Show simple item record

dc.contributor.authorSchwagerus, Elena
dc.contributor.authorSladek, Svenja
dc.contributor.authorBuckley, Stephen T
dc.contributor.authorArmas-Capote, Natalia
dc.contributor.authorAlvarez de la Rosa, Diego
dc.contributor.authorHarvey, Brian J
dc.contributor.authorFischer, Horst
dc.contributor.authorIllek, Beate
dc.contributor.authorHuwer, Hanno
dc.contributor.authorSchneider-Daum, Nicole
dc.contributor.authorLehr, Claus-Michael
dc.contributor.authorEhrhardt, Carsten
dc.date.accessioned2016-01-05T09:05:20Zen
dc.date.available2016-01-05T09:05:20Zen
dc.date.issued2015-11en
dc.identifier.citationExpression and function of the epithelial sodium channel δ-subunit in human respiratory epithelial cells in vitro. 2015, 467 (11):2257-73 Pflugers Arch.en
dc.identifier.issn1432-2013en
dc.identifier.pmid25677639en
dc.identifier.doi10.1007/s00424-015-1693-5en
dc.identifier.urihttp://hdl.handle.net/10033/592820en
dc.description.abstractUsing human airway epithelial cell lines (i.e. NCI-H441 and Calu-3) as well as human alveolar epithelial type I-like (ATI) cells in primary culture, we studied the contribution of the epithelial sodium channel δ-subunit (δ-ENaC) to transepithelial sodium transport in human lung in vitro. Endogenous δ-ENaC protein was present in all three cell types tested; however, protein abundance was low, and no expression was detected in the apical cell membrane of these cells. Similarly, known modulators of δ-ENaC activity, such as capsazepine and icilin (activators) and Evans blue (inhibitor), did not show effects on short-circuit current (I SC), suggesting that δ-ENaC is not involved in the modulation of transcellular sodium absorption in NCI-H441 cell monolayers. Over-expression of δ-ENaC in NCI-H441 cells resulted in detectable protein expression in the apical cell membrane, as well as capsazepine and icilin-stimulated increases in I SC that were effectively blocked by Evans blue and that were consistent with δ-ENaC activation and inhibition, respectively. Consequently, these observations suggest that δ-ENaC expression is low in NCI-H441, Calu-3, and ATI cells and does not contribute to transepithelial sodium absorption.
dc.language.isoenen
dc.titleExpression and function of the epithelial sodium channel δ-subunit in human respiratory epithelial cells in vitro.en
dc.typeArticleen
dc.contributor.departmentHelmholtz Institute for Pharmaceutical Research Saarland, 66123 Saarbrücken, Germanyen
dc.identifier.journalPflügers Archiv : European journal of physiologyen
refterms.dateFOA2016-11-15T00:00:00Z
html.description.abstractUsing human airway epithelial cell lines (i.e. NCI-H441 and Calu-3) as well as human alveolar epithelial type I-like (ATI) cells in primary culture, we studied the contribution of the epithelial sodium channel δ-subunit (δ-ENaC) to transepithelial sodium transport in human lung in vitro. Endogenous δ-ENaC protein was present in all three cell types tested; however, protein abundance was low, and no expression was detected in the apical cell membrane of these cells. Similarly, known modulators of δ-ENaC activity, such as capsazepine and icilin (activators) and Evans blue (inhibitor), did not show effects on short-circuit current (I SC), suggesting that δ-ENaC is not involved in the modulation of transcellular sodium absorption in NCI-H441 cell monolayers. Over-expression of δ-ENaC in NCI-H441 cells resulted in detectable protein expression in the apical cell membrane, as well as capsazepine and icilin-stimulated increases in I SC that were effectively blocked by Evans blue and that were consistent with δ-ENaC activation and inhibition, respectively. Consequently, these observations suggest that δ-ENaC expression is low in NCI-H441, Calu-3, and ATI cells and does not contribute to transepithelial sodium absorption.


Files in this item

Thumbnail
Name:
Schwagerus et al.pdf
Size:
2.174Mb
Format:
PDF
Description:
original manuscript

This item appears in the following Collection(s)

Show simple item record