Protease-activated receptor-2-mediated inhibition of ion transport in human bronchial epithelial cells

1  Novartis Horsham Research Centre, Horsham, West Sussex RH12 5AB, United Kingdom; and 2  Department of Cell Biology and Physiology, University of Pittsburgh, Pittsburgh, Pennsylvania 15261 A cytoprotective role for protease-activated receptor-2 (PAR2) has been suggested in a number of systems incl...

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Published in:American Journal of Physiology: Cell Physiology 2001-06, Vol.280 (6), p.C1455-C1464
Main Authors: Danahay, Henry, Withey, Louise, Poll, Christopher T, van de Graaf, Stan F. J, Bridges, Robert J
Format: Article
Language:English
Subjects:
Biological Transport - drug effects
Biological Transport - physiology
Bronchi - cytology
Calcium - metabolism
Cells, Cultured
Dose-Response Relationship, Drug
Epithelial Cells - cytology
Epithelial Cells - metabolism
Gene Expression - physiology
Hemostatics - pharmacology
Humans
Oligopeptides - pharmacology
Receptor, PAR-2
Receptors, Thrombin - genetics
Receptors, Thrombin - metabolism
RNA, Messenger - analysis
Sodium - metabolism
Sodium Channels - metabolism
Thrombin - pharmacology
Trypsin - pharmacology
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Summary:1  Novartis Horsham Research Centre, Horsham, West Sussex RH12 5AB, United Kingdom; and 2  Department of Cell Biology and Physiology, University of Pittsburgh, Pittsburgh, Pennsylvania 15261 A cytoprotective role for protease-activated receptor-2 (PAR2) has been suggested in a number of systems including the airway, and to this end, we have studied the role that PARs play in the regulation of airway ion transport, using cultures of normal human bronchial epithelial cells. PAR2 activators, added to the basolateral membrane, caused a transient, Ca 2+ -dependent increase in short-circuit current ( I sc ), followed by a sustained inhibition of amiloride-sensitive I sc . These phases corresponded with a transient increase in intracellular Ca 2+ concentration and then a transient increase, followed by decrease, in basolateral K + permeability. After PAR2 activation and the addition of amiloride, the forskolin-stimulated increase in I sc was also attenuated. By contrast, PAR2 activators added to the apical surface of the epithelia or PAR1 activators added to both the apical and basolateral surfaces were without effect. PAR2 may, therefore, play a role in the airway, regulating Na + absorption and anion secretion, processes that are central to the control of airway surface liquid volume and composition. trypsin; epithelial sodium channel; human airway
ISSN:0363-6143
1522-1563
DOI:10.1152/ajpcell.2001.280.6.c1455