Abstract
In Xenopus oocytes expressing slowly activating IsK channels superfusion with the nitroso-donor S-Nitroso-Cysteine (SNOC) resulted in an increase of IsK, which was greatly enhanced when the amino acid-exchanger rBAT was coexpressed. The effects of SNOC on IsK could not be prevented by the guanylate cyclase inhibitor LY-83,583 and the cGMP kinase inhibitor H8, but was abolished in the presence of staurosporine. SNOC also increased the currents induced by the expression of protein mutants lacking intracellular sites, previously described to be involved in IsK regulation by oxidation and phosphorylation. These data suggest that the NO-donor SNOC regulates IsK indirectly via a cGMP independent, but staurosporine sensitive, pathway.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alkaloids / pharmacology
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Aminoquinolines / pharmacology
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Animals
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Cyclic GMP / physiology*
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Cyclic GMP-Dependent Protein Kinases / antagonists & inhibitors
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Cysteine / analogs & derivatives*
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Cysteine / pharmacology
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Female
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Guanylate Cyclase / antagonists & inhibitors
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Isoquinolines / pharmacology
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Kinetics
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Membrane Potentials / drug effects
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Membrane Potentials / physiology
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Nitroso Compounds / pharmacology*
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Oocytes / drug effects
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Oocytes / physiology*
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Potassium Channels / biosynthesis*
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Protein Kinase C / antagonists & inhibitors
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S-Nitrosothiols*
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Staurosporine
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Xenopus laevis
Substances
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Alkaloids
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Aminoquinolines
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Isoquinolines
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Nitroso Compounds
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Potassium Channels
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S-Nitrosothiols
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N-(2-(methylamino)ethyl)-5-isoquinolinesulfonamide
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6-anilino-5,8-quinolinedione
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S-nitrosocysteine
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Cyclic GMP-Dependent Protein Kinases
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Protein Kinase C
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Guanylate Cyclase
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Cyclic GMP
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Staurosporine
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Cysteine