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Published ahead of print on May 12, 2008, doi:10.1165/rcmb.2007-0410OC

Am. J. Respir. Cell Mol. Biol., Volume 39, Number 5, November 2008, 530-535

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Submitted on November 13, 2007
Revised on May 8, 2008

Chitinase Activates Protease-activated Receptor-2 in Human Airway Epithelial Cells

Jeong Hee Hong1, Jung Yeon Hong2, Boryung Park1, Syng-Ill Lee1, Jeong Taeg Seo1, Kyu-Earn Kim2, Myung Hyun Sohn2, and Dong Min Shin1*

1 Department of Oral Biology, Brain Korea 21 Project, Yonsei University College of Dentistry, Center for Natural Defense System, Seoul, 120-752, Korea, Republic of, 2 Department of Pediatrics, Brain Korea 21 Project, Yonsei University College of Medicine, Institute of Allergy, Seoul, 120-752, Korea, Republic of

* To whom correspondence should be addressed. E-mail: dmshin{at}yuhs.ac.

Mammalian chitinase released by airway epithelia is thought to be an important mediator of disease manifestation in an experimental model of asthma. However, the intracellular signaling mechanisms engaged by exogenous chitinase in human airway epithelial cells are unknown. Here, we investigated the direct effects of exogenous chitinase from Streptomyces griseus on Ca2+ signaling in human airway epithelial cells. Spectrofluorometry was used to measure intracellular Ca2+ concentration ([Ca2+]i) in fura-2-AM-loaded cells. S. griseus chitinase induced dose-dependent [Ca2+]i increases in normal human bronchial epithelial cells and promoted [Ca2+]i oscillations in H292 cells. Chitinase-induced [Ca2+]i oscillations were independent of extracellular Ca2+, suggesting that the observed [Ca2+]i increases were due to Ca2+ release from intracellular stores. Accordingly, after depleting endoplasmic reticulum (ER) Ca2+ with the ER Ca2+ ATPase inhibitor, thapsigargin, chitinase-mediated [Ca2+]i increases were abolished. Treatment with the phospholipase C (PLC) inhibitor U73122 or the 1, 4, 5-trisinositolphosphate (IP3) receptor inhibitor 2-APB attenuated chitinase-induced [Ca2+]i increases. Desensitization of protease-activated receptor-2 (PAR-2) by repetitive agonist stimulation or siRNA-mediated PAR-2 knock-down revealed that chitinase-mediated [Ca2+]i increases were exclusively mediated by PAR-2 activation. Finally, chitinase was found to cleave a model peptide representing the cleavage site of PAR-2 and enhanced IL-8 production. These results indicate that exogenous chitinase is a potent proteolytic activator of PAR-2 that can directly induce PLC/IP3-dependent Ca2+ signaling in human airway epithelial cells.




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