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Related Experiment Videos

The gastric H+,K(+)-ATPase.

B Wallmark1, P Lorentzon, G Sachs

  • 1Department of Biology, Gastrointestinal Research, Mölndal, Sweden.

Journal of Internal Medicine. Supplement
|January 1, 1990
PubMed
Summary
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The gastric H+,K(+)-ATPase proton pump activity is stimulated by potassium ions. This stimulation results from increased hydrolysis of the phosphoenzyme intermediate, with inhibition observed only at high potassium concentrations in permeable vesicles.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Physiology

Background:

  • Mammalian extramitochondrial pumps include vacuolar H(+)-ATPases and E1E2-type ATPases.
  • The gastric H+,K(+)-ATPase is the proton pump in gastric mucosa, localized to parietal cells.
  • This enzyme exchanges H+ and K+ to create a highly acidic environment in the secretory canaliculus.

Purpose of the Study:

  • To investigate the role of extracytosolic potassium ions in activating the gastric H+,K(+)-ATPase.
  • To elucidate the mechanism by which potassium ions stimulate the H+,K(+)-ATPase activity.

Main Methods:

  • Kinetic studies using isolated ion-tight and ion-permeable gastric vesicles.
  • Analysis of H+,K(+)-ATPase activity under varying potassium concentrations and vesicle permeability.

Related Experiment Videos

  • Measurement of phosphorylenzyme intermediate breakdown.

    • Main Results:

    • Intravesicular potassium (K+) stimulates H+,K(+)-ATPase activity.
    • Potassium accelerates the breakdown of the phosphorylenzyme intermediate, indicating increased hydrolysis.
    • Inhibition of ATPase activity was observed at high K+ concentrations in permeable vesicles, but not in ion-tight vesicles.

    Conclusions:

    • Potassium ion stimulation of gastric H+,K(+)-ATPase activity is primarily due to an increased rate of phosphoenzyme hydrolysis.
    • Vesicle permeability and potassium concentration influence the observed ATPase activity and potential-dependent inhibition.