Evidence map›Paper›PMID 20026600›Full record

ArticleThe Journal of biological chemistry2010

Vesicle-associated membrane protein (VAMP) cleavage by a new metalloprotease from the Brazilian scorpion Tityus serrulatus.

Paul L Fletcher, Maryann D Fletcher, Keith Weninger, Trevor E Anderson, Brian M Martin

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

38 citing papers in PubMed, 83 citations in OpenAlex.

  1. Proteomic characterization ofThe journal of venomous animals and toxins including tropical diseases · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. An overview of some enzymes from buthid scorpion venoms from Colombia:The journal of venomous animals and toxins including tropical diseases · 2024
    Article
  8. Understanding the complexity ofThe journal of venomous animals and toxins including tropical diseases · 2024
    Review
  9. Review
  10. Article
  11. Article
  12. Comparison of biological activities ofThe journal of venomous animals and toxins including tropical diseases · 2021
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Proteome of fraction fromThe journal of venomous animals and toxins including tropical diseases · 2019
    Article
  18. Article
  19. Article
  20. Article
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

5 authors at 3 institutions in 1 country.

Paul L FletcherDepartment of Microbiology and Immunology, Brody School of Medicine, East Carolina University, Greenville, North Carolina 27834, USA.
Maryann D Fletcher
Keith Weninger
Trevor E Anderson
Brian M Martin
East Carolina University · USNorth Carolina State University · USNational Institutes of Health · US

Funding

Neuropsychiatric Disorders--protein Structure/activity StudiesZIAMH002344 · NIMH · NATIONAL INSTITUTE OF MENTAL HEALTH · PI MARTIN, BRIAN M · 2009 to 2014
$835k
Intramural NIH HHS ZIA MH002344
6 · The paper itself

Abstract

We present evidence that venom from the Brazilian scorpion Tityus serrulatus and a purified fraction selectively cleave essential SNARE proteins within exocrine pancreatic tissue. Western blotting for vesicle-associated membrane protein type v-SNARE proteins (or synaptobrevins) reveals characteristic alterations to venom-treated excised pancreatic lobules in vitro. Immunocytochemistry by electron microscopy confirms both the SNARE identity as VAMP2 and the proteolysis of VAMP2 as a marked decrease in secondary antibody-conjugated colloidal gold particles that are predominantly associated with mature zymogen granules. Studies with recombinant SNARE proteins were used to determine the specific cleavage site in VAMP2 and the susceptibility of VAMP8 (endobrevin). The VAMP2 cleavage site is between the transmembrane anchor and the SNARE motif that assembles into the ternary SNARE complex. Inclusion of divalent chelating agents (EDTA) with fraction nu, an otherwise active purified component from venom, eliminates SNARE proteolysis, suggesting the active protein is a metalloprotease. The unique cleavages of VAMP2 and VAMP8 may be linked to pancreatitis that develops following scorpion envenomation as both of these v-SNARE proteins are associated with zymogen granule membranes in pancreatic acinar cells. We have isolated antarease, a metalloprotease from fraction nu that cleaves VAMP2, and report its amino acid sequence.

Indexed as

Amino Acid SequenceAnimalsGuinea PigsImmunohistochemistryMetalloproteasesModels, MolecularMolecular Sequence DataPancreas, ExocrineProtein ConformationProtein IsoformsR-SNARE ProteinsScorpionsScorpion VenomsSecretory VesiclesSNARE ProteinsMetalloproteasesProtein IsoformsR-SNARE ProteinsScorpion VenomsSNARE Proteins

Identifiers

PMID20026600
PMCPMC2844189
OpenAlexW1996771340

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.