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Am J Physiol Cell Physiol 280: C1599-C1606, 2001;
0363-6143/01 $5.00
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Vol. 280, Issue 6, C1599-C1606, June 2001

Localization of ClC-2 Clminus channels in rabbit gastric mucosa

Ann M. Sherry1, Danuta H. Malinowska1, Randal E. Morris2, Georgianne M. Ciraolo2, and John Cuppoletti1

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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