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*
Unité d’Immuno-Allergie, Institut Pasteur, Paris, France; and
Centre National de la Recherche Scientifique, Unité Mixte de Recherche 144, Institut Curie, Paris, France
Mast cells upon stimulation through high affinity IgE receptors
massively release inflammatory mediators by the fusion of specialized
secretory granules (related to lysosomes) with the plasma membrane.
Using the RBL-2H3 rat mast cell line, we investigated whether granule
secretion involves components of the soluble
N-ethylmaleimide-sensitive factor attachment protein
receptor (SNARE) machinery. Several isoforms of each family of SNARE
proteins were expressed. Among those, synaptosome-associated protein of
23 kDa (SNAP23) was central in SNARE complex formation. Within the
syntaxin family, syntaxin 4 interacted with SNAP23 and all
vesicle-associated membrane proteins (VAMPs) examined, except tetanus
neurotoxin insensitive VAMP (TI-VAMP). Overexpression of syntaxin 4,
but not of syntaxin 2 nor syntaxin 3, caused inhibition of
Fc
RI-dependent exocytosis. Four VAMP proteins, i.e., VAMP2,
cellubrevin, TI-VAMP, and VAMP8, were present on intracellular membrane
structures, with VAMP8 residing mainly on mediator-containing secretory
granules. We suggest that syntaxin 4, SNAP23, and VAMP8 may be involved
in regulation of mast cell exocytosis. Furthermore, these results are
the first demonstration that the nonneuronal VAMP8 isoform, originally
localized on early endosomes, is present in a regulated secretory
compartment.
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