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B Activity in Human T Lymphocytes Induces Caspase-Dependent Apoptosis Without Detectable Activation of Caspase-1 and -31
,2,
Departments of
*
Immunology,
Hematology-Oncology,
Urology, and
§
Anatomic Pathology, Cleveland Clinic Foundation, Cleveland, OH 44195
NF-
B is involved in the transcriptional control of various genes
that act as extrinsic and intrinsic survival factors for T cells. Our
findings show that suppression of NF-B activity with cell-permeable
SN50 peptide, which masks the nuclear localization sequence of NF-B1
dimers and prevents their nuclear localization, induces apoptosis in
resting normal human PBL. Inhibition of NF-B resulted in the
externalization of phosphatidylserine, induction of DNA breaks, and
morphological changes consistent with apoptosis. DNA fragmentation was
efficiently blocked by the caspase inhibitor Z-VAD-fmk and partially
blocked by Ac-DEVD-fmk, suggesting that SN50-mediated apoptosis is
caspase-dependent. Interestingly, apoptosis induced by NF-B
suppression, in contrast to that induced by TPEN
(N,N,N',N'-tetrakis
[2-pyridylmethyl]ethylenediamine) or soluble Fas ligand (CD95), was
observed in the absence of active death effector proteases
caspase-1-like (IL-1 converting enzyme), caspase-3-like
(CPP32/Yama/apopain), and caspase-6-like and without cleavage of
caspase-3 substrates poly(ADP-ribose) polymerase and DNA fragmentation
factor-45. These findings suggest either low level of activation is
required or that different caspases are involved. Preactivation of T
cells resulting in NF-B nuclear translocation protected cells from
SN50-induced apoptosis. Our findings demonstrate an essential role of
NF-B in survival of naive PBL.
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