Temperature- and structure-dependent interaction of pyrethroids with the sodium channels in frog node of Ranvier

Vijverberg, Henk P.M.; Zalm, J.M. van der; Kleef, Regina G.D.M. van; Bercken, Joep van den

doi:10.1016/0005-2736(83)90438-8

Cited by 59 publications

(16 citation statements)

References 22 publications

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“…Currents modified by type I pyrethroids decay one to several orders of magnitude faster than currents modified by type II pyrethroids (Vijverberg et al 1983, Lund & Narahashi 1983). However, the range of decay rates within a group is also one to two orders of magnitude, and one study reported that certain pyrethroids did not fit clearly into one group or the other but were intermediate between the members of the two groups (Lund & Narahashi 1983).…”

Section: The Pyrethroidsmentioning

confidence: 98%

“…Therefore, the two groups are best viewed as representing the polar ends of a continuous spectrum of activity. Vijverberg et al (1983) applied transition rate theory to describe the decay of the pyrethroid-modifi ed currents. By measuring the rates at different temperatures, they were able to obtain values of the enthalpy and entropy, and thus the free energy, of the first-order process.…”

Section: The Pyrethroidsmentioning

confidence: 99%

See 1 more Smart Citation

An Integrated view of the Molecular Toxinology of Sodium Channel Gating in Excitable Cells

Strichartz¹,

Rando²,

Wang³

1987

Annu. Rev. Neurosci.

216

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The neurotoxins that modify Na channels have actions that are characterized by different degrees of specificity (Table 2). These specificities can be correlated with their chemical properties. For example, guanidinium toxins, which are small charged ligands, appear only to "block" Na channels by binding to a site on the external surface. Peptide toxins, which are also positively charged and relatively small, also act from the external solution to modify channel activation and inactivation processes but do not alter ion selectivity. The lipophilic toxins, hydrophobic, neutral drugs, act from either side of the membrane and modify all the functions of Na channels. From such differences, and from the independence of toxin binding as well as toxin action, separate binding sites for these agents have been classified (Catterall 1980). Recent findings reviewed here suggest that all these toxins share certain features: They differentiate between various states of the channel. Effects of lipophilic activators, polypeptide toxins, and, indeed, even STX and TTX are enhanced or reversed in fractions of seconds under voltage clamp by patterns of membrane potential that selectively populate the channel open state, or the slow or fast inactivated states. Other assays--such as the binding of radiolabeled ligands or the changes of steady-state Na flux that require seconds to minutes of toxin-channel interaction--reveal interactions of the toxins with states of the channel not detected in the usual voltage-clamp analysis. Pharmacological probes may thus reveal channel states or transitions previously unrecognized. The bound toxins appear to interact with one another. The well-documented synergism at equilibrium of alpha-toxins with lipophilic activators provided a model for allosteric interactions between two separate binding sites (Catterall 1979, 1980). The other toxin interactions are more ephemeral and are characterized by kinetic variations that reflect the availability of reactive channel states. For example, the appearance of beta-toxin induced modifications of Na currents is accelerated in the presence of alpha-toxin (Wang & Strichartz 1983), whereas the modifications of inactivation by alpha-toxins are prevented by concurrent incubation with tetrodotoxin, although such modifications, once effected, are not reversed by the subsequent addition of TTX. Modifications of gating by lipophilic toxins confer a selective voltage-dependence on STX and TTX inhibition of open channels that is not observed in drug-free channels.(ABSTRACT TRUNCATED AT 400 WORDS)

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Section: The Pyrethroidsmentioning

confidence: 98%

Section: The Pyrethroidsmentioning

confidence: 99%

An Integrated view of the Molecular Toxinology of Sodium Channel Gating in Excitable Cells

Strichartz¹,

Rando²,

Wang³

1987

Annu. Rev. Neurosci.

216

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“…Based on electrophysiological studies in invertebrates (Lund and Narahashi 1983;Narahashi 1983Narahashi , 1985Laufer et al 1985) and amphibians (Vijverberg and van den Bercken 1982;Vijverberg et al 1983;Vijverberg and deWeille 1985;Ruight and van den Bercken 1986), it seems likely that the mechanism of pyrethroid action is associated with the nerve membrane sodium channel. Type I pyrethroids (see Section IIIB for a discussion of Type I and Type II pyrethroids) cause repetitive discharges in nerve fibers as a result of prolongation of sodium current.…”

Section: A Mode Of Actionmentioning

confidence: 98%

Comparative Toxicology of the Pyrethroid Insecticides

Bradbury¹,

Coats

1989

Reviews of Environmental Contamination and Toxicology

278

142

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“…The symptoms of pyrethroid insecticide poisoning are characterized by hyperexcitation and convulsions followed by paralysis [2]. The main target site of the pyrethroids has been identified to be the Na + channels, which are kept open for unusually long periods of time, causing a prolonged Na + current to flow, which, in turn, leads to hyperexcitation of the nervous system [3].…”

Section: Introductionmentioning

confidence: 99%

Interaction of pyrethroids with ion transport pathways present in frog skin

Cassano

Bellantuono

Quaranta

et al. 2000

Enviro Toxic and Chemistry

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Abstract-We measured the ability of deltamethrin and permethrin to stimulate the ion transport operated by the frog skin. Ion transport was monitored by measuring the short-circuit current. Deltamethrin and permethrin, added to the fluid bathing the internal surface of the isolated frog skin, showed a seasonal feature and were more effective in increasing short-circuit current in the period between June and October. Transepithelial influxes and outfluxes of 22 Na ϩ and 36 Cl Ϫ across symmetrical parts of the short-circuited skin were then measured. Deltamethrin was found to increase net Na ϩ absorption and, to a lesser extent, Cl Ϫ secretion. The presence of a Cl Ϫ secretory mechanism is supported by two observations, those being that the short-circuit current value, recorded when deltamethrin and amiloride (inhibitor of Na ϩ channels) were simultaneously present, was higher than that obtained in the presence of amiloride alone and that bumetanide, a classic inhibitor of Cl Ϫ secretion, completely inhibited the component of the Cl Ϫ outflux that was induced by the deltamethrin stimulation. The stimulations of short-circuit current respectively caused by deltamethrin (type II pyrethroid) and permethrin (type I) were comparable and similarly affected by indomethacin (an inhibitor of cyclooxygenase) and W7 (an inhibitor of the Ca 2ϩ /calmodulin system). These findings suggest that, in frog skin, the cellular mechanism of action of type I and type II pyrethroids is similar.

show abstract

Temperature- and structure-dependent interaction of pyrethroids with the sodium channels in frog node of Ranvier

Cited by 59 publications

References 22 publications

An Integrated view of the Molecular Toxinology of Sodium Channel Gating in Excitable Cells

An Integrated view of the Molecular Toxinology of Sodium Channel Gating in Excitable Cells

Comparative Toxicology of the Pyrethroid Insecticides

Interaction of pyrethroids with ion transport pathways present in frog skin

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