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Blood, Vol. 95 No. 3 (February 1), 2000:
pp. 921-929
Molecular mechanisms of platelet exocytosis: role of SNAP-23
and syntaxin 2 in dense core granule release
Dong Chen,
Audrey M. Bernstein,
Paula P. Lemons, and
Sidney W. Whiteheart
From the Department of Biochemistry, University of Kentucky College
of Medicine, Lexington, KY.
To characterize the molecular mechanisms of platelet secretion, we
focused on the calcium-induced exocytosis of dense core granules.
Platelets contain several known t-SNAREs (soluble N-ethylmaleimide sensitive factor [NSF] attachment protein receptors) such as
syntaxins 2, 4, and 7 and SNAP-23 (synaptosomal associated
protein 23). By using an in vitro exocytosis assay, we have been able
to assign roles for some of these t-SNAREs in dense core granule
release. This calcium-induced secretion relies on the SNARE proteins
because it is stimulated by the addition of recombinant  -SNAP and
inhibited by a dominant negative -SNAP-L294A mutant or by
anti--SNAP and anti-NSF antibodies. SNAP-23 antibodies and an
inhibitory C-terminal SNAP-23 peptide both blocked dense core granule
release, demonstrating a role for SNAP-23. Unlike other cell types,
platelets contain a significant pool of soluble SNAP-23, which does not
partition into Triton X-114. Of the anti-syntaxin antibodies tested,
only anti-syntaxin 2 antibody inhibited dense core granule release. Immunoprecipitation studies showed that the 2 t-SNAREs syntaxin 2 and
SNAP-23 do form a complex in vivo. These data clearly show that SNAPs,
NSF, and specific t-SNAREs are used for dense core granule release;
these data provide a greater understanding of regulated exocytosis in platelets.
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