Document Detail


Kir4.1 channel expression is essential for parietal cell control of acid secretion.
MedLine Citation:
PMID:  21367857     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Kir4.1 channels were found to colocalize with the H(+)/K(+)-ATPase throughout the parietal cell (PC) acid secretory cycle. This study was undertaken to explore their functional role. Acid secretory rates, electrophysiological parameters, PC ultrastructure, and gene and protein expression were determined in gastric mucosae of 7-8-day-old Kir4.1-deficient mice and WT littermates. Kir4.1(-/-) mucosa secreted significantly more acid and initiated secretion significantly faster than WT mucosa. No change in PC number but a relative up-regulation of H(+)/K(+)-ATPase gene and protein expression (but not of other PC ion transporters) was observed. Electron microscopy revealed fully fused canalicular membranes and a lack of tubulovesicles in resting state Kir4.1(-/-) PCs, suggesting that Kir4.1 ablation may also interfere with tubulovesicle endocytosis. The role of this inward rectifier in the PC apical membrane may therefore be to balance between K(+) loss via KCNQ1/KCNE2 and K(+) reabsorption by the slow turnover of the H(+)/K(+)-ATPase, with consequences for K(+) reabsorption, inhibition of acid secretion, and membrane recycling. Our results demonstrate that Kir4.1 channels are involved in the control of acid secretion and suggest that they may also affect secretory membrane recycling.
Authors:
Penghong Song; Stephanie Groos; Brigitte Riederer; Zhe Feng; Anja Krabbenhöft; Michael P Manns; Adam Smolka; Susan J Hagen; Clemens Neusch; Ursula Seidler
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2011-03-02
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  286     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2011 Apr 
Date Detail:
Created Date:  2011-04-18     Completed Date:  2011-06-28     Revised Date:  2012-04-23    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  14120-8     Citation Subset:  IM    
Affiliation:
Department of Gastroenterology, Hepatology, and Endocrinology, Hannover Medical School, D-30625 Hannover, Germany.
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MeSH Terms
Descriptor/Qualifier:
Animals
Biological Transport
Electrophysiology / methods
Endocytosis
Gastric Acid / metabolism*
Gastric Mucosa / metabolism
Gene Expression Regulation*
H(+)-K(+)-Exchanging ATPase / chemistry
Mice
Mice, Knockout
Microscopy, Electron, Transmission / methods
Microscopy, Fluorescence / methods
Parietal Cells, Gastric / cytology*
Potassium / chemistry
Potassium Channels, Inwardly Rectifying / biosynthesis,  physiology*
Chemical
Reg. No./Substance:
0/Potassium Channels, Inwardly Rectifying; 0/potassium inwardly-rectifying channel, subfamily J, member 10; 7440-09-7/Potassium; EC 3.6.1.10/H(+)-K(+)-Exchanging ATPase

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