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Papers In Press, published online ahead of print November 12, 2001
Microbiology-Immunology and Pediatrics, Dalhousie University, Halifax, Nova Scotia B3J 3G9
Corresponding Author: tlin{at}is.dal.ca
Pulmonary infection with P. aeruginosa is characterized by massive airway inflammation, which comprises significant cytokine production. Although mast cells are abundant in the lung and are potent sources of various cytokines, a role of mast cells in P. aeruginosa infection remains undefined and P. aeruginosa-induced signaling mechanisms in mast cells have not been studied previously. Here we demonstrate that human cord blood-derived mast cells, mouse bone marrow-derived mast cells (BMMC) and the mouse mast cell line MC/9 produce significant amounts of interleukin 6 (IL-6) in response to P. aeruginosa. This response was accompanied by a stimulation of PKC
J. Biol. Chem, 10.1074/jbc.M108623200
Submitted on September 6, 2001
Revised on November 5, 2001
Accepted on November 9, 2001
Protein phosphatase 2A and protein kinase C
are physically associated and are involved in Pseudomonas aeruginosa-induced interleukin 6 production by mast cells
phosphorylation and PKC activity, and was significantly blocked by the PKC inhibitors Ro 31-8220 and PKC pseudosubstrate. Interestingly, mast cells treated with P. aeruginosa had reduced protein levels of phosphatase 2A catalytic unit (PP2Ac), which prompted us to determine whether a direct association between PKC and PP2A occurs in mast cells. In BMMC and MC/9 cells, as well as in the human mast cell line HMC-1, PP2A co-immunoprecipitated with PKC either using PKC- or PP2Ac-specific antibodies, suggesting that PKC and PP2Ac are physically associated in mast cells. The PP2A inhibitor okadaic acid induced P. aeruginosa-like responses in mast cells including increased PKC phosphorylation, stimulated PKC activity, and augmented IL-6 production; the latter being blocked by the PKC inhibitor Ro 31-8220. Finally, okadaic acid potentiated the P. aeruginosa-induced IL-6 production. Collectively, these data provide, to our knowledge, the first evidence of both a direct physical association of PP2A and PKC in mammalian cells, and their co-involvement in regulating mast cell activation in response to P. aeruginosa.
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