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J Biol Chem, Vol. 274, Issue 4, 2072-2076, January 22, 1999
From the Department of Surgery, University of Pittsburgh School of
Medicine, Pittsburgh, Pennsylvania 15261
It is likely that endogenous inhibitors of the
apical caspases such as caspase-9 exist to prevent undesirable
activation of caspase cascades. A naturally occurring variant of
caspase-9 named caspase-9S was cloned from human liver. Caspase-9S is
missing most of the large subunit of caspase-9, including the catalytic site, but has the intact prodomain and small subunit. Caspase-9S did
not show apoptotic activity in transfection analysis. Overexpression of
caspase-9S inhibited apoptosis induced by caspase-9, indicating that
caspase-9S is an endogenous dominant-negative of caspase-9. Moreover,
caspase-9S inhibited apoptosis induced by tumor necrosis factor(TNF)-
, TNF factor-related apoptosis-inducing ligand (TRAIL), Bax, or Fas-associated death domain-containing protein (FADD) as
well as the combination of Apaf-1 and caspase-9. In vitro
binding assays demonstrated that caspase-9S binds to Apaf-1 and blocks the binding of caspase-9 to Apaf-1. Coexpression of caspase-9 and
caspase-9S mRNA was identified in various cell lines. Thus, caspase-9S acts as a dominant-negative inhibitor of caspase-9 activation, at least in part, by blocking Apaf-1-caspase-9 interaction.
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