A study on the membrane depolarization of skeletal muscles caused by a scorpion toxin, sea anemone toxin II and crotamine and the interaction between toxins
Open Access
- 19 July 1983
- journal article
- research article
- Published by Wiley in British Journal of Pharmacology
- Vol. 79 (3) , 673-680
- https://doi.org/10.1111/j.1476-5381.1983.tb10004.x
Abstract
1 Quinquestriatus toxin (QTX) isolated from the venom of a scorpion (Leiurus quinquestriatus) and sea anemone (Anemonia sulcata) toxin II enhanced the twitch response of the rat and mouse diaphragms and like crotamine (isolated from the venom of Crotalus durissus terrificus) caused spontaneous fasciculation of the muscle. 2 Trains of action potentials in muscles at 70–250 Hz, which could not be antagonized by (+)-tubocurarine, were triggered by single stimulation or occurred spontaneously after treatment with these toxins. 3 QTX and toxin II prolonged the rat muscle action potential 3 to 4 fold whereas crotamine prolonged the action potential by only 30%. 4 The membrane potential was depolarized from about −82 mV to −55 mV by crotamine 2 μg ml−1, −41 mV by toxin II 5 μg ml−1 and to −50 mV by QTX 1 μg ml−1. The concentrations to induce 50% maximal depolarization (K0.5) were 0.07, 0.15 and > 0.4 μg ml−1, respectively, for QTX, crotamine and toxin II, whereas the rates of depolarization were in the order toxin II > crotamine > QTX. The depolarizing effects of crotamine and QTX, but not of toxin II, were saturable. 5 The depolarizing effects of all three toxins were irreversible whereas the membrane potential could be restored by tetrodotoxin non-competitively. 6 Simultaneous treatment with crotamine and QTX or crotamine and toxin II at concentrations below K0.5 caused only additive effects on depolarization. 7 When the muscle was depolarized by pretreating with a saturating concentration of crotamine, the onset of depolarization by QTX was greatly retarded whereas that by toxin II was unaffected. Action potentials were further prolonged in both cases. 8 It is inferred that all three peptide toxins act at sites on the sodium channel and the binding sites for QTX and crotamine overlap to a considerable extent. On the other hand, the site for toxin II appears not to overlap with that of crotamine but may overlap with that of QTX.This publication has 39 references indexed in Scilit:
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