Abstract
Gastric acid secretion is mediated by a K+ dependent proton pump, which requires a K+ channel to continuously supply K+ at the luminal side of the apical membrane. However, the identity of potassium channel coupled with gastric acid secretion is still elusive. We aimed to investigate the role of potassium channel KCNJ15 in acid secretion. A recombinant adenovirus expressing CFP tagged KCNJ15 was used to infect parietal cells and live cell imaging was conducted to record the pathway of KCNJ15‐CFP in stimulated acid secretion. KCNJ15 molecules are scattered all over in resting cells, but exhibited apical localization in histamine‐stimulated live cells. Further, the effect of knocking down KCNJ15 on acid secretion was analyzed. KCNJ15 shRNA was delivered into rabbit primary parietal cells using a recombinant adenoviral vector. The knockdown of KCNJ15 was confirmed by western blotting. Histamine stimulated acid production was monitored by [14C] aminopyrine uptake assays. Knocking down KCNJ15 abolished histamine stimulated acid secretion, indicating that KCNJ15 is critical for stimulated acid secretion. In addition to rabbit, we also detected KCNJ15 proteins in human and mouse gastric mucosa, suggesting KCNJ15 could play a similar role in acid secretion in other species. These results further support that KCNJ15 plays a critical role in gastric acid secretion.
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