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XB-ART-24450
FEBS Lett 1991 Oct 21;2912:341-4.
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Molecular mechanism of protein kinase C modulation of sodium channel alpha-subunits expressed in Xenopus oocytes.

Schreibmayer W , Dascal N , Lotan I , Wallner M , Weigl L .


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The mechanism of modulation of sodium channel alpha-subunits (Type IIA) by a protein kinase C (PKC) activator was studied on single channel level. It was found that: (i) time constants for channel activation were prolonged; (ii) inactivation remained virtually unchanged; (iii) peak sodium inward current was reduced as evidenced by calculation of average sodium currents; and (iv) time constants for current activation and decay were prolonged. (i), (iii) and (iv) were voltage dependent, being most prominent at threshold potentials. The data show that a voltage dependent action on the activation gate can account for the observed reduction of peak inward sodium current and prolongation of current decay in macroscopic experiments.

???displayArticle.pubmedLink??? 1657647
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