ArticleBritish journal of pharmacology2003
Tityustoxin-K(alpha) blockade of the voltage-gated potassium channel Kv1.3.
Article in British journal of pharmacology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- The First KToxins · 2025Article
- Characterization and Chemical Synthesis of Cm39 (α-KTx 4.8): A Scorpion Toxin That Inhibits Voltage-Gated KToxins · 2023Article
- Ion Channels Orchestrate Pancreatic Ductal Adenocarcinoma Progression and Therapy.Frontiers in pharmacology · 2020Review
- Effects of Brazilian scorpion venoms on the central nervous system.The journal of venomous animals and toxins including tropical diseases · 2018Review
- Use-dependent activation of neuronal Kv1.2 channel complexes.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Article
- Article
- Cellular mechanisms and behavioral consequences of Kv1.2 regulation in the rat cerebellum.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- Article
- Variable threshold of trigeminal cold-thermosensitive neurons is determined by a balance between TRPM8 and Kv1 potassium channels.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009Article
- Kv1 channels selectively prevent dendritic hyperexcitability in rat Purkinje cells.The Journal of physiology · 2005Article
- K+ currents activated by depolarization in cardiac fibroblasts.Biophysical journal · 2005Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
1. We investigated the action of TsTX-Kalpha on cloned Kv1.3 channels of the Shaker subfamily of voltage-gated potassium channels, using the voltage-clamp technique. Highly purified TsTX-Kalpha was obtained from the venom of the Brazilian scorpion Tityus serrulatus using a new purification protocol. Our results show that TsTX-Kalpha blocks Kv1.3 with high affinity in two expression systems. 2. TsTX-Kalpha blockade of Kv1.3 channels expressed in Xenopus oocytes was found to be completely reversible and to exhibit a pH dependence. The K(D) was 3.9 nM at pH 7.5, 9.5 nM at pH 7.0 and 94.5 nM at pH 6.5. 3. The blocking properties of TsTX-Kalpha in a mammalian cell line (L929), stably transfected to express Kv1.3, were studied using the patch-clamp technique. In this preparation, the toxin had a K(D) of 19.8 nM at pH 7.4. 4. TsTX-Kalpha was found to affect neither the voltage-dependence of activation, nor the activation and deactivation time constants. The block appeared to be independent of the transmembrane voltage and the toxin did not interfere with the C-type inactivation process. 5. Taken as a whole, our findings indicate that TsTX-Kalpha acts as a simple blocker of Kv1.3 channels. It is concluded that this toxin is a useful tool for probing not only the physiological roles of Kv1.2, but also those mediated by Kv1.3 channels.
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