Effects of n-dodecylguanidine on A-type potassium channels: role of external surface charges in channel gating
n-Dodecylguanidine (C12-G) is an amphipathic compound with a guanidine moiety, which is positively charged at physiological pH, and a hydrophobic side chain. Its effects on an A-type K+ channel clone (rKv1.4) expressed in Xenopus oocytes were examined. C12-G caused a concentration-dependent (1-20 mi...
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Veröffentlicht in: | Molecular pharmacology 1995-07, Vol.48 (1), p.160-171 |
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Zusammenfassung: | n-Dodecylguanidine (C12-G) is an amphipathic compound with a guanidine moiety, which is positively charged at physiological
pH, and a hydrophobic side chain. Its effects on an A-type K+ channel clone (rKv1.4) expressed in Xenopus oocytes were examined.
C12-G caused a concentration-dependent (1-20 microM) positive shift in the voltage dependences of the following channel properties:
activation, inactivation, rate of decay during depolarization, and rate of recovery from inactivation. C12-G was effective
when added to the bath solution but was without effect when applied to the cytoplasm of oocytes, indicating an extracellular
site of action. The effects of C12-G were antagonized by elevation of the extracellular Mg2+ concentration and by external
guanidine ions but were augmented by lowering of the ionic strength of the external solution. C12-G did not affect the instantaneous
current-voltage relationship for rKv1.4 or the time constant of decay during strong depolarizations, when the voltage dependence
of channel activation approached a plateau. Our observations suggest that C12-G exerts its actions by causing a positive shift
in the external surface potential around rKv1.4, without altering the ion permeation process or voltage-independent transition
steps. In canine ventricular myocytes, C12-G caused changes in the function of a native A-type K+ channel similar to those
seen with rKv1.4. However, C12-G had negligible effects on the voltage dependence of the slow delayed-rectifier K+ channel
in the same cell type, suggesting that the actions of C12-G are not nonspecific. |
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ISSN: | 0026-895X 1521-0111 |