THE INTERACTION OF K+ WITH GASTRIC PARIETAL CELLS AND GASTRIC ATPASE

The gastric H+ secretion in isolated cell requires K+ and is ATP dependent. There is also evidence in the cell system for Na+ inhibition of H+ secretion. The isolated gastric ATPase also shows K+ activation and inhibition by K+ or Na+ located on the ATP binding side of the enzyme, which corresponds...

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Bibliographic Details
Published in:Annals of the New York Academy of Sciences 1980-12, Vol.358 (1), p.118-137
Main Authors: Sachs, G., Berglindh, T., Rabon, E., Wallmark, B., Barcellona, M. L., Stewart, H. B., Saccomani, G.
Format: Article
Language:English
Subjects:
Adenosine Triphosphate - pharmacology
Aminopyrine - metabolism
Animals
Binding Sites - drug effects
Biological Transport - drug effects
Cell Membrane - enzymology
Cell Membrane - metabolism
Chemical Phenomena
Chemistry
Gastric Acid - metabolism
Gastric Mucosa - enzymology
Gastric Mucosa - metabolism
Gastric Mucosa - ultrastructure
Hydrogen - metabolism
Potassium - metabolism
Potassium - pharmacology
Quinolines - pharmacology
Rabbits
Sodium-Potassium-Exchanging ATPase - antagonists & inhibitors
Sodium-Potassium-Exchanging ATPase - metabolism
Swine
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Summary:The gastric H+ secretion in isolated cell requires K+ and is ATP dependent. There is also evidence in the cell system for Na+ inhibition of H+ secretion. The isolated gastric ATPase also shows K+ activation and inhibition by K+ or Na+ located on the ATP binding side of the enzyme, which corresponds to the cytoplasmic face of the enzyme. Gastric vesicles are activated in terms of transport activity by internal K+, and this site, inhibited by reagents that modify carboxyl groups, is required for enzyme turnover and transport.
ISSN:0077-8923
1749-6632
DOI:10.1111/j.1749-6632.1980.tb15391.x