Scorpion venom inhibits carbamylcholine‐induced 86rubidium efflux from rat parotid acini
- 27 July 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 219 (2) , 451-454
- https://doi.org/10.1016/0014-5793(87)80270-3
Abstract
The muscarinic agonist carbamylcholine stimulated 5‐fold 86Rb efflux from preloaded rat parotid acini. Apamin was without effect on this carbamylcholine‐induced 86Rb efflux. By contrast, the venom from Leiurus quinquestriatus (a scorpion from Israel) inhibited non‐competitively this efflux while being without effect on the carbamylcholine‐stimulated 45Ca efflux and amylase release. This heat‐resistant inhibitory effect of the venom was destroyed by boiling in the presence of dithiothreitol. These results suggest that the venom from L. quinquestriatus contains a toxin capable to block apamin‐insensitive calcium‐activated potassium channels in rat parotid acini.Keywords
This publication has 14 references indexed in Scilit:
- Scorpion venom inhibits selectively Ca2+‐activated K+ channels in situFEBS Letters, 1986
- Identification of two toxins from scorpion (Leiurus quinquestriatus) venom which block distinct classes of calcium‐activated potassium channelFEBS Letters, 1986
- Identification of Cellular Activation Mechanisms Associated with Salivary SecretionAnnual Review of Physiology, 1986
- Leiurus quinquestriatus venom inhibits different kinds of Ca2+-dependent K+ channelsBiochimica et Biophysica Acta (BBA) - Biomembranes, 1986
- 36Cl− and 86Rb+ uptake in rat parotid acinar cellsArchives of Oral Biology, 1986
- Binding in vitro of vasoactive intestinal peptide on isolated acini of rat parotid glandsArchives of Oral Biology, 1985
- Voltage and Ca2+-activated K+ channel in baso-lateral acinar cell membranes of mammalian salivary glandsNature, 1983
- Na+ Channels with Binding Sites of High and Low Affinity for Tetrodotoxin in Different Excitable and Non‐excitable CellsEuropean Journal of Biochemistry, 1982
- Scorpion neurotoxin — A presynaptic toxin which affects both Na+ and K+ channels in axonsBiochemical and Biophysical Research Communications, 1975
- Sur les enzymes amylolytiqucs III. La β‐amylase: dosage d'activité et contrôle de l'absence d'α‐amylaseHelvetica Chimica Acta, 1948