Evidence map›Paper›PMID 9045719›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience1997

Inhibition of transmitter release correlates with the proteolytic activity of tetanus toxin and botulinus toxin A in individual cultured synapses of Hirudo medicinalis.

D Bruns, S Engers, C Yang, R Ossig, A Jeromin, R Jahn

Open access · greenAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

14 citing papers in PubMed, 50 citations in OpenAlex.

  1. SNAP25 expression in mammalian retinal horizontal cells.The Journal of comparative neurology · 2011
    Article
  2. Role of the synaptobrevin C terminus in fusion pore formation.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  3. Article
  4. Article
  5. Homotypic fusion of early endosomes: SNAREs do not determine fusion specificity.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  6. Protein kinase C-dependent phosphorylation of synaptosome-associated protein of 25 kDa at Ser187 potentiates vesicle recruitment.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2002
    Article
  7. The SNARE protein SNAP-25 is linked to fast calcium triggering of exocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  8. Article
  9. The SNARE Vti1a-beta is localized to small synaptic vesicles and participates in a novel SNARE complex.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2000
    Article
  10. Article
  11. Article
  12. Exocytosis and endocytosisThe Plant cell · 1999
    Article
  13. Article
  14. Review
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

6 authors at 2 institutions in 1 country.

D BrunsThe Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06510, USA.
S Engers
C Yang
R Ossig
A Jeromin
R Jahn
Yale University · USHoward Hughes Medical Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have studied the effects of tetanus toxin and botulinus toxin A on neurotransmitter release in the Retzius-->P-cell synapse of the leech and exploited the unique properties of this system, which allow for combined physiological and biochemical analyses in single-cell pairs. The sequences of Hirudo medicinalis synaptobrevin and synaptosomal-associated protein of 25 kDa (SNAP-25), deduced by cDNA cloning, are 61 and 55% identical, respectively, to their corresponding mammalian homologs. Whereas Hirudo synaptobrevin is proteolyzed by tetanus toxin, its SNAP-25 isoform is resistant to botulinus toxin A cleavage because of amino acid substitutions within and around the putative cleavage site. In close correlation, microinjection of tetanus toxin into the presynaptic neuron produced a block of transmitter release, whereas botulinus toxin A had no effect on synaptic transmission. Subsequent immunoblotting of single-cell pairs demonstrated directly that the tetanus toxin-mediated block of exocytosis is accompanied by cleavage of synaptobrevin in the injected neuron, resulting in the generation of a detectable C-terminal cleavage product. Immunoblotting also confirmed the resistance of SNAP-25 to botulinus toxin A cleavage in vivo. Using recombinant proteins, we show that the N-terminal fragment of synaptobrevin released by tetanus toxin, but not its C-terminal membrane-anchored cleavage product, participates with syntaxin and SNAP-25 in synaptic SNAP receptor (SNARE) ternary complex formation in Hirudo. Our data demonstrate a direct correlation between the inhibition of transmitter release and the ability of the neurotoxin to proteolyze its target protein and support the view that SNARE ternary complex formation is an important step leading to synaptic vesicle exocytosis.

Indexed as

Amino Acid SequenceAnimalsBase SequenceBotulinum ToxinsCells, CulturedLeechesMolecular Sequence DataNeurotransmitter AgentsSynapsesTetanus ToxinBotulinum ToxinsNeurotransmitter AgentsTetanus Toxin

Identifiers

PMID9045719
PMCPMC6793773
OpenAlexW2138727954

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.