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. 1984 May;350:429–445. doi: 10.1113/jphysiol.1984.sp015210

The asymmetrical effects of some ionized n-octyl derivatives on the sodium current of the giant axon of Loligo forbesi.

J R Elliott, D A Haydon, B M Hendry
PMCID: PMC1199278  PMID: 6747855

Abstract

The effects of octyltrimethylammonium ions (OTMA+), octyl sulphate ions (OS-) and octanoic acid (OA) on the sodium current of the voltage-clamped squid giant axon have been investigated using intracellular and extracellular application of the test substances. OTMA+ applied externally at concentrations of 0.8-5.0 mM produces a small reversible increase in the peak inward sodium current in both intact and CsF-perfused axons. Intracellular application of OTMA+ at 0.8 mM to CsF-perfused axons causes a reversible 50% suppression of peak inward sodium current. The inhibition of peak inward current by internal OTMA+ arises largely from a shift of the steady-state activation parameter (m infinity) in the depolarizing direction along the voltage axis. There is little use dependence of the current suppression by OTMA+ OA applied either internally or externally is more effective at suppressing peak inward sodium current at pH 6.0 than at pH 7.4. At pH 6.0 external application of 5 mM-OA to perfused axons causes approximately 60% suppression. This is associated with a depolarizing shift of m infinity of about 13 mV and a hyperpolarizing shift of the steady-state inactivation (h infinity) curve of about 4 mV. The effects of internal and external OA are broadly similar except that the h infinity shift is not seen with internal application. OS- at concentrations above 2.0 mM produces complete irreversible loss of sodium current. At 2.0 mM, OS- produces 10% current suppression and a small depolarizing shift of the m infinity curve. Internal and external applications of OS- differ little except that external OS- causes a 25% increase in the time constant of activation (tau m). The possible origins of these effects are discussed. It is proposed that the shift of m infinity caused by internal OTMA+ is due to a diminution of the lipid dipole potential at the internal surface of the membrane caused by OTMA+ adsorption. This effect could also account for the m infinity shift caused by OA. The results showing that OA produces shifts of opposite sign in the voltage dependence of m infinity and h infinity are discussed with respect to their implications for models of sodium channel gating.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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