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Measuring Synaptic Vesicle Endocytosis in Cultured Hippocampal Neurons
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Neurotoxic phospholipases directly affect synaptic vesicle function.

Philipp Treppmann1, Irene Brunk, Terence Afube

  • 1AG Funktionelle Zellbiologie, Institut für Integrative Neuroanatomie, Charité Centrum 2 für Grundlagenmedizin, Berlin, Germany.

Journal of Neurochemistry
|March 16, 2011
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Summary
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Snake neurotoxic phospholipases (SPANs) disrupt neurotransmission by dissociating the synaptophysin/synaptobrevin complex on synaptic vesicles. SPANs also inhibit neurotransmitter uptake, impairing nerve function.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Toxicology

Background:

  • Snake neurotoxic phospholipases (SPANs) are known to block neurotransmission at pre-synaptic nerve terminals.
  • The precise mechanisms underlying SPAN-induced neurotoxicity remain incompletely understood.

Purpose of the Study:

  • To investigate the direct effects of SPANs on synaptic vesicle protein complexes.
  • To elucidate the role of calcium ions and SPANs in synaptic vesicle function and neurotransmitter uptake.

Main Methods:

  • Experiments were conducted on isolated synaptic vesicles and synaptosomal cytosol.
  • The dissociation of synaptophysin/synaptobrevin complexes was assessed in the presence and absence of calcium ions and SPANs.
  • Lipid raft association and neurotransmitter uptake (serotonin, glutamate) were analyzed.

Main Results:

  • Taipoxin and paradoxin (SPANs) directly dissociated the synaptophysin/synaptobrevin complex on synaptic vesicles at nanomolar concentrations, independent of Ca(2+).
  • Ca(2+) alone also dissociated the complex, but SPANs disturbed lipid raft association, unlike Ca(2+).
  • SPANs, but not Ca(2+), inhibited vesicular uptake of serotonin and glutamate.

Conclusions:

  • SPANs directly alter synaptic vesicle properties independently of their phospholipase activity.
  • Both SPANs and Ca(2+) dissociate the synaptophysin/synaptobrevin complex, a step prerequisite for exocytosis.
  • SPANs contribute to neurotoxicity by preventing synaptic vesicle filling, thus inhibiting neurotransmission.