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Schreibmayer, W; Dascal, N; Lotan, I; Wallner, M; Weigl, L.
Molecular mechanism of protein kinase C modulation of sodium channel alpha-subunits expressed in Xenopus oocytes.
FEBS Lett. 1991; 291(2):341-344
Doi: 10.1016%2F0014-5793%2891%2981316-Z
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- Leading authors Med Uni Graz
- Schreibmayer Wolfgang
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- Abstract:
- 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.
- Find related publications in this database (using NLM MeSH Indexing)
- Animals -
- Membrane Potentials -
- Oocytes - metabolism
- Protein Kinase C - biosynthesis
- Sodium Channels - drug effects
- Tetradecanoylphorbol Acetate - pharmacology
- Xenopus laevis - metabolism
- Find related publications in this database (Keywords)
- Sodium Channel Modulation
- Protein Kinase-C (PKC)
- Phorbol Ester
- Xenopus-Laevis
- Patch Clamp
- RNA Expression