PROTEASE-ACTIVATED RECEPTOR (PAR)1 ALTERS BIOELECTRIC PROPERTIES OF DISTAL LUNG EPITHELIA WITHOUT COMPROMISING BARRIER FUNCTION EXPERIMENTAL LUNG RESEARCH Moraes, T. J., Rafii, B., Niessen, F., Suzuki, T., Martin, R., Vachon, E., Vogel, W., Ruf, W., O'Brodovich, H., Downey, G. P. 2009; 35 (2): 136-154

Abstract

Proteinases contribute to the pathogenesis of various lung diseases, partly through activating cell surface receptors by limited proteolytic cleavage. The authors provide evidence that in primary cultures of distal lung epithelia, basolateral protease-activated receptor 1 activation rapidly reduces transepithelial resistance but does not alter paracellular permeability to small uncharged solutes. Changes in transepithelial resistance were partially blocked by ion transport inhibitors and were completely blocked by placing cells in low chloride buffer. In vivo studies did not reveal enhanced lung permeability in response to pulmonary or intravenous administration of protease-activated receptor 1 activators. This information is relevant as strategies to inhibit protease-activated receptor 1 signaling are considered in order to preserve lung epithelial barrier function.

View details for DOI 10.1080/01902140802490723

View details for Web of Science ID 000263870100004

View details for PubMedID 19263282