Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1938651 | Biochemical and Biophysical Research Communications | 2007 | 6 Pages |
Abstract
The major outer sheath protein (Msp) of Treponema denticola induces Ca2+ entry and actin reorganization in cultured fibroblasts, but the pathways by which Msp mediates these responses are not yet defined. We considered that Msp may activate protein kinases as a stress response that precedes actin remodelling. Phospho-kinase screens showed that Msp induced phosphorylation of multiple kinases in pathways that respond to extracellular agonists and regulate actin assembly. 34 kinases were significantly activated, including p38 and ERK 1/2. Accordingly, the expression and phosphorylation of p38 and ERK 1/2 in whole cell lysates were measured by immunoblotting and densitometry. Both kinases responded in a dose- and time-dependent manner to Msp exposure, were inhibited by SB202190 and U1026, respectively, and were unaffected by extracellular Ca2+. These data indicate that T. denticola Msp may exert transient stress on fibroblasts through activation of MAP kinase pathways.
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Authors
Marie-Claude Jobin, Inderpreet Virdee, Christopher A. McCulloch, Richard P. Ellen,