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Blood, 1 August 2002, Vol. 100, No. 3, pp. 1081-1083
BRIEF REPORT
Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are
present in human platelets and are required for granule
secretion
János Polgár,
Sul-Hee Chung, and
Guy L. Reed
From the Cardiovascular Biology Laboratory, Harvard School of
Public Health; and Massachusetts General Hospital, Boston, MA.
Secretion of platelet granules is necessary for normal hemostasis.
Platelet secretion requires soluble N-ethylmaleimide-sensitive factor
attachment protein (SNAP) receptor (SNARE) complex formation between
different members of the syntaxin, SNAP-25, and vesicle-associated membrane protein (VAMP) gene families. Using microcapillary
reverse-phase high-performance liquid chromatography-nano-electrospray
tandem mass spectrometry, we identified VAMP-3 and VAMP-8 as VAMP
isoforms coimmunoprecipitated from platelets with syntaxin 4. Immunoblotting experiments confirmed the presence of VAMP-3 and VAMP-8
but not VAMP-1 or VAMP-2 in platelets. To examine the effect of VAMP
proteins on platelet secretion, soluble recombinant (r) VAMP-2,
rVAMP-3, and rVAMP-8 were incubated with streptolysin O-permeabilized
platelets. Secretion of granules (monitored by flow cytometric
measurement of P-selectin) was blocked, and dense-granule secretion
(assessed by release of carbon 14-serotonin) was almost completely
inhibited by rVAMP-3, whereas rVAMP-8 inhibited secretion of dense
granules but not granules. In contrast, rVAMP-2, which formed SNARE
complexes in vitro, had no effect on platelet exocytosis. We conclude
that VAMP-3 and VAMP-8 form SNARE complexes with platelet syntaxin 4 and are required for platelet granule secretion.

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