Effects of botulinum toxin on neuromuscular transmission in the rat.

Cull-Candy, SG; Lundh, Håkan; Thesleff, S.

doi:10.1113/jphysiol.1976.sp011510

Cited by 228 publications

(120 citation statements)

References 38 publications

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“…Our findings are in accord with earlier studies (36)(37)(38) that showed that Ca 2ϩ cooperativity of transmitter release is reduced in Botulinum toxin A (BoTxA, which cleaves SNAP-25) and tetanus toxin (which cleaves VAMP͞synaptobrevin) poisoned rat neuromuscular junctions. We report the involvement of syntaxin in Ca 2ϩ cooperativity and altogether these studies show that independent manipulation of any one of the three SNARE proteins can alter cooperativity.…”

Section: No Change In Synaptotagmin Expression or Synaptic Localizationsupporting

confidence: 83%

“…This result differs from BoTxA studies in which inhibition of transmitter release by the toxin can be reversed by increasing intracellular Ca 2ϩ (36,39). Together these data suggest that whereas a small C-terminal fragment of SNAP-25 may be important for an interaction that determines Ca 2ϩ sensitivity, the full SNARE complex is important for determining Ca 2ϩ cooperativity.…”

Section: No Change In Synaptotagmin Expression or Synaptic Localizationcontrasting

confidence: 54%

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SNARE proteins contribute to calcium cooperativity of synaptic transmission

Stewart

Mohtashami

Trimble

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

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A hallmark of calcium-triggered synaptic transmission is the cooperative relationship between calcium and the amount of transmitter released. This relationship is thought to be important for improving the efficiency of synaptic vesicle exocytosis. Although it is generally held that cooperativity arises from the interaction of multiple calcium ions with a single calcium-sensing molecule, the precise molecular basis of this phenomenon is not known. The SNARE proteins are known to be critical for synaptic vesicle exocytosis. We therefore tested for a contribution of SNARE proteins to cooperativity by genetically reducing the levels of syntaxin IA and neuronal-synaptobrevin in Drosophila. Surprisingly, we found that reducing these SNARE proteins also reduced Ca 2؉ cooperativity. Thus, SNARE proteins are important for determining the cooperative relationship between calcium and synaptic transmission.

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Section: No Change In Synaptotagmin Expression or Synaptic Localizationsupporting

confidence: 83%

Section: No Change In Synaptotagmin Expression or Synaptic Localizationcontrasting

confidence: 54%

SNARE proteins contribute to calcium cooperativity of synaptic transmission

Stewart

Mohtashami

Trimble

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

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“…Moreover, transmitter release was observed in toxin-treated cultures during repetitive firing of presynaptic neurons, a condition of neuronal activity associated with a high concentration of Ca 2+ -ions in presynaptic terminals. the conclusion that blockade of synaptic transmission by botulinum toxin A is overridden by high Ca 2+ is also backed by in vivo studies and by investigations using the nervus phrenicus diaphragm preparation (Burgen et al, 1949;Cull-Candy et al, 1976;Humeau et al, 2000). In summary, the results of the present study, namely that incobotulinumtoxin A reduced muscle activity to a large extent, but did not completely abolish muscle contractions, is clearly in accordance with the reported effects of botulinum toxin A as observed in several experimental preparations.…”

Section: Actions Of Botulinum Toxins At the Neuromuscular Junctionsupporting

confidence: 79%

Spinal cord - skeletal muscle cocultures detect muscle-relaxant action of botulinum neurotoxin A

Eckle

Drexler

Grasshoff

et al. 2014

ALTEX

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“…In intact cells, evoked membrane fusion involves the cooperative action of multiple SNARE complexes (Cull-Candy et al, 1976;Bevan and Wendon, 1984;Stewart et al, 2000). The exact number of complexes required is currently unknown, and estimates vary from three (Hua and Scheller, 2001) to five to eight (Han et al, 2004) to 10 -15 (Keller and Neale, 2001;Keller et al, 2004;Montecucco et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

A Role for Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor Complex Dimerization during Neurosecretion

Fdez

Jowitt

Wang

et al. 2008

MBoC

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The interactions underlying the cooperativity of soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes during neurotransmission are not known. Here, we provide a molecular characterization of a dimer formed between the cytoplasmic portions of neuronal SNARE complexes. Dimerization generates a two-winged structure in which the C termini of cytosolic SNARE complexes are in apposition, and it involves residues from the vesicleassociated SNARE synaptobrevin 2 that lie close to the cytosol-membrane interface within the full-length protein.Mutation of these residues reduces stability of dimers formed between SNARE complexes, without affecting the stability of each individual SNARE complex. These mutations also cause a corresponding decrease in the ability of botulinum toxin-resistant synaptobrevin 2 to rescue regulated exocytosis in toxin-treated neuroendocrine cells. Moreover, such synaptobrevin 2 mutants give rise to a dominant-negative inhibition of exocytosis. These data are consistent with an important role for SNARE complex dimers in neurosecretion.

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Effects of botulinum toxin on neuromuscular transmission in the rat.

Cited by 228 publications

References 38 publications

SNARE proteins contribute to calcium cooperativity of synaptic transmission

SNARE proteins contribute to calcium cooperativity of synaptic transmission

Spinal cord - skeletal muscle cocultures detect muscle-relaxant action of botulinum neurotoxin A

A Role for Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor Complex Dimerization during Neurosecretion

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