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Molecular Pharmacology

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Abstract

Polypeptide toxins from the venoms of Old World and New World scorpions preferentially block different potassium channels.

M P Blaustein, R S Rogowski, M J Schneider and B K Krueger
Molecular Pharmacology December 1991, 40 (6) 932-942;
M P Blaustein
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R S Rogowski
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M J Schneider
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B K Krueger
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Abstract

Venoms from five Old World and two New World scorpions were tested for their ability to block various K+ channels in rat brain synaptosomes. A 86Rb efflux kinetic assay was used to identify three types of K+ channels, Ca(2+)-independent, voltage-gated, inactivating (A-type) and noninactivating (delayed rectifier) K+ channels and Ca(2+)-activated K+ channels [J. Physiol. (Lond.) 361:419-440, 441-457 (1985)]. The venoms from the Old World scorpions all blocked the A-type K+ channel but not the delayed rectifier K+ channel; only venom from the Israeli scorpion, Leiurus quinqestriatus hebraeus (Lqh), blocked the Ca(2+)-activated K+ channel. In contrast, venoms from the two New World scorpions selectively blocked the delayed rectifier K+ channel. Water-soluble components from Lqh venom from the Brazillian scorpion, Tityus serrulatus (Ts), were separated by ion exchange high performance liquid chromatography (HPLC). Seven components that blocked synaptosome K+ channels were isolated from Lqh venom by ion exchange HPLC. All seven components blocked the A-type K+ channel; the five most potent toxins had IC50 values of 18-40 nM. Two of the components from Lqh venom (one identified as charybdotoxin and the other denoted as Lqk4) also blocked a Ca(2+)-activated K+ channel (IC50 = 15 and 60 nM for charybdotoxin and Lqk4, respectively). Five K+ channel-blocking components were isolated from the Ts venom; all five blocked the delayed rectifier channel selectively, and the two most potent components had IC50 values of 8 and 30 nM. Several of the more potent Lqh and Ts toxins were purified to near-homogeneity by reverse phase HPLC. These toxins should be useful as ligands for K+ channel purification, for elucidation of K+ channel structure, and for studies of K+ channel function.

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Molecular Pharmacology
Vol. 40, Issue 6
1 Dec 1991
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Abstract

Polypeptide toxins from the venoms of Old World and New World scorpions preferentially block different potassium channels.

M P Blaustein, R S Rogowski, M J Schneider and B K Krueger
Molecular Pharmacology December 1, 1991, 40 (6) 932-942;

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Abstract

Polypeptide toxins from the venoms of Old World and New World scorpions preferentially block different potassium channels.

M P Blaustein, R S Rogowski, M J Schneider and B K Krueger
Molecular Pharmacology December 1, 1991, 40 (6) 932-942;
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