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Blood, 15 March 2001, Vol. 97, No. 6, pp. 1835-1844
NEOPLASIA
Involvement of caspase-2 long isoform in Fas-mediated cell death
of human leukemic cells
Nathalie Droin,
Florence Bichat,
Cedric Rébé,
Anne Wotawa,
Olivier Sordet,
Arlette Hammann,
Richard Bertrand, and
Eric Solary
From INSERM U517, Faculties of Medicine and Pharmacy,
Dijon, France and Research Centre of University of Montreal Hospital
Centre, Notre Dame Hospital, Montreal, QC, Canada.
Engagement of the plasma membrane receptor Fas can induce apoptosis
of leukemic cells. Signaling through Fas requires the formation of a
death-inducing signaling complex (DISC) that involves the cytoplasmic
domain of Fas, the adaptor molecule FADD/MORT-1, and procaspase-8. The
present study investigated whether another caspase, known as
procaspase-2L, played a role in Fas-mediated cell death. A series of
human leukemic variant cells was derived by stable transfection with a
CASP2L antisense construct (CASP2L/AS). Specific down-regulation of procaspase-2L decreased the sensitivity of
these cells to apoptosis induced by an agonistic anti-Fas antibody (Ab,
clone CH11), as determined by studying DNA fragmentation, chromatin
condensation, and externalization of phosphatidylserine on the plasma
membrane. In leukemic cells transfected with an empty vector, anti-Fas
Ab treatment activated caspase-8, decreased the expression of the BH3
domain-only protein Bid, triggered the release of cytochrome c from the
mitochondria to the cytosol, and activated caspase-3. All these events
could not be observed when CASP2L/AS cells were
similarly treated with anti-Fas Abs. CASP2L/AS
transfection did not inhibit the formation of the DISC and no direct
interaction between procaspase-2L and either Fas or FADD or
procaspase-8 was identified. Down-regulation of procaspase-2L inhibited
anti-Fas Ab-mediated cleavage of c-FLIP (FLICE-inhibitory protein), a
protein that interferes with the formation of a functional DISC. These
results suggest that the long isoform of caspase-2 plays a role in the
Fas-mediated pathway to cell death by contributing to caspase-8
activation at the DISC level.
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