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Ouabain-sensitive Na+,K(+)-ATPase activity in toad brain

J F Morris1, F Ismail-Beigi, V P Butler

  • 1Department of Medicine, College of Physicians and Surgeons, Columbia University, New York, NY 10032, USA.

Comparative Biochemistry and Physiology. Part A, Physiology
|December 24, 1997
PubMed
Summary

Toad brains possess a highly ouabain-sensitive sodium-potassium ATPase (Na+,K(+)-ATPase). This enzyme shows significantly greater sensitivity to digitalis compounds compared to other toad tissues, suggesting unique functional roles.

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Area of Science:

  • Biochemistry
  • Pharmacology
  • Comparative Physiology

Background:

  • Toads (genus Bufo) exhibit remarkable resistance to digitalis glycosides.
  • The sodium-potassium ATPase (Na+,K(+)-ATPase) in toad tissues is generally insensitive to digitalis compounds.

Purpose of the Study:

  • To investigate the sensitivity of Na+,K(+)-ATPase in toad brain tissue to digitalis compounds.
  • To determine if multiple Na+,K(+)-ATPase isoforms with varying sensitivities are present in toad brains.

Main Methods:

  • Enzymatic assays of Na+,K(+)-ATPase activity using [3H]ouabain binding in brain microsomal preparations from Bufo marinus and Bufo viridis.
  • Measurement of 86Rb+ uptake in Bufo marinus brain tissue slices.

Main Results:

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  • Toad brain Na+,K(+)-ATPase demonstrated high sensitivity to ouabain, with Ki values significantly lower (0.085–3.7 microM) than in toad bladder (Ki = 5940 microM).
  • Both enzymatic assays and 86Rb+ uptake studies confirmed the presence of a highly ouabain-sensitive Na+,K(+)-ATPase in toad brain.
  • The contribution of the high-sensitivity site differed between enzymatic activity (63%) and ion transport (17%).

Conclusions:

  • A highly ouabain-sensitive Na+,K(+)-ATPase is present and functional in toad brain.
  • This specific enzyme isoform's function might be partially modulated in vivo despite its high sensitivity.