Document Detail

Molecular mechanism of protein kinase C modulation of sodium channel alpha-subunits expressed in Xenopus oocytes.
MedLine Citation:
PMID:  1657647     Owner:  NLM     Status:  MEDLINE    
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.
W Schreibmayer; N Dascal; I Lotan; M Wallner; L Weigl
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  FEBS letters     Volume:  291     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1991 Oct 
Date Detail:
Created Date:  1991-12-09     Completed Date:  1991-12-09     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  341-4     Citation Subset:  IM    
Institute of Medical Physics and Biophysics, Karl-Franzens University Graz, Austria.
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MeSH Terms
Membrane Potentials
Oocytes / metabolism*
Protein Kinase C / biosynthesis,  physiology*
Sodium Channels / drug effects,  enzymology*
Tetradecanoylphorbol Acetate / pharmacology
Xenopus laevis / metabolism*
Reg. No./Substance:
0/Sodium Channels; 16561-29-8/Tetradecanoylphorbol Acetate; EC Kinase C

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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