Role of vesicle-associated membrane protein-2, through Q-soluble N-ethylmaleimide-sensitive factor attachment protein receptor/R-soluble N-ethylmaleimide-sensitive factor attachment protein receptor interaction, in the exocytosis of specific and tertiary granules of human neutrophils
Autor: | Pedro A. Lazo, Svetlana M. Nabokina, Faustino Mollinedo, Jero Calafat, Belén Martín-Martín |
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Rok vydání: | 2003 |
Předmět: |
Cell Membrane Permeability
Neutrophils Immunoelectron microscopy Glutamine Immunology Molecular Sequence Data Vesicular Transport Proteins Biology Arginine Cytoplasmic Granules GPI-Linked Proteins Exocytosis Neutrophil Activation R-SNARE Proteins Tetanus Toxin Membrane region Antigens CD Antigens Neoplasm Immunology and Allergy Humans Microscopy Immunoelectron Interphase Conserved Sequence VAMP2 Qa-SNARE Proteins Antibodies Monoclonal Membrane Proteins Munc-18 Syntaxin 3 Vesicle-Associated Membrane Protein 2 Cell biology Electroporation Solubility Cell activation SNARE Proteins Cell Adhesion Molecules |
Zdroj: | Journal of immunology (Baltimore, Md. : 1950). 170(2) |
ISSN: | 0022-1767 |
Popis: | 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-γ-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. |
Databáze: | OpenAIRE |
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