Activation of MAPK in fibroblasts by Treponema denticola major outer sheath protein

The major outer sheath protein (Msp) of Treponema denticola induces Ca 2+ 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 r...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2007-04, Vol.356 (1), p.213-218
Main Authors: Jobin, Marie-Claude, Virdee, Inderpreet, McCulloch, Christopher A., Ellen, Richard P.
Format: Article
Language:English
Subjects:
Animals
Bacterial Proteins - pharmacology
Butadienes - pharmacology
Calcium - metabolism
Cell Line
Dose-Response Relationship, Drug
Enzyme Activation - drug effects
Enzyme Inhibitors - pharmacology
ERK 1/2
Fibroblasts
Fibroblasts - cytology
Fibroblasts - drug effects
Fibroblasts - metabolism
Imidazoles - pharmacology
Immunoblotting
Kinase proteome
MAPK phosphorylation
Mitogen-Activated Protein Kinase 1 - metabolism
Mitogen-Activated Protein Kinase 3 - metabolism
Mitogen-Activated Protein Kinases - metabolism
Msp
Nitriles - pharmacology
p38
p38 Mitogen-Activated Protein Kinases - metabolism
Pore-forming toxin
Porins - pharmacology
Protein Kinases - metabolism
Pyridines - pharmacology
Rats
Time Factors
Treponema denticola
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Summary:The major outer sheath protein (Msp) of Treponema denticola induces Ca 2+ 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 Ca 2+. These data indicate that T. denticola Msp may exert transient stress on fibroblasts through activation of MAP kinase pathways.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2007.02.111