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 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.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000632:Aminopyrine / Q000378:metabolism; D000818:Animals; D001665:Binding Sites / Q000187:drug effects; D001692:Biological Transport / Q000187:drug effects; D002462:Cell Membrane / Q000201:enzymology / Q000378:metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D005744:Gastric Acid / Q000378:metabolism*; D005753:Gastric Mucosa / Q000201:enzymology* / Q000378:metabolism / Q000648:ultrastructure; D006859:Hydrogen / Q000378:metabolism; D011188:Potassium / Q000378:metabolism* / Q000494:pharmacology; D011804:Quinolines / Q000494:pharmacology; D011817:Rabbits; D000254:Sodium-Potassium-Exchanging ATPase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D013552:Swine
D011804:Quinolines; D000632:Aminopyrine; C000470:EEDQ; D006859:Hydrogen; D000255:Adenosine Triphosphate; D000254:Sodium-Potassium-Exchanging ATPase; D011188:Potassium