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Blood, Vol. 95 No. 3 (February 1), 2000:
pp. 959-964
Activation of the small GTPases, rac and cdc42, after ligation
of the platelet PAR-1 receptor
A. C. Azim,
K. Barkalow,
J. Chou, and
J.
H. Hartwig
From the Division of Hematology, Brigham and Women's Hospital,
Harvard Medical School, Boston, MA.
Stimulation of platelet PAR-1 receptors results in the rapid (10 to
30 seconds) and extensive (30% to 40% of total) guanosine triphosphate (GTP) charging of endogenous platelet rac, previously identified as a possible key intermediate in the signal pathway between
PAR-1 and actin filament barbed-end uncapping, leading to actin
assembly. During PAR-1-mediated platelet activation, rac distributes
from the cell interior to the cell periphery, and this reorganization
is resistant to the inhibition of PI-3-kinase activity. Rac, in resting
or activated platelets, is Triton X-100 soluble, suggesting that it
does not form tight complexes with actin cytoskeletal proteins,
though its retention in octyl-glucoside-treated platelets and
ultrastructural observations of activated platelets implies that rac
binds to plasma membranes, where it can interact with phosphoinositide
kinases implicated in actin assembly reactions. PAR-1 stimulation also
rapidly and extensively activates cdc42, though, in contrast to rac,
some cdc42 associates with the actin cytoskeleton in resting platelets,
and the bound fraction increases during stimulation. The differences in
subcellular distribution and previous evidence showing quantitatively
divergent effects of rac and cdc42 on actin nucleation in permeabilized
platelets indicate different signaling roles for these GTPases.
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