Literature DB >> 2422660

Potassium conductance of the squid giant axon is modulated by ATP.

F Bezanilla, C Caputo, R DiPolo, H Rojas.   

Abstract

This communication reports a modulating effect of intracellular ATP on the steady-state and kinetic properties of the delayed rectifier of the giant axon of the squid. When internally dialyzed or perfused giant axons from Loligo plei or Loligo pealei are voltage clamped at -60 mV and washed free of ATP, the potassium current at 0 mV is decreased, and the time course of the potassium current is faster. Upon readmitting ATP, the potassium current for pulses to potentials more positive than -30 mV is increased by a factor of up to 2.5, while for pulses to potentials more negative than -30 mV, it is decreased. In the presence of ATP the turn-on of the time course of the potassium current is slower, but the turn-off of the time course is faster. The effect of ATP is only observed when magnesium ions are present in the internal medium; ADP or the nonhydrolyzable ATP analogue adenosine 5'-[beta, gamma-methylene]-triphosphate has no effect. When the holding potential is -70 mV, the conductance-voltage curve is shifted to more positive potentials by ATP, but the maximum conductance is only slightly increased. Most of the effects of ATP may be explained by a phosphorylation step that alters the voltage sensor of the activation and inactivation gates of the potassium channels shifting the voltage dependence of both processes to more depolarized potentials.

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Year:  1986        PMID: 2422660      PMCID: PMC323376          DOI: 10.1073/pnas.83.8.2743

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  6 in total

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3.  Voltage dependence of the Na/Ca exchange in voltage-clamped, dialyzed squid axons. Na-dependent Ca efflux.

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5.  Divalent cations and the activation kinetics of potassium channels in squid giant axons.

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6.  Sodium extrusion by internally dialyzed squid axons.

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  6 in total
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Review 4.  Phosphorylation of K+ channels in the squid giant axon. A mechanistic analysis.

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