• Corpus ID: 24481930

Tissue binding sites involved in quinidine-cardiac glycoside interactions.

@article{Kim1981TissueBS,
  title={Tissue binding sites involved in quinidine-cardiac glycoside interactions.},
  author={D H Kim and Tai Akera and Theodore M. Brody},
  journal={The Journal of pharmacology and experimental therapeutics},
  year={1981},
  volume={218 2},
  pages={
          357-62
        }
}
  • D. KimT. AkeraT. Brody
  • Published 1 August 1981
  • Biology, Chemistry, Medicine
  • The Journal of pharmacology and experimental therapeutics
Quinidine has been shown to alter pharmacokinetics of digoxin by displacing the glycoside from mutual binding sites which are stereospecific with respect to quinidine. Characteristics of the binding site involved in quinidine-digoxin interaction were studied further in guinea pigs and rats. In the anesthetized rat quinidine significantly increased digoxin, but not digitoxin or ouabain, concentration in plasma during an i.v. infusion of a radiolabeled glycoside. In the anesthetized guinea pig… 
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The results indicate that PK 10139 could be associated with digoxin without risk of side‐effects, and quinidine induced an increase in digoxin plasma concentrations in rats and dogs.

Energy-dependent transport of digoxin across renal tubular cell monolayers (LLC-PK1).

The results suggest that digoxin undergoes transepithelial secretion by an energy-dependent, carrier-mediated process in renal tubules, a process that seems to be distinct from the tetraethylammonium transport system.

Quinidine decreases the intestinal secretion of digoxin and digitoxin in the guinea-pig

The secretion of digoxin and digitoxin into in situ perfused jejunal and colonic segments of normal or quinidine treated guinea-pigs was studied. Quinidine was administered intravenously by constant

Reduction of digoxin effect during the digoxin‐quinidine interaction

The results indicate that while serum digoxin levels were elevated, the improved cardiac function due to digoxin declined during combined therapy, and this provides an alternate explanation for the changes previously interpreted as “enhanced digitalis effects” during the interaction.

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