Vesicle associated membrane protein (VAMP)-7 and VAMP-8, but not VAMP-2 or VAMP-3, are required for activation-induced degranulation of mature human mast cells

Eur J Immunol. 2008 Mar;38(3):855-63. doi: 10.1002/eji.200737634.

Abstract

Mediator release from mast cells (MC) is a crucial step in allergic and non-allergic inflammatory disorders. However, the final events in response to activation leading to membrane fusion and thereby facilitating degranulation have hitherto not been analyzed in human MC. Soluble N-ethyl-maleimide-sensitive factor attachment protein receptors (SNARE) represent a highly conserved family of proteins that have been shown to mediate intracellular membrane fusion events. Here, we show that mature MC isolated from human intestinal tissue express soluble N-ethylmaleide sensitive factor attachment protein (SNAP)-23, Syntaxin (STX)-1B, STX-2, STX-3, STX-4, and STX-6 but not SNAP-25. Furthermore, we found that primary human MC express substantial amounts of vesicle associated membrane protein (VAMP)-3, VAMP-7 and VAMP-8 and, in contrast to previous reports about rodent MC, only low levels of VAMP-2. Furthermore, VAMP-7 and VAMP-8 were found to translocate to the plasma membrane and interact with SNAP-23 and STX-4 upon activation. Inhibition of SNAP-23, STX-4, VAMP-7 or VAMP-8, but not VAMP-2 or VAMP-3, resulted in a markedly reduced high-affinity IgE receptor-mediated histamine release. In summary, our data show that mature human MC express a specific pattern of SNARE and that VAMP-7 and VAMP-8, but not VAMP-2, are required for rapid degranulation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies / pharmacology
  • Blotting, Western
  • Cell Degranulation / drug effects
  • Cell Degranulation / physiology*
  • Cell Membrane / metabolism
  • Cytoplasm / metabolism
  • Fluorescent Antibody Technique
  • Gene Expression / drug effects
  • Histamine Release / drug effects
  • Histamine Release / physiology
  • Humans
  • Mast Cells / drug effects
  • Mast Cells / metabolism
  • Mast Cells / physiology*
  • Metalloendopeptidases / pharmacology
  • Qa-SNARE Proteins / genetics
  • Qa-SNARE Proteins / immunology
  • Qa-SNARE Proteins / metabolism
  • Qb-SNARE Proteins / genetics
  • Qb-SNARE Proteins / immunology
  • Qb-SNARE Proteins / metabolism
  • Qc-SNARE Proteins / genetics
  • Qc-SNARE Proteins / immunology
  • Qc-SNARE Proteins / metabolism
  • R-SNARE Proteins / genetics
  • R-SNARE Proteins / metabolism
  • R-SNARE Proteins / physiology*
  • Reverse Transcriptase Polymerase Chain Reaction
  • SNARE Proteins / genetics
  • SNARE Proteins / metabolism
  • Tetanus Toxin / pharmacology
  • Vesicle-Associated Membrane Protein 2 / genetics
  • Vesicle-Associated Membrane Protein 2 / metabolism
  • Vesicle-Associated Membrane Protein 2 / physiology
  • Vesicle-Associated Membrane Protein 3 / genetics
  • Vesicle-Associated Membrane Protein 3 / metabolism
  • Vesicle-Associated Membrane Protein 3 / physiology

Substances

  • Antibodies
  • Qa-SNARE Proteins
  • Qb-SNARE Proteins
  • Qc-SNARE Proteins
  • R-SNARE Proteins
  • SNAP23 protein, human
  • SNARE Proteins
  • Tetanus Toxin
  • VAMP2 protein, human
  • VAMP3 protein, human
  • VAMP7 protein, human
  • VAMP8 protein, human
  • Vesicle-Associated Membrane Protein 2
  • Vesicle-Associated Membrane Protein 3
  • Metalloendopeptidases
  • zinc-endopeptidase, tetanus neurotoxin