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Am J Physiol Lung Cell Mol Physiol (January 12, 2002). doi:10.1152/ajplung.00392.2001
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Articles in PresS, published online ahead of print January 11, 2002
Am J Physiol Lung Cell Mol Physiol, 10.1152/ajplung.00392.2001
Submitted on October 5, 2001
Accepted on January 7, 2002

Human bronchial epithelial cells express protease-activated receptor-2 with different sensitivity to thermolysin

Joachim J Ubl1, Zoryana V Grishina2, Tania K Sukhomlin3, Fariba Sedehizade1, Tobias Welte4, and Georg Reiser1*

1 Institut fur Neurobiochemie, Medizinische Fakultat der Otto-von-Guericke-Universitat, Magdeburg, Germany
2 Institut fur Neurobiochemie, Medizinische Fakultat der Otto-von-Guericke-Universitat, Magdeburg, Germany; A.N.Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow, Russian Federation
3 Institut fur Neurobiochemie, Medizinische Fakultat der Otto-von-Guericke-Universitat, Magdeburg, Germany; Research Centre of Molecular Diagnostics and Therapy, Moscow, Russian Federation
4 Abt. fur Pneumologie, Medizinische Fakultat der Otto-von-Guericke-Universitat, Magdeburg, Germany

* To whom correspondence should be addressed. E-mail: georg.reiser{at}medizin.uni-magdeburg.de.

Protease-activated receptor-2 (PAR-2) plays a role in inflammatory reactions in airway physiology. Proteases cleaving the extracellular N-terminus of receptors activate or inactivate PAR thus possessing a therapeutic potential. Using RT-PCR and immunohistochemistry we show PAR-2 in human airway epithelial cell lines HBE and A549. Functional expression of PAR-2 was confirmed by Ca2+ imaging studies using the receptor agonist protease trypsin. The effect was abolished by soybean trypsin inhibitor, and mimicked by the specific PAR-2 peptide agonist, SLIGKV. Amplitude and duration of PAR-2-elicited Ca2+ response in HBE and A549 cells depend on concentration and time of agonist superfusion. The response is partially Pertussis toxin (PTX)-insensitive, abolished by the PLC inhibitor U 73122, diminished by the InsP3 receptor antagonist 2-APB. Cathepsin G altered neither the resting Ca2+ level nor PAR-2-elicited Ca2+ response. Thermolysin, a prototypic bacterial metalloprotease, induced a dose-dependent Ca2+ response in HBE, but not A549 cells. In both cell lines thermolysin abolished the response to a subsequent trypsin challenge, but not to SLIGKV. Thus, different epithelial cell types express different PAR-2 with identical responses to physiological stimuli (trypsin, SLIGKV) but different sensitivity to modifying proteases, such as thermolysin.




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