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Journal of Toxicology
Volume 2012, Article ID 103608, 9 pages
Review Article

Potassium Channels Blockers from the Venom of Androctonus mauretanicus mauretanicus

Aix-Marseille University, CNRS, UMR 7286, CRN2M, Faculté de Médecine secteur Nord, CS80011, Boulevard Pierre Dramard, 13344 Marseille Cedex 15, France

Received 2 February 2012; Accepted 16 March 2012

Academic Editor: Maria Elena de Lima

Copyright © 2012 Marie-France Martin-Eauclaire and Pierre E. Bougis. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


K+ channels selectively transport K+ ions across cell membranes and play a key role in regulating the physiology of excitable and nonexcitable cells. Their activation allows the cell to repolarize after action potential firing and reduces excitability, whereas channel inhibition increases excitability. In eukaryotes, the pharmacology and pore topology of several structural classes of K+ channels have been well characterized in the past two decades. This information has come about through the extensive use of scorpion toxins. We have participated in the isolation and in the characterization of several structurally distinct families of scorpion toxin peptides exhibiting different K+ channel blocking functions. In particular, the venom from the Moroccan scorpion Androctonus mauretanicus mauretanicus provided several high-affinity blockers selective for diverse K+ channels ( S K C a , K v 4.x, and K v 1.x K+ channel families). In this paper, we summarize our work on these toxin/channel interactions.