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Am J Physiol Lung Cell Mol Physiol (June 25, 2004). doi:10.1152/ajplung.00385.2003
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Submitted on November 12, 2003
Accepted on June 3, 2004

Pseudomonas aeruginosa Stimulates Phosphorylation of the Epithelial Membrane Glycoprotein Muc1 and Activates MAP Kinase

Erik P. Lillehoj1, Hakryul Kim1, Ellen Y. Chun1, and Kwang Chul Kim2*

1 Department of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, MD, USA
2 Department of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, MD, USA; Division of Pulmonary and Critical Care Medicine, University of Maryland School of Medicine, Baltimore, MD, USA

* To whom correspondence should be addressed. E-mail: kkim{at}umaryland.edu.

We reported previously that Muc1 on the surface of epithelial cells was a receptor for Pseudomonas aeruginosa (Lillehoj EP et al., Am J Physiol (Lung) 282:L751-L756). Other studies showed that the Muc1 cytoplasmic tail (CT) contains multiple phosphorylation sites, some of which were phosphorylated constitutively and associated with signaling proteins. However, the relationship between extracellular P. aeruginosa binding and intracellular signaling is unknown. To investigate the signaling mechanism of Muc1, this study examined phosphorylation of its CT and activation of the extracellular signal-regulated kinase (ERK) in response to stimulation by P. aeruginosa or purified flagellin. Our results showed: (i) the Muc1 CT was phosphorylated constitutively on serine and tyrosine, (ii) serine phosphorylation was stimulated by bacterial cells or flagellin, and (iii) binding of P. aeruginosa or flagellin to Muc1 induced phosphorylation of ERK. These results are the first to demonstrate Muc1 CT phosphorylation and ERK activation in response to a clinically important airway pathogen.




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