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Blood, Vol. 93 No. 10 (May 15), 1999:
pp. 3309-3316
Interferon  Induces Upregulation and Activation of Caspases 1, 3, and 8 to Produce Apoptosis in Human Erythroid Progenitor Cells
Chunhua Dai and
Sanford B. Krantz
From the Hematology/Oncology Division, Department of Medicine,
Department of Veterans Affairs Medical Center, Nashville, TN; and the
Vanderbilt Cancer Center, Vanderbilt University School of Medicine,
Nashville, TN.
Interferon  (IFN) induces apoptosis in purified human
erythroid colony-forming cells (ECFC) and inhibits cell growth. Fas (APO-1; CD95) and Fas ligand (FasL) mediate apoptosis induced by
IFN, because Fas is significantly upregulated by IFN, whereas Fas
ligand is constitutively present in the ECFC and neutralization of FasL
greatly reduces the apoptosis. Because conversion of caspases from
their dormant proenzyme forms to active enzymes has a critical role in
transducing a cascade leading to apoptosis, we performed further
studies of the expression and activation of caspases in normal human
and IFN-treated day-6 ECFC to better understand the mechanism of
IFN action in producing this cell death. RNase protection assays
showed that the caspase-1, -2, -6, -8, and -9 mRNAs were upregulated by
IFN, whereas the caspase-5 and -7 mRNAs were not increased. Western
blots showed that FLICE/caspase-8 was upregulated and activated by 24 hours of incubation with IFN. FADD was not similarly altered by
incubation with IFN. Western blots of ICE/caspase-1, which might be
required for amplification of the initial FLICE activation signal,
showed that pro-ICE expression significantly increased after treatment
with IFN for 24 hours and cleavage of pro-ICE also increased.
CPP32/apopain/caspase-3, responsible for the proteolytic cleavage of
poly (ADP) ribose polymerase (PARP), was also studied and treatment of
ECFC with IFN resulted in an increased concentration of caspase-3 by
24 hours and a clear induction of enzyme activation by 48 hours, which
was identified by the appearance of its p17-kD peptide fragment. The
cleavage of PARP was demonstrated by an obvious increase of the 89-kD
PARP cleavage product, which was observed at almost the same time as
caspase-3 activation in the IFN-treated cells, whereas untreated
ECFC showed little change. Peptide inhibitors of the caspase proteins,
DEVD-fmk, DEVD-cho, YVAD-cho, and IETD-fmk, were incubated with the
ECFC to obtain further evidence for the involvement of caspases in
IFN-induced apoptosis. The activation of FLICE/caspase-8 and
CPP32/caspase-3 and cleavage of PARP clearly were inhibited, but the
reduction of cell growth due to apoptosis, induced by IFN, was only
partially blocked by the presence of the inhibitors. These results
indicate that IFN acts on ECFC not only to upregulate Fas, but also
to selectively upregulate caspases-1, -3, and -8, which are activated
and produce apoptosis, whereas the concentrations of FasL and FADD are
not demonstrably changed.
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