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Blood, Vol. 94 No. 5 (September 1), 1999:
pp. 1683-1692
Calpain Functions in a Caspase-Independent Manner to Promote
Apoptosis-Like Events During Platelet Activation
Beni B. Wolf,
Joshua C. Goldstein,
Henning R. Stennicke,
Helen Beere,
Gustavo P. Amarante-Mendes,
Guy S. Salvesen, and
Douglas R. Green
From the Division of Cellular Immunology, La Jolla Institute for
Allergy and Immunology, San Diego, CA; the Department of Internal
Medicine, University of California, San Diego, CA; and The Program for
Apoptosis and Cell Death, The Burnham Institute, La Jolla, CA.
Apoptosis and platelet activation share common morphological and
biochemical features. Because caspases are essential mediators of
apoptosis, we examined whether platelets contain these proteinases and
use them during platelet activation. Human platelets contained caspase-9, caspase-3, and the caspase activators APAF-1 and cytochrome c as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting. Upon treatment with cytochrome c and dATP, platelet cytoplasmic extracts recapitulated apoptotic events, including
sequential activation of procaspase-9 and procaspase-3 and subsequent
proteolysis of caspase substrates. Calcium ionophore-stimulated platelets also recapitulated apoptotic events, including cell shrinkage, plasma membrane microvesiculation, phosphatidyl serine externalization, and proteolysis of procaspase-9, procaspase-3, gelsolin, and protein kinase C- . Strikingly, however, these events occurred without caspase activation or release of mitochondrial cytochrome c, suggesting a role for a noncaspase proteinase. Supporting this, inhibition of the calcium-dependent proteinase, calpain, prevented caspase proteolysis, `apoptotic' substrate cleavage, and
platelet microvesiculation. In vitro, purified calpain cleaved recombinant procaspase-9 and procaspase-3 without activating either caspase, confirming the inhibitor studies. These data implicate calpain
as a potential regulator of caspases and suggest that calpain, not
caspases, promotes apoptosis-like events during platelet activation.
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