Evidence map›Paper›PMID 7796801›Full record

ArticleThe EMBO journal1995

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.

R Regazzi, C B Wollheim, J Lang, J M Theler, O Rossetto, C Montecucco, K Sadoul, U Weller, M Palmer, B Thorens

Abstract read
In one paragraph

Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
25.5field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

62 citing papers in PubMed, 227 citations in OpenAlex.

  1. Article
  2. Article
  3. A surviving beta cell subpopulation enriched in patients with T1D.bioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Article
  6. The function of VAMP2 in mediating membrane fusion: An overview.Frontiers in molecular neuroscience · 2022
    Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Pancreatic regulation of glucose homeostasis.Experimental & molecular medicine · 2016
    Review
  18. Article
  19. Article
  20. Article

2 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 1 institution in 1 country.

R RegazziDepartment of Medicine, University of Geneva, Switzerland.
C B Wollheim
J Lang
J M Theler
O Rossetto
C Montecucco
K Sadoul
U Weller
M Palmer
B Thorens
University of Geneva · CH

Funding

Telethon 473
6 · The paper itself

Abstract

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.

Indexed as

AnimalsBotulinum ToxinsBrain ChemistryCalciumCell FractionationCell LineCloning, MolecularCytoplasmic GranulesExocytosisGuanosine 5'-O-(3-Thiotriphosphate)InsulinInsulin SecretionIslets of LangerhansMembrane ProteinsNerve Tissue ProteinsRatsBotulinum ToxinsCalciumGuanosine 5'-O-(3-Thiotriphosphate)InsulinMembrane ProteinsNerve Tissue ProteinsR-SNARE ProteinsTetanus ToxinVesicle-Associated Membrane Protein 3

Identifiers

PMID7796801
PMCPMC398391
OpenAlexW267655585

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.