VAMP‐2 and cellubrevin are expressed in pancreatic beta‐cells and are essential for Ca(2+)‐but not for GTP gamma S‐induced insulin secretion.
Open accessAbstract
VAMP proteins are important components of the machinery controlling docking and/or fusion of secretory vesicles with their target membrane. We investigated the expression of VAMP proteins in pancreatic beta-cells and their implication in the exocytosis of insulin. cDNA cloning revealed that VAMP-2 and cellubrevin, but not VAMP-1, are expressed in rat pancreatic islets and that their sequence is identical to that isolated from rat brain. Pancreatic beta-cells contain secretory granules that store and secrete insulin as well as synaptic-like microvesicles carrying gamma-aminobutyric acid. After subcellular fractionation on continuous sucrose gradients, VAMP-2 and cellubrevin were found to be associated with both types of secretory vesicle. The association of VAMP-2 with insulin-containing granules was confirmed by confocal microscopy of primary cultures of rat pancreatic beta-cells. Pretreatment of streptolysin-O permeabilized insulin-secreting cells with tetanus and botulinum B neurotoxins selectively cleaved VAMP-2 and cellubrevin and abolished Ca(2+)-induced insulin release (IC50 approximately 15 nM). By contrast, the pretreatment with tetanus and botulinum B neurotoxins did not prevent GTP gamma S-stimulated insulin secretion. Taken together, our results show that pancreatic beta-cells express VAMP-2 and cellubrevin and that one or both of these proteins selectively control Ca(2+)-mediated insulin secretion.
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Numerous SNARE isoforms, including syntaxin-1, -3 and -4, SNAP-25 and -23, and VAMP2 and -3, are involved in glucose-stimulated insulin secretion, whereas VAMP8 is non-essential for glucose-stimulated insulin secretion but has a role in GLP-1-potentiated insulin secretion.
“To date, numerous SNARE isoforms, including syntaxin-1, -3 and -4, SNAP-25 and -23, as well as syntaptobrevins 2 and 3 (VAMP2 and 3), have been shown to be involved in glucose-stimulated insulin secretion,42, 43, 44, 45, 46 whereas VAMP8, a non-essential SNARE protein for glucose-stimulated insulin secretion, has a role in the regulation of the glucagon-like peptide-1-potentiated insulin secretion”
From Pancreatic regulation of glucose homeostasis. (2016) · cites this paper as [45]
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References 56 · Cited by 233
Research works printed but not linked: 7
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- Authors
- Regazzi, R., Wollheim, C. B., Lang, J., Theler, J. M., Rossetto, O., Montecucco, C., Sadoul, K., Weller, U., Palmer, M., & Thorens, B.
- Affiliations
- University of Geneva (CH)
- Venue
- The EMBO Journal
- Published
- 1995-06-01
- Volume
- 14
- Issue
- 12
- Pages
- 2723-2730
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC398391
- OpenAlex
- W267655585
- Cited by
- 233
- References
- 56
- Citations by year
- 2026: 6 · 2025: 1 · 2024: 3 · 2023: 4 · 2022: 3 · 2021: 5 · 2020: 2 · 2019: 1 · 2018: 1 · 2017: 6 · 2016: 4 · 2015: 5 · 2014: 11 · 2013: 7 · 2012: 4
- FWCI
- 25.40
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- IRIS (submittedVersion)
- SERVAL (Université de Lausanne) (submittedVersion)
- Funders
- National Science Foundation
- Yale University
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (30313, 32376)
- Topics
- Health Sciences › Medicine › Surgery › Pancreatic function and diabetes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- VAMP2, cellubrevin, pancreatic beta cells, insulin secretion, calcium-induced exocytosis, secretory granules, synaptic-like microvesicles, tetanus neurotoxin, vesicle fusion
- MeSH terms
- Insulin Secretion, Animals, Botulinum Toxins, Brain Chemistry, Calcium, Cell Fractionation, Cell Line, Cloning, Molecular, Cytoplasmic Granules, Exocytosis, Insulin, Islets of Langerhans, Membrane Proteins, Nerve Tissue Proteins, Tetanus Toxin, Guanosine 5'-O-(3-Thiotriphosphate), Sequence Analysis, DNA, R-SNARE Proteins, Vesicle-Associated Membrane Protein 3, Rats
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