The crude extract of glands appended to the jaws of the polychaete annelid Glycera convoluta induces an important increase in the spontaneous quantal transmitter release on frog and crayfish neuromuscular junctions and on Torpedo nerve-electroplaque junctions. The venom similarly triggers acetylcholine (ACh) release from synaptosomes purified from Torpedo electric organ. At the frog neuromuscular junction, the reproducibility, the reversibility and the dose-dependence of the venom action permit a quantitative evaluation of the effect. The crude venom extract has been fractionated by gel-filtration. The effect on transmitter release has been found in a high molecular weight fraction distinct from those which contain the protease and phospholipase activities.
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J Cell Sci
April 2010
Molecular Dynamics of Synaptic Function Laboratory, Queensland Brain Institute and School of Biomedical Sciences, The University of Queensland, Brisbane, QLD 4072, Australia.
Glycerotoxin (GLTx), a large neurotoxin isolated from the venom of the sea worm Glycera convoluta, promotes a long-lasting increase in spontaneous neurotransmitter release at the peripheral and central synapses by selective activation of Ca(v)2.2 channels. We found that GLTx stimulates the very high frequency, long-lasting (more than 10 hours) spontaneous release of acetylcholine by promoting nerve terminal Ca(2+) oscillations sensitive to the inhibitor omega-conotoxin GVIA at the amphibian neuromuscular junction.
View Article and Find Full Text PDFEMBO J
December 2002
Molecular Neuropathobiology Laboratory, Cancer Research UK, London Research Institute, Lincoln's Inn Fields Laboratories, 44 Lincoln's Inn Fields, London WC2A 3PX, UK.
We report here the purification of glycerotoxin from the venom of Glycera convoluta, a novel 320 kDa protein capable of reversibly stimulating spontaneous and evoked neurotransmitter release at the frog neuromuscular junction. However, glycerotoxin is ineffective at the murine neuromuscular junction, which displays a different subtype of voltage- dependent Ca(2+) channels. By sequential and selective inhibition of various types of Ca(2+) channels, we found that glycerotoxin was acting via Ca(v)2.
View Article and Find Full Text PDFThe presynaptic plasma membrane (PSPM) of cholinergic nerve terminals was purified from Torpedo electric organ using a large-scale procedure. Up to 500 g of frozen electric organ were fractioned in a single run, leading to the isolation of greater than 100 mg of PSPM proteins. The purity of the fraction is similar to that of the synaptosomal plasma membrane obtained after subfractionation of Torpedo synaptosomes as judged by its membrane-bound acetylcholinesterase activity, the number of Glycera convoluta neurotoxin binding sites, and the binding of two monoclonal antibodies directed against PSPM.
View Article and Find Full Text PDFNeurochem Int
October 2012
Unité des Venins, Institut Pasteur, 28, rue du Dr Roux, 75015 Paris, France.
The venom secreted from glands appended to the jaws of Glycera convoluta, a Polychaete Annelid, increases the spontaneous quantal release of transmitter from nerve terminals. The component that is biologically active on vertebrate cholinergic nerve terminals has recently been shown to be a high molecular weight protein. In the present work, the crude extract from the venom apparatus was shown to be toxic for mammals and crustaceans.
View Article and Find Full Text PDFThe membrane potential of purely cholinergic synaptosomes isolated from Torpedo electric organ was monitored with fluorescent carbocyanine dyes. An increased fluorescence was associated with depolarization and a quenching with hyperpolarization. Fluorescence data provided evidence that Torpedo synaptosomes have a membrane potential mainly driven by a K+ diffusion potential and a membrane potential of about -50 mV could be estimated after calibration of fluorescence signals with ionophore antibiotics.
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