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J Biol Chem, Vol. 274, Issue 4, 2492-2501, January 22, 1999
From the To understand the molecular basis of
granule release from platelets, we examined the role of
vesicle-associated membrane protein, SNAP-23, and syntaxin 4 in
Proteins of the Exocytotic Core Complex Mediate Platelet
-Granule Secretion
ROLES OF VESICLE-ASSOCIATED MEMBRANE PROTEIN, SNAP-23, AND
SYNTAXIN 4
§,
,,, and
Center for Hemostasis and Thrombosis
Research, Beth Israel Deaconess Medical Center and Harvard Medical
School, Boston, Massachusetts 02215, § Howard Hughes
Medical Institute, and Department of Biochemistry, Tufts
University School of Medicine, Boston, Massachusetts 02111
-granule secretion. A vesicle-associated membrane protein, SNAP-23,
and syntaxin 4 were detected in platelet lysate. These proteins form a
SDS-resistant complex that disassembles upon platelet activation. To
determine whether these proteins are involved in -granule secretion,
we developed a streptolysin O-permeabilized platelet model
of -granule secretion. Streptolysin O-permeabilized
platelets released -granules, as measured by surface expression of
P-selectin, in response to Ca2+ up to 120 min after
permeabilization. Incubation of streptolysin O-permeabilized platelets with an antibody directed against
vesicle-associated membrane protein completely inhibited
Ca2+-induced -granule release. Tetanus toxin cleaved
platelet vesicle-associated membrane protein and inhibited
Ca2+-induced -granule secretion from streptolysin
O-permeabilized platelets. An antibody to syntaxin 4 also
inhibited Ca2+-induced -granule release by
approximately 75% in this system. These results show that
vesicle-associated membrane protein, SNAP-23, and syntaxin 4 form
a heterotrimeric complex in platelets that disassembles with
activation and demonstrate that -granule release is dependent on
vesicle SNAP receptor-target SNAP receptor (vSNARE-tSNARE) interactions.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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