batrachotoxinin-a-20-alpha-benzoate has been researched along with transcainide* in 1 studies
1 other study(ies) available for batrachotoxinin-a-20-alpha-benzoate and transcainide
Article | Year |
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Transcainide: biochemical evidence for state-dependent interaction with the class I antiarrhythmic drug receptor.
The mechanism of action of the lidocaine derivative transcainide was examined using [3H]batrachotoxinin 20 alpha-benzoate, which binds specifically to and stabilizes activated states of the sodium channel. Transcainide (IC50 0.3 microM) inhibited equilibrium [3H]batrachotoxinin binding to sodium channels present on freshly isolated rat cardiac myocytes. Scatchard analysis of [3H]batrachotoxinin binding showed that transcainide both reduced maximal binding and altered the KD for [3H]batrachotoxinin binding, indicating noncompetitive, allosteric inhibition. Inhibition by transcainide of [3H]batrachotoxinin binding was reversible within 60 min. We used state-dependent [3H]batrachotoxinin binding assays to examine whether transcainide preferentially binds to activated or nonactivated sodium channels. Transcainide had little effect on the k-1 of [3H]batrachotoxinin even at concentrations 1000-fold greater than its IC50, indicating low affinity of transcainide for activated channels. However, transcainide decreased the k + 1 of [3H]batrachotoxinin at a concentration very close to its IC50 concentration for inhibiting equilibrium [3H]batrachotoxinin binding. The results are discussed in terms of a model in which transcainide inhibits [3H]batrachotoxinin binding by binding specifically to and stabilizing a nonactivated state of the cardiac sodium channel. Topics: Animals; Anti-Arrhythmia Agents; Batrachotoxins; In Vitro Techniques; Lidocaine; Male; Myocardium; Rats; Rats, Inbred Strains; Receptors, Drug; Sodium Channels | 1991 |