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Blood, Vol. 93 No. 12 (June 15), 1999:
pp. 4222-4231
Role of Caspase in a Subset of Human Platelet Activation Responses
Anna Shcherbina and
Eileen Remold-O'Donnell
From The Center for Blood Research and the Department of Pediatrics,
Harvard Medical School, Boston, MA.
Platelets function to protect the integrity of the vascular wall. A
subset of platelet activation responses that are especially important
for thrombus formation include exposure of phosphatidylserine and
release of microparticles, which generate procoagulant surfaces. The
resemblance of these platelet activation processes to events occurring
in nucleated cells undergoing apoptosis suggests a possible role for
caspases, which are major effector enzymes of nucleated cell apoptosis. We demonstrate here the presence of caspase-3 in human
platelets and its activation by physiological platelet agonists. Using
cell-permeable specific inhibitors, we demonstrate a role for a
caspase-3-like protease in the agonist-induced (collagen plus thrombin
or Ca2+ ionophore) platelet activation events of
phosphatidylserine exposure, microparticle release, and cleavage of
moesin, a cytoskeletal-membrane linker protein. The role of caspase-3
in platelet activation is restricted rather than global, because other
activation responses,  granule secretion, shape change, and
aggregation were unaffected by caspase-3 inhibitors. Experiments with
two classes of protease inhibitors show that caspase-3 function is
distinct from that of calpain, which is also involved in late platelet
activation events. These findings show novel functions of caspase and
provide new insights for understanding of platelet activation.
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