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ECB-ART-30413
J Physiol 1978 Jun 01;279:167-85. doi: 10.1113/jphysiol.1978.sp012338.
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Blocking effects of barium and hydrogen ions on the potassium current during anomalous rectification in the starfish egg.

Hagiwara S , Miyazaki S , Moody W , Patlak J .


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1. The blocking effects of Ba+ and H+ on the inward K current during anomalous rectification of the giant egg membrane of the starfish, Mediaster aequalis, were studied using voltage clamp techniques. 2. External Ba2+ at a low concentration (10--100 micron) suppresses the inward K current; the extent of suppression, expressed as the ratio of currents with and without Ba2+, can be described by a conventional bimolecular adsorption isotherm, K/(K + [Ba2+]o), K being an apparent dissociation constant. 3. The dissociation constant, K, decreases as the membrane potential V becomes more negative and can be expressed by K(V) = K(0) exp (zmuFV/RT), where K(0) is the K at V = 0, z is the charge of the blocking ion, and mu is a parameter for the membrane potential dependence of Ba2+ blockage. The value of mu ranges between 0.64 and 0.68. 4. Upon a sudden change in membrane potential the change in the blocking effect of Ba2+ follows first order kinetics; the forward rate constant is membrane-potential-dependent whereas the backward constant is potential-independent. 5. The blocking effect of Ba2+ appears to be independent of the activation of K channels during anomalous rectification. 6. The blocking effect of Ba2+ depends on V alone, in contrast to the activation of the K channel during anomalous rectification which depends on V--VK. 7. In these respects, the effect of Ba2+ is equivalent to the introduction of inactivation into the anomalous rectification. 8. SI2+ and Ca2+ show small but observable blocking effects only at much higher concentrations (about 10--20 mM). 9. The inward K current is suppressed when the external pH is reduced below 6.0. The blocking effect of H+ shows no significant potential dependence. The concentration dependence suggests that three H+ ions simultaneously titrate the acidic groups of each channel (pK = 5.3--5.4). 10. The implications of these results are discussed in terms of molecular models of the potassium channel of anomalous rectification and possible mechanisms of K channel inactivation.

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Genes referenced: LOC115924212 tefl

References [+] :
ADRIAN, Potassium conductance of frog muscle membrane under controlled voltage. 1962, Pubmed