ArticleBritish journal of pharmacology2013
Co-expression of Na(V)β subunits alters the kinetics of inhibition of voltage-gated sodium channels by pore-blocking μ-conotoxins.
Article in British journal of pharmacology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 59 citations in OpenAlex.
- The double-edged sword of ion channel-targeting pesticides: a paradigm shift from health risks to precision intervention.Archives of toxicology · 2026Review
- From marine predator to pharmacology: Conotoxin diversity, discovery, and therapeutic potential.Zoological research · 2026Review
- Marine-derived bioactive compounds for neuropathic pain: pharmacology and therapeutic potential.Naunyn-Schmiedeberg's archives of pharmacology · 2025Review
- Article
- Sodium Channel β Subunits-An Additional Element in Animal Tetrodotoxin Resistance?International journal of molecular sciences · 2024Article
- Review
- Identification of sodium channel toxins from marine cone snails of the subgenera Textilia and Afonsoconus.Cellular and molecular life sciences : CMLS · 2023Article
- Pain-causing stinging nettle toxins target TMEM233 to modulate NaNature communications · 2023Article
- Historical Perspective of the Characterization of Conotoxins Targeting Voltage-Gated Sodium Channels.Marine drugs · 2023Review
- Computational design of peptides to target NaeLife · 2022Article
- Article
- Pharmacological determination of the fractional block of Nav channels required to impair neuronal excitability andFrontiers in cellular neuroscience · 2022Article
- Evidence that toxin resistance in poison birds and frogs is not rooted in sodium channel mutations and may rely on "toxin sponge" proteins.The Journal of general physiology · 2021Article
- The Voltage-Gated Sodium Channel Beta4 Subunit Maintains Epithelial Phenotype in Mammary Cells.Cells · 2021Article
- Spider venom-derived peptide induces hyperalgesia in NaNature communications · 2020Article
- Venom-Derived Peptide Modulators of Cation-Selective Channels: Friend, Foe or Frenemy.Frontiers in pharmacology · 2019Review
- Selective NaProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Heat-resistant action potentials require TTX-resistant sodium channels NaThe Journal of general physiology · 2018Article
- Determination of the μ-Conotoxin PIIIA Specificity Against Voltage-Gated Sodium Channels from Binding Energy Calculations.Marine drugs · 2018Article
- Voltage-gated sodium channel β subunits: The power outside the pore in brain development and disease.Neuropharmacology · 2018Review
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
background and purposeVoltage-gated sodium channels (VGSCs) are assembled from two classes of subunits, a pore-bearing α-subunit (NaV 1) and one or two accessory β-subunits (NaV βs). Neurons in mammals can express one or more of seven isoforms of NaV 1 and one or more of four isoforms of NaV β. The peptide μ-conotoxins, like the guanidinium alkaloids tetrodotoxin (TTX) and saxitoxin (STX), inhibit VGSCs by blocking the pore in NaV 1. Hitherto, the effects of NaV β-subunit co-expression on the activity of these toxins have not been comprehensively assessed. EXPERIMENTAL APPROACH: Four μ-conotoxins (μ-TIIIA, μ-PIIIA, μ-SmIIIA and μ-KIIIA), TTX and STX were tested against NaV 1.1, 1.2, 1.6 or 1.7, each co-expressed in Xenopus laevis oocytes with one of NaV β1, β2, β3 or β4 and, for NaV 1.7, binary combinations of thereof. KEY
resultsCo-expression of NaV β-subunits modifies the block by μ-conotoxins: in general, NaV β1 or β3 co-expression tended to increase kon (in the most extreme instance by ninefold), whereas NaV β2 or β4 co-expression decreased kon (in the most extreme instance by 240-fold). In contrast, the block by TTX and STX was only minimally, if at all, affected by NaV β-subunit co-expression. Tests of NaV β1 : β2 chimeras co-expressed with NaV 1.7 suggest that the extracellular portion of the NaV β subunit is largely responsible for altering μ-conotoxin kinetics. CONCLUSIONS AND IMPLICATIONS: These results are the first indication that NaV β subunit co-expression can markedly influence μ-conotoxin binding and, by extension, the outer vestibule of the pore of VGSCs. μ-Conotoxins could, in principle, be used to pharmacologically probe the NaV β subunit composition of endogenously expressed VGSCs.
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