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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Pflügers Archiv 427 (1994), S. 399-405 
    ISSN: 1432-2013
    Keywords: Sodium channel ; Oocyte ; Patch clamp
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Na currents recorded from inside-out macropatches excised from Xenopus oocytes expressing the α subunit of the rat brain Na channel IIA show at least two distinguishable components in their inactivation time course, with time constants differing about tenfold (τ h1 = approx. 150 μs and τ h2 = approx. 2 ms). In excised patches, the inactivation properties of Na currents changed with time, favoring the faster inactivation kinetics. Analysis of the fast and slow current kinetics shows that only the relative magnitudes of τ h1 and τ h2 components are altered without significant changes in the time constants of activation or inactivation. In addition, voltage dependence of both activation and steady-state inactivation of Na currents are shifted to more negative potentials in patches with predominantly fast inactivation, although reversal potentials and valences remained unaltered. We conclude that the two inactivation modes discerned in this study are conferred by two states of Na channel the interconversion of which are regulated by an as yet unknown mechanism that seems to involve cytosolic factors.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2013
    Keywords: Sodium channel ; Oocyte ; Patch clamp
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Macroscopic currents of wild-type rat brain IIA (RBIIA) and mutant Na channels were recorded in excised patches from Xenopus oocytes. A charge deletion (K859Q) and an adjacent conservative mutation (L860F) in the second domain S4 membrane-spanning region differentially altered voltage sensitivity and kinetics. Analysis of voltage dependence was confined to Na currents with fast inactivation kinetics, although RBIIA and K859Q (but not L860F) also showed proportional shifts between at least two gating modes, rendering currents with fast or slow inactivation kinetics, respectively. Compared to RBIIA, the midpoint of the activation curve was shifted in both K859Q and L860F by 22 mV to more positive potentials, yet this shift was not associated with a corresponding change in the voltage dependence of time constants for activation (τ a) or inactivation (τ h1, τ h2). L860F showed faster activation time constants τ a than RBIIA, while K859Q was slower for both the activation (τ a) and the inactivation components (τ h1). Similarly, the steady-state inactivation curve of L860F but not K859Q shifted by 9 mV in the hyperpolarizing direction. Thus, the fourth charge in the IIS4 transmembrane segment exerts control over voltage sensitivity and kinetics of activation and may interact with structure that influence other aspects of channel gating.
    Type of Medium: Electronic Resource
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