Fusion protein vesicle-associated membrane protein 2 is implicated in IFN-gamma-induced piecemeal degranulation in human eosinophils from atopic individuals

J Allergy Clin Immunol. 2001 Apr;107(4):671-8. doi: 10.1067/mai.2001.113562.

Abstract

Background: Exocytosis is an integral event during IFN-gamma-induced piecemeal degranulation in eosinophils. In many tissues soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs), including vesicle-associated membrane protein (VAMP), act as specific intracellular receptors to allow granule fusion with the membrane during degranulation. However, the mechanisms underlying eosinophil piecemeal degranulation induced by IFN-gamma are not well understood.

Objective: We sought to assess whether eosinophils express the vesicular SNARE protein VAMP-2 and to determine the involvement of VAMP-2 in IFN-gamma-induced piecemeal degranulation.

Methods: Human peripheral blood eosinophils (> or =97%) from atopic subjects were subjected to RT-PCR and sequence analysis with specific primers for VAMP-2 mRNA. Western blotting and flow cytometric analysis were carried out to confirm the identity of VAMP-2 and its susceptibility to cleavage by tetanus toxin. Confocal laser scanning microscopy imaging was conducted on double-labeled cytospin preparations of eosinophils at 0, 5, 10, 30, and 60 minutes and 16 hours of IFN-gamma (500 U/mL) stimulation.

Results: Eosinophils expressed VAMP-2 mRNA (n = 4 donors), which exhibited 100% homology with human VAMP-2 cDNA on sequencing. Eosinophils were also found to express tetanus toxin-sensitive VAMP-2 protein. RANTES and VAMP-2 immunofluorescence were observed to colocalize to similar intracellular structures by means of confocal imaging. IFN-gamma induced a rapid translocation of VAMP-2(+) organelles toward the cell membrane in correlation with RANTES.

Conclusions: These findings suggest that exocytosis in human eosinophils is regulated by SNAREs, with a specific role indicated for VAMP-2 in piecemeal degranulation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antigens, CD / analysis
  • Cell Degranulation
  • Chemokine CCL5 / analysis
  • Eosinophils / physiology*
  • Humans
  • Hypersensitivity / blood*
  • Interferon-gamma / pharmacology*
  • Membrane Proteins / analysis
  • Membrane Proteins / genetics
  • Membrane Proteins / physiology*
  • Mice
  • Molecular Sequence Data
  • Platelet Membrane Glycoproteins / analysis
  • R-SNARE Proteins
  • RNA, Messenger / analysis
  • Rats
  • SNARE Proteins
  • Tetraspanin 30
  • Vesicular Transport Proteins*

Substances

  • Antigens, CD
  • CD63 protein, human
  • Cd63 protein, mouse
  • Chemokine CCL5
  • Membrane Proteins
  • Platelet Membrane Glycoproteins
  • R-SNARE Proteins
  • RNA, Messenger
  • SNARE Proteins
  • Tetraspanin 30
  • Vesicular Transport Proteins
  • Interferon-gamma