J. Gen. Physiol.
© The Rockefeller University Press
0022-1295/97/04/435/14 $2.00
Volume 109, Number 4, April 1997 435-448

Fast Inactivation of Delayed Rectifier K Conductance in Squid Giant Axon and Its Cell Bodies

Chris Mathes,^* Joshua J.C. Rosenthal,^* Clay M. Armstrong, and William F. Gilly^*

From the ^* Hopkins Marine Station, Department of Biological Sciences, Stanford University, Pacific Grove, California 93950; and  Department of Physiology, University of Pennsylvania, Philadelphia, Pennsylvania 19104

Inactivation of delayed rectifier K conductance (g_K) was studied in squid giant axons and in the somata of giant fiber lobe (GFL) neurons. Axon measurements were made with an axial wire voltage clamp by pulsing to V_K (~10 mV in 50-70 mM external K) for a variable time and then assaying available g_K with a strong, brief test pulse. GFL cells were studied with whole-cell patch clamp using the same prepulse procedure as well as with long depolarizations. Under our experimental conditions (12-18°C, 4 mM internal MgATP) a large fraction of g_K inactivates within 250 ms at 10 mV in both cell bodies and axons, although inactivation tends to be more complete in cell bodies. Inactivation in both preparations shows two kinetic components. The faster component is more temperature-sensitive and becomes very prominent above 12°C. Contribution of the fast component to inactivation shows a similar voltage dependence to that of g_K, suggesting a strong coupling of this inactivation path to the open state. Omission of internal MgATP or application of internal protease reduces the amount of fast inactivation. High external K decreases the amount of rapidly inactivating I_K but does not greatly alter inactivation kinetics. Neither external nor internal tetraethylammonium has a marked effect on inactivation kinetics. Squid delayed rectifier K channels in GFL cell bodies and giant axons thus share complex fast inactivation properties that do not closely resemble those associated with either C-type or N-type inactivation of cloned Kv1 channels studied in heterologous expression systems.

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