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Blood, 1 June 2002, Vol. 99, No. 11, pp. 4006-4014
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Subcellular distribution of 3 functional platelet SNARE proteins:
human cellubrevin, SNAP-23, and syntaxin 2
Dian Feng,
Katharine Crane,
Nataliya Rozenvayn,
Ann M. Dvorak, and
Robert Flaumenhaft
From the Departments of Medicine and Pathology, Beth
Israel Deaconess Medical Center, Harvard Medical School, Boston, MA.
Morphologic studies have demonstrated a process by which
 -granule contents are released from platelets. Studies aimed at defining the molecular mechanisms of this release have
demonstrated that SNARE proteins are required for -granule
secretion. These observations raise the possibility that morphologic
features of -granule secretion may be influenced by the subcellular
distribution of SNARE proteins in the platelet. To evaluate this
possibility, we analyzed the subcellular distribution of 3 functional
platelet SNARE proteins human cellubrevin, SNAP-23, and syntaxin 2. Exposure of streptolysin O-permeabilized platelets to antihuman
cellubrevin antibody inhibited Ca++-induced -granule
secretion by approximately 50%. Inhibition of -granule secretion by
antihuman cellubrevin was reversed by a blocking peptide. Syntaxin 2 and SNAP-23 have previously been demonstrated to mediate platelet
granule secretion. The subcellular localization of the 3 SNARE proteins
was determined by ultrastructural studies, using a pre-embedding
immunonanogold method, and by immunoblot analysis of
subcellular fractions. Immunonanogold localization demonstrated that
approximately 80% of human cellubrevin in resting platelets
was localized to platelet granule membranes. In contrast, SNAP-23
localized predominantly to plasma membrane, whereas syntaxin 2 was more
evenly distributed among membranes of -granules, the open
canalicular system, and plasma membrane. Thus, each of these SNARE
proteins has a distinct subcellular distribution in platelets, and each
of these membrane compartments demonstrates a unique SNARE protein
composition. This distribution provides a basis for several
characteristics of -granule secretion that include homotypic
-granule fusion and the fusion of -granules with the open
canalicular system and plasma membrane.
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