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Blood, 1 October 2000, Vol. 96, No. 7, pp. 2574-2583
PHAGOCYTES
Involvement of SNAP-23 and syntaxin 6 in human
neutrophil exocytosis
Belén Martín-Martín,
Svetlana M. Nabokina,
Juan Blasi,
Pedro A. Lazo, and
Faustino Mollinedo
From the Centro de Investigación del
Cáncer, Instituto de Biología Molecular y Celular del
Cáncer, CSIC-Universidad de Salamanca, Campus Miguel de Unamuno,
Salamanca, Spain; and Departament de Biologia Celular i
Anatomia Patologica, Campus de Bellvitge, Universidad de Barcelona,
L'Hospitalet de Llobregat, Spain.
To understand the molecular basis of exocytosis in human
neutrophils, the role of syntaxin 6 and SNAP-23 in neutrophil
degranulation was examined. Human syntaxin 6 was cloned and identified
as a 255-amino acid protein with a carboxy-terminal transmembrane
region and two coiled-coil domains. Syntaxin 6 was localized mainly in the plasma membrane of human resting neutrophils, whereas SNAP-23 was
located primarily in the mobilizable tertiary and specific granules.
SNAP-23 was translocated to the cell surface, colocalizing with
syntaxin 6, on neutrophil activation. In vitro binding studies established that SNAP-23 binds to syntaxin 6. Coimmunoprecipitation assays indicated that SNAP-23 interacts with syntaxin 6 in vivo, and
this interaction was dramatically increased on neutrophil activation.
Antibodies against SNAP-23 inhibited Ca++ and
GTP- -S-induced exocytosis of CD67-enriched specific granules, but
they hardly affected exocytosis of the CD63-enriched azurophilic granules, when introduced into electropermeabilized neutrophils. Anti-syntaxin 6 antibodies prevented exocytosis of both CD67- and
CD63-enriched granules in electropermeabilized neutrophils. These data
show that syntaxin 6 and SNAP-23 are involved in human neutrophil
exocytosis, demonstrating that vesicle SNAP receptor-target SNAP
receptor (v-SNARE- t-SNARE) interactions modulate neutrophil secretion. Syntaxin 6 acts as a target for secretion of specific and
azurophilic granules, whereas SNAP-23 mediates specific granule secretion.
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