ArticleNeuroscience bulletin2012
Pharmacological kinetics of BmK AS, a sodium channel site 4-specific modulator on Nav1.3.
Article in Neuroscience bulletin, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Scorpion venom peptides: Novel therapeutic approaches for inflammatory and hepatic disorders.iLIVER · 2026Review
- The underlying mechanism of scorpion venom peptide BmK AS in reducing epilepsy seizures: mediated through dual modulation of Nav1.6 and the inflammasome pathway.Frontiers in pharmacology · 2026Article
- Scorpion (Buthus martensii Karsch) in Chinese medicine: a review of traditional uses, chemical constituents, pharmacology, and toxicology.Frontiers in pharmacology · 2025Review
- The Significant Therapeutic Effects of Chinese Scorpion: Modern Scientific Exploration of Ion Channels.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Peptides with Diverse Functions from Scorpion Venom: A Great Opportunity for the Treatment of a Wide Variety of Diseases.Iranian biomedical journal · 2023Article
- Scorpion Venom: Detriments and Benefits.Biomedicines · 2020Review
- Modulatory effects of bufalin, an active ingredient from toad venom on voltage-gated sodium channels.Molecular biology reports · 2018Article
- Voltage-dependent blockade by bupivacaine of cardiac sodium channels expressed in Xenopus oocytes.Neuroscience bulletin · 2014Article
- PKA phosphorylation reshapes the pharmacological kinetics of BmK AS, a unique site-4 sodium channel-specific modulator.Scientific reports · 2014Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
objectiveIn this study, the pharmacological kinetics of Buthus martensi Karsch (BmK) AS, a specific modulator of voltage-gated sodium channel site 4, was investigated on Na(v)1.3 expressed in Xenopus oocytes.
methodsTwo-electrode voltage clamp was used to record the whole-cell sodium current.
resultsThe peak currents of Na(v)1.3 were depressed by BmK AS over a wide range of concentrations (10, 100, and 500 nmol/L). Most remarkably, BmK AS at 100 nmol/L hyperpolarized the voltage-dependence and increased the voltage-sensitivity of steady-state activation/inactivation. In addition, BmK AS was capable of hyperpolarizing not only the fast inactivation but also the slow inactivation, with a greater preference for the latter. Moreover, BmK AS accelerated the time constant and increased the ratio of recovery in Na(v)1.3 at all concentrations.
conclusionThis study provides direct evidence that BmK AS facilitates steady-state activation and inhibits slow inactivation by stabilizing both the closed and open states of the Na(v)1.3 channel, which might result from an integrative binding to two receptor sites on the voltage-gated sodium channels. These results may shed light on therapeutics against Na(v)1.3-targeted pathology.
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