MersV1, France, Analysis, bibRecord, 000371

Exploring the functional domain and the target of the tetanus toxin light chain in neurohypophysial terminals

Identifieur interne : 000371 ( France/Analysis ); précédent : 000370; suivant : 000372

Exploring the functional domain and the target of the tetanus toxin light chain in neurohypophysial terminals

Auteurs : G. Dayanithi [France] ; B. Stecher [Allemagne] ; B. Ho Hne-Zell [Allemagne] ; S. Yamasaki [Allemagne] ; T. Binz [Allemagne] ; U. Weller [Allemagne] ; H. Niemann [Allemagne] ; M. Gratzl [Allemagne]

Source :

Neuroscience [ 0306-4522 ] ; 1994.

RBID : ISTEX:63359B3A1EF0499383E7711D7AFBE30023A790C9

English descriptors

KwdEn :
- DPA, DTT, EDTA, EGTA, HEPES, PIPES, TeTxL, WT.
Teeft :
- Aplysia neurons, Atomic absorption spectroscopy, Biochem, Biol, Botulinum, Botulinum neurotoxins, Captopril, Cell biol, Chelating, Chelating agent, Chem, Chromaffin, Clostridial, Clostridial neurotoxins, Control experiments, Covalent modification, Dayanithi, Dipicolinic acid, Edta, Egta, Endocrine, Endocrine cells, Exocytosis, Exocytotic release, Experimental procedures, Granule, Gratzl, Heavy chain, Histidine, Jahn, Light chain, Light chains, Locke saline, Nerve endings, Nerve terminals, Neurohypophysial, Neurohypophysial nerve endings, Neuron, Neurotoxin, Neurotransmitter release, Niemann, Peptidase, Peptide, Perifused, Permeabilized, Permeabilized nerve terminals, Recombinant, Secretory, Secretory granules, Streptolysin, Synaptic, Synaptic vesicles, Synaptobrevin, Synaptobrevin family, Synthetic peptides, Tetanus, Tetanus toxin, Tetanus toxin light chain, Tetanus toxin light chain action, Tetx, Tetxl, Tetxl acts, Toxin, Vasopressin, Vasopressin release, Vesicle, Weller, Zinc binding motif, Zinc peptidase, Zinc peptidases.

Abstract

Abstract: The tetanus toxin light chain blocks calcium induced vasopressin release from neurohypophysial nerve terminals. Here we show that histidine residue 233 within the putative zinc binding motif of the tetanus toxin light chain is essential for the inhibition of exocytosis, in the rat. The zinc chelating agent dipicolinic acid as well as captopril, an inhibitor of zinc-dependent peptidases, counteract the effect of the neurotoxin. Synthetic peptides, the sequences of which correspond to motifs present in the cytoplasmic domain of the synaptic vesicle membrane protein synaptobrevin 1 and 2, prevent the effect of the tetanus toxin light chain.Our results indicate that zinc bound to the zinc binding motif constitutes the active site of the tetanus toxin light chain. Moreover they suggest that cleavage of synaptobrevin by the neurotoxin causes the inhibition of exocytotic release of vasopressin from secretory granules.

Url:

https://api.istex.fr/ark:/67375/6H6-STN16FNG-F/fulltext.pdf

DOI: 10.1016/0306-4522(94)90048-5

Affiliations:

Links toward previous steps (curation, corpus...)

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to stream Main, to step Curation: 004668
to stream Main, to step Exploration: 004668
to stream France, to step Extraction: 000371

Links to Exploration step

ISTEX:63359B3A1EF0499383E7711D7AFBE30023A790C9

Le document en format XML

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<term>Gratzl</term>
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<term>Histidine</term>
<term>Jahn</term>
<term>Light chain</term>
<term>Light chains</term>
<term>Locke saline</term>
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<term>Nerve terminals</term>
<term>Neurohypophysial</term>
<term>Neurohypophysial nerve endings</term>
<term>Neuron</term>
<term>Neurotoxin</term>
<term>Neurotransmitter release</term>
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<front><div type="abstract" xml:lang="en">Abstract: The tetanus toxin light chain blocks calcium induced vasopressin release from neurohypophysial nerve terminals. Here we show that histidine residue 233 within the putative zinc binding motif of the tetanus toxin light chain is essential for the inhibition of exocytosis, in the rat. The zinc chelating agent dipicolinic acid as well as captopril, an inhibitor of zinc-dependent peptidases, counteract the effect of the neurotoxin. Synthetic peptides, the sequences of which correspond to motifs present in the cytoplasmic domain of the synaptic vesicle membrane protein synaptobrevin 1 and 2, prevent the effect of the tetanus toxin light chain.Our results indicate that zinc bound to the zinc binding motif constitutes the active site of the tetanus toxin light chain. Moreover they suggest that cleavage of synaptobrevin by the neurotoxin causes the inhibition of exocytotic release of vasopressin from secretory granules.</div>
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Exploring the functional domain and the target of the tetanus toxin light chain in neurohypophysial terminals

Exploring the functional domain and the target of the tetanus toxin light chain in neurohypophysial terminals

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri