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. 2012 Feb 15;23(4):533–542. doi: 10.1091/mbc.E11-01-0039

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© 2012 Ivkovic et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 7: — Myosin IIA heavy chain phosphorylation in GBM. (A) Immunoblot analysis of myosin IIA Ser-1943 phosphorylation in human tissue lysates derived from human epilepsy temporal lobe (red) or GBM (blue). GAPDH was used as a loading control. Relative phosphorylation levels were determined by dividing the myosin IIA pSer-1943/GAPDH ratio by the total myosin IIA/GAPDH ratio. (B) The normalized level of pSer-1943 myosin IIA is significantly increased in GBM samples (0.44 ± 0.15) vs. epileptic temporal lobes (0.20 ± 0.08). Values represent the mean ± SD. (C) EGF-mediated increases in myosin IIA pSer-1943 in C6 (red) and C6-EGFR (blue) glioma cells as a function of time after EGF exposure. Cells were serum-starved and stimulated with 16.5 ng/ml EGF, and the phosphorylation status of the myosin IIA heavy chain was examined by immunoblot with an antibody that recognizes pSer-1943. Phosphorylation is expressed as the change relative to unstimulated cells. Values represent mean ± SD for three (C6) and two (C6-EGFR) independent experiments.