Document Detail


KCNQ1 is the luminal K+ recycling channel during stimulation of gastric acid secretion.
MedLine Citation:
PMID:  19491250     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Parietal cell (PC) proton secretion via H(+)/K(+)-ATPase requires apical K(+) recycling. A variety of K(+) channels and transporters are expressed in the PC and the molecular nature of the apical K(+) recycling channel is under debate. This study was undertaken to delineate the exact function of KCNQ1 channels in gastric acid secretion. Acid secretory rates and electrophysiological parameters were determined in gastric mucosae of 7- to 8-day-old KCNQ1(+/+), (+/-) and (-/-) mice. Parietal cell ultrastructure, abundance and gene expression levels were quantified. Glandular structure and PC abundance, and housekeeping gene expression did not differ between the KCNQ1(-/-) and (+/+) mucosae. Microvillar secretory membranes were intact, but basal acid secretion was absent and forskolin-stimulated acid output reduced by approximately 90% in KCNQ1(-/-) gastric mucosa. Application of a high K(+) concentration to the luminal membrane restored normal acid secretory rates in the KCNQ1(-/-) mucosa. The study demonstrates that the KCNQ1 channel provides K(+) to the extracellular K(+) binding site of the H(+)/K(+)-ATPase during acid secretion, and no other gastric K(+) channel can substitute for this function.
Authors:
Penghong Song; Stephanie Groos; Brigitte Riederer; Zhe Feng; Anja Krabbenhöft; Adam Smolka; Ursula Seidler
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-06-02
Journal Detail:
Title:  The Journal of physiology     Volume:  587     ISSN:  1469-7793     ISO Abbreviation:  J. Physiol. (Lond.)     Publication Date:  2009 Aug 
Date Detail:
Created Date:  2009-08-03     Completed Date:  2009-11-17     Revised Date:  2013-06-02    
Medline Journal Info:
Nlm Unique ID:  0266262     Medline TA:  J Physiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  3955-65     Citation Subset:  IM    
Affiliation:
Department of Gastroenterology, Hepatology and Endocrinology, Hannover Medical School, Carl-Neuberg-Strasse 1, D-30625, Germany.
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MeSH Terms
Descriptor/Qualifier:
Animals
Anion Transport Proteins / metabolism
Antiporters / metabolism
Body Weight / physiology
Forskolin / pharmacology
Gastric Acid / secretion*
Gastric Mucosa / drug effects,  metabolism*,  pathology
H(+)-K(+)-Exchanging ATPase / metabolism
KCNQ1 Potassium Channel / genetics,  metabolism*
Mice
Mice, Inbred BALB C
Mice, Inbred C57BL
Mice, Knockout
Potassium / metabolism
Potassium Channels, Inwardly Rectifying / metabolism
Chemical
Reg. No./Substance:
0/AE2 anion exchanger; 0/Anion Transport Proteins; 0/Antiporters; 0/KCNQ1 Potassium Channel; 0/Kcnq1 protein, mouse; 0/Kir5.1 channel; 0/Potassium Channels, Inwardly Rectifying; 66428-89-5/Forskolin; 7440-09-7/Potassium; EC 3.6.1.10/H(+)-K(+)-Exchanging ATPase
Comments/Corrections
Comment In:
J Physiol. 2009 Sep 1;587(Pt 17):4149-50   [PMID:  19720854 ]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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