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* Centro de Investigación del Cáncer, Instituto de Biología Molecular y Celular del Cáncer, Consejo Superior de Investigaciones Cientificas-Universidad de Salamanca, Salamanca, Spain; and
Division of Cell Biology, The Netherlands Cancer Institute, Amsterdam, The Netherlands
We have examined the role of the R-soluble
N-ethylmaleimide-sensitive factor attachment protein
receptor (SNARE) synaptobrevin-2/vesicle-associated membrane protein
(VAMP)-2 in neutrophil exocytosis. VAMP-2, localized in the membranes
of specific and gelatinase-containing tertiary granules in resting
human neutrophils, resulted translocated to the cell surface following
neutrophil activation under experimental conditions that induced
exocytosis of specific and tertiary granules. VAMP-2 was also found on
the external membrane region of granules docking to the plasma membrane
in activated neutrophils. Specific Abs against VAMP-2 inhibited
Ca2+ and GTP-
-S-induced exocytosis of CD66b-enriched
specific and tertiary granules, but did not affect exocytosis of
CD63-enriched azurophilic granules, in electropermeabilized
neutrophils. Tetanus toxin disrupted VAMP-2 and inhibited exocytosis of
tertiary and specific granules. Activation of neutrophils led to the
interaction of VAMP-2 with the plasma membrane Q-SNARE syntaxin 4, and
anti-syntaxin 4 Abs inhibited exocytosis of specific and tertiary
granules in electropermeabilized neutrophils. Immunoelectron microscopy
showed syntaxin 4 on the plasma membrane contacting with docked
granules in activated neutrophils. These data indicate that VAMP-2
mediates exocytosis of specific and tertiary granules, and that
Q-SNARE/R-SNARE complexes containing VAMP-2 and syntaxin 4 are involved
in neutrophil exocytosis.
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