ArticleToxicon : official journal of the International Society on Toxinology2008
Evidence for multiple effects of ProTxII on activation gating in Na(V)1.5.
Article in Toxicon : official journal of the International Society on Toxinology, 2008. 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, 22 citations in OpenAlex.
- Ion Channel-Targeting Toxins: Structural Mechanisms of Activation, Inhibition, and Therapeutic Potential.Toxins · 2025Review
- State-Dependent Inhibition of Nav1.8 Sodium Channels by VX-150 and VX-548.Molecular pharmacology · 2024Article
- Molecular Interactions between Tarantula Toxins and Low-Voltage-Activated Calcium Channels.Scientific reports · 2016Article
- The hitchhiker's guide to the voltage-gated sodium channel galaxy.The Journal of general physiology · 2016Review
- Gating-pore currents demonstrate selective and specific modulation of individual sodium channel voltage-sensors by biological toxins.Molecular pharmacology · 2014Article
- Animal toxins influence voltage-gated sodium channel function.Handbook of experimental pharmacology · 2014Review
- Palmitoylation influences the function and pharmacology of sodium channels.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Inhibition of the activation pathway of the T-type calcium channel Ca(V)3.1 by ProTxII.Toxicon : official journal of the International Society on Toxinology · 2010Article
- Sodium channelopathies and pain.Pflugers Archiv : European journal of physiology · 2010Review
- Targeting voltage sensors in sodium channels with spider toxins.Trends in pharmacological sciences · 2010Review
- Target promiscuity and heterogeneous effects of tarantula venom peptides affecting Na+ and K+ ion channels.The Journal of biological chemistry · 2010Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The peptide toxin ProTxII, recently isolated from the venom of the tarantula spider Thrixopelma pruriens, modifies gating in voltage-gated Na+ and Ca2+ channels. ProTxII is distinct from other known Na+ channel gating modifier toxins in that it affects activation, but not inactivation. It shifts activation gating positively and decreases current magnitude such that the dose-dependence of toxin action measured at a single potential reflects both effects. To test the extent to which these effects were independent, we tracked several different measures of current amplitude, voltage-dependent activation, and current kinetics in Na(V)1.5 in a range of toxin concentrations. Changes in voltage dependence and a decrease in G(max) appeared at relatively low concentrations (40-100 nM) while a positive shift in the voltage range of activation was apparent at higher toxin concentrations (> or =500 nM). Because ProTxII carries a net +4 charge we tested whether electrostatic interactions contributed to toxin action. We examined the effects of ProTxII in the presence of high extracellular Ba2+, known to screen and/or bind to surface charge. Some, but not all aspects of ProTxII modification were sensitive to the presence of Ba2+ indicating the contribution of an electrostatic, surface charge-like mechanism and supporting the idea of a multi-faceted toxin-channel interaction.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.