Essential Structural Features of TNF-α Lectin-like Domain Derived Peptides for Activation of Amiloride-Sensitive Sodium Current in A549 Cells
In: Journal of Medicinal Chemistry, Jg. 53 (2010-10-27), S. 8021-8029
Online
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Zugriff:
The amiloride-sensitive epithelial sodium channel (ENaC) plays a prominent role in sodium uptake from alveolar fluid, and is the major component in alveolar fluid clearance in normal and diseased lungs. The lectin-like domain of TNF-α has been shown to activate amiloride-sensitive sodium uptake in type II alveolar epithelial cells. Therefore, several synthetic peptides that mimic the lectin-like domain of TNF-α (TIP) were synthesised and their ability to enhance sodium current through ENaC was studied in A549 cells with the patch clamp technique. Our data suggest that a free positively-charged N-terminal amino group on residue 1 and/or a free negatively-charged carboxyl group on residue 17 of the TIP peptide is essential for the ENaC-activating effect. Ventilation strategies apart, no standard treatment exists for pulmonary permeability oedema. Therefore, novel therapies activating sodium uptake from the alveolar fluid via ENaC could improve clinical outcome.
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Essential Structural Features of TNF-α Lectin-like Domain Derived Peptides for Activation of Amiloride-Sensitive Sodium Current in A549 Cells
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Autor/in / Beteiligte Person: | Tzotzos, Susan ; Pietschmann, Helmut ; Lucas, Rudolf ; Lemmens-Gruber, Rosa ; Gowri Shankar Bagavananthem Andavan ; Hazemi, Parastoo ; Fischer, Hendrik ; Fischer, Bernhard |
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Zeitschrift: | Journal of Medicinal Chemistry, Jg. 53 (2010-10-27), S. 8021-8029 |
Veröffentlichung: | American Chemical Society (ACS), 2010 |
Medientyp: | unknown |
ISSN: | 1520-4804 (print) ; 0022-2623 (print) |
DOI: | 10.1021/jm100767p |
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