Journal article
Characterization of NA+/H+ exchanger isoform (NHE1, NH32 and NHE3) expression in prairie dog gallbladder
The Journal of membrane biology, v 182(2)
15 Jul 2001
PMID: 11447504
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Gallbladder Na+ absorption is linked to gallstone formation in prairie dogs. Na+/H+ exchange (NHE) is one of the major Na+ absorptive pathways in gallbladder. In this study, we measured gallbladder Na+/H+ exchange and characterized the NHE isoforms expressed in prairie dogs. Na+/H+ exchange activity was assessed by measuring amiloride-inhibitable transepithelial Na+ flux and apical 22Na+ uptake using dimethylamiloride (DMA). HOE-694 was used to determine NHE2 and NHE3 contributions. Basal JNams was higher than JNasm with JNanet absorption. Mucosal DMA inhibited transepithelial Na+ flux in a dose-dependent fashion, causing JNams equal to JNasm and blocking JNanet absorption at 100 microm. Basal 22Na+ uptake rate was 10.9 +/- 1.0 micromol. cm-2. hr-1 which was inhibited by approximately 43% by mucosal DMA and approximately 30% by mucosal HOE-694 at 100 microm. RT-PCR and Northern blot analysis demonstrated expression of mRNAs encoding NHE1, NHE2 and NHE3 in the gallbladder. Expression of NHE1, NHE2 and NHE3 polypeptides was confirmed using isoform-specific anti-NHE antibodies. These data suggest that Na+/H+ exchange accounts for a substantial fraction of gallbladder apical Na+ entry and most of net Na+ absorption in prairie dogs. The NHE2 and NHE3 isoforms, but not NHE1, are involved in gallbladder apical Na+ uptake and transepithelial Na+ absorption.
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Details
- Title
- Characterization of NA+/H+ exchanger isoform (NHE1, NH32 and NHE3) expression in prairie dog gallbladder
- Creators
- M Z Abedin - Hahnemann University HospitalD I Giurgiu - Hahnemann University HospitalZ R Abedin - Hahnemann University HospitalE A Peck - Hahnemann University HospitalX Su - University of Alabama at BirminghamP R Smith - University of Alabama at Birmingham
- Publication Details
- The Journal of membrane biology, v 182(2)
- Publisher
- Springer Nature
- Resource Type
- Journal article
- Language
- English
- Web of Science ID
- WOS:000169944900004
- Scopus ID
- 2-s2.0-0035879605
- Other Identifier
- 991019318946904721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology
- Cell Biology
- Physiology