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channels in
rabbit gastric mucosa
Departments of 1 Molecular and Cellular Physiology and 2 Cell Biology, Neurobiology, and Anatomy, University of Cincinnati College of Medicine, Cincinnati, Ohio 43267-0576
HCl secretion across the parietal cell apical secretory
membrane involves the H+-K+-ATPase, the ClC-2
Cl
channel, and a K+ channel. In the present
study, the cellular and subcellular distribution of ClC-2 mRNA and
protein was determined in the rabbit gastric mucosa and in isolated
gastric glands. ClC-2 mRNA was localized to parietal cells by in situ
hybridization and by direct in situ RT-PCR. By immunoperoxidase
microscopy, ClC-2 protein was concentrated in parietal cells.
Immunofluorescent confocal microscopy suggested that the ClC-2 was
localized to the secretory canalicular membrane of stimulated parietal
cells and to intracellular structures of resting parietal cells.
Immunogold electron microscopy confirmed that ClC-2 is in the secretory
canalicular membrane of stimulated cells and in tubulovesicles of
resting parietal cells. These findings, together with previous
functional characterization of the native and recombinant channel,
strongly indicate that ClC-2 is the Cl
channel, which
together with the H+-K+-ATPase and a
K+ channel, results in HCl secretion across the parietal
cell secretory membrane.
gastric chloride channel; hydrochloric acid secretion; secretory canalicular membrane; tubulovesicles
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