no caspase activity was observed in activated T-cells, whereas it was
clearly detected when PBLs were treated with the apoptosis-inducing
anticancer drug etoposide. Since the granzyme B is a direct activator
of caspase-3 and its expression is induced following T-cell activation,
we tested the effects of anti-GraB, an engineered serpin that
specifically inhibits GraB. When the activated T-lymphocytes were lysed
in RIPA buffer containing anti-GraB, no proteolytic processing or
activation of caspase-3 was observed, strongly suggesting that release
of GraB or similar proteases from their storage sites in cytotoxic granules during the lysis procedure is responsible for caspase activation. These findings demonstrate that T-cells do not process caspases upon activation and caution about the method of cell lysis
used when studying granzyme-expressing cells.
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