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A role of VAMP8/endobrevin in regulated exocytosis of pancreatic acinar cells.

Despite our general understanding that members of the SNARE superfamily participate in diverse intracellular docking/fusion events, the physiological role of the majority of SNAREs in the intact organism remains elusive. In this study, through targeted gene knockout in mice, we establish that VAMP8/endobrevin is a major player in regulated exocytosis of the exocrine pancreas. VAMP8 is enriched on the membrane of zymogen granules and exists in a complex with syntaxin 4 and SNAP-23. VAMP8-/- mice developed normally but showed severe defects in the pancreas. VAMP8 null acinar cells contained three times more zymogen granules than control acinar cells. Furthermore, secretagogue-stimulated secretion was abolished in pancreatic fragments derived from VAMP8-/- mice. In addition, VAMP8-/- mice were partially resistant to supramaximal caerulein-induced pancreatitis. These results suggest a major physiological role of VAMP8 in regulated exocytosis of pancreatic acinar cells by serving as a v-SNARE of zymogen granules.

Pubmed ID: 15363411


  • Wang CC
  • Ng CP
  • Lu L
  • Atlashkin V
  • Zhang W
  • Seet LF
  • Hong W


Developmental cell

Publication Data

September 14, 2004

Associated Grants


Mesh Terms

  • Amylases
  • Animals
  • Blotting, Western
  • Carrier Proteins
  • Cell Division
  • Cells, Cultured
  • Endocytosis
  • Exocytosis
  • Fibroblasts
  • Genotype
  • Glutathione Transferase
  • Immunohistochemistry
  • Liver
  • Membrane Proteins
  • Mice
  • Mice, Knockout
  • Mice, Transgenic
  • Microscopy, Fluorescence
  • Models, Genetic
  • Pancreas
  • Pancreatitis
  • Precipitin Tests
  • Qa-SNARE Proteins
  • Qb-SNARE Proteins
  • Qc-SNARE Proteins
  • R-SNARE Proteins
  • SNARE Proteins
  • Time Factors
  • Vesicular Transport Proteins