Mechanical force activates eIF-2alpha phospho-kinases in fibroblast.
Mechanical forces can induce differentiation of fibroblasts into myofibroblasts, a process which requires activation of the MAP kinase p38. Currently, the identification of other phospho-kinases involved in myofibroblast differentiation has not been explored. We applied static tensile forces to rat cardiac fibroblasts via collagen-coated magnetite beads and examined activation of protein phospho-kinases by the Kinexus phospho-antibody screening system. Of 75 candidate protein kinases screened, 39 were detected and, of these, 31 phospho-kinases were analyzed. Following force application, 12 out of 31 phospho-kinases exhibited increases of phosphorylation including PKR (>4-fold), MKK3 (3-fold), MKK6 ( approximately 2-fold), and p38 ( approximately 2-fold). In several types of mechanically sensitive, contractile fibroblasts including rat cardiac, human gingival, and Rat-2 fibroblasts, tensile forces increased eIF-2alpha phosphorylation, a downstream effector of PKR. We conclude that phospho-antibody screening is an efficient method for discovery of novel mechanical force- induced phospho-kinases and force can activate eIF-2alpha phospho-kinases in fibroblasts.[1]References
- Mechanical force activates eIF-2alpha phospho-kinases in fibroblast. Wang, J., Laschinger, C., Zhao, X.H., Mak, B., Seth, A., McCulloch, C.A. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
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