Sodium-permeable channels in the apical membrane of human nasal epithelial cells
We used patch-clamp techniques to study the channels that underlie the Na+ conductance of the apical membrane of human normal nasal epithelial cells. Cells were cultured on permeable supports and studied after confluence. In 172 of 334 (52%) excised membrane patches, we observed 20-pS Na+-permeable channels that do not discriminate between Na+ and K+ (pNa/pK = 1.33). These nonselective cation channels contained subpopulations that differed by dependence of open probability on voltage and bath Ca2+ activity, suggesting two or more channel types with similar electrical properties. In the presence of 10-4 M amiloride in the pipette, the proportion of excised patches with nonselective cation channels decreased to 52 of 139 patches (37%), but the decrease was spread across all subpopulations of nonselective cation channels in excised patches. Thus no distinctive Na+-selective amiloride-sensitive channels were identified in excised patches. In cell-attached patches, Na+-permeable channels were recorded in 56 of 262 patches (21%). Their conductance was 21.4 ± 1.5 pS (n = 25), and most were selective for Na+ over K+ (pNa/pK > 6). In the presence of amiloride (10-4 M) in the pipette, the frequency of λ Na+- permeable channels in cell-attached patches decreased to 8 of 134 patches (6%), revealing a population of Na+-selective channels recorded in cell- attached patches that was inhibited by amiloride. We conclude that, in excised patches, Na+-permeable channels are nonselective for Na+ over K+ and <30% appear to be amiloride sensitive. In contrast, in cell-attached patches, most channels that conduct sodium are 1) selective for Na+ over K+ and 2) amiloride sensitive. Although we have not discovered the explanation for the discrepancy between cell-attached and excised patch data, we speculate that the channels recognized on cell account for the amiloride- sensitive Na+ conductance of the apical membrane, whereas the excision process alters the properties of the Na+-permeable channels and/or activate new channels.
Authors
- Shaojie Ma (ORCID: https://orcid.org/0000-0002-3534-1599)
- Boucher R.C.
- Chinet T.C.
- Fullton J.M.
Institutions
- University of North Carolina at Chapel Hill (US)
Publication Details
- Journal
- UNC Libraries
- Published
- 2025-08-16
- DOI
- https://doi.org/10.17615/hbva-xh12
- Primary Topic
- Ion Transport and Channel Regulation
- Type
- article
- Field-Weighted Citation Impact
- 0.00