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Embryonic stem (ES) cell-derived myotubes derived from differentiating embryonic stem cells (ESCs) express fetal myosin heavy chain (FMyHC). In order to provide a potential in vivo model for investigating the intracellular mechanism involved in the switch from MyoD to the alternative MyoD2 myogenic repressor, we overexpressed MyoD2 in F9 and ESC-derived myotube cells (ESC-MTCs) to determine the effect of this protein on MyoD activity. We found that an up-regulation of MyoD2 prevented commitment of the myogenic program in both types of cells. Since MyoD2 inhibits the activity of MyoD through sequestering it away from chromatin, we investigated the role of the bcl-2 protein, a known inhibitor of MyoD transcriptional activity. Our results indicate that the transcriptional activity of MyoD is regulated by bcl-2 and ecotropic viral integration site 1 (Evi-1). Both proteins interacted with MyoD in an immunoprecipitation assay. Furthermore, we found that bcl-2 silencing decreased MyoD protein activity, while Evi-1 overexpression increased MyoD activity in vitro in a MyoD-dependent manner. Since MyoD activity is not regulated by any known post-translational modifications in these cells, this suggest that MyoD activity is regulated by its direct interaction with bcl-2 and Evi-1. These data indicate that bcl-2 and Evi-1 act as potent modulators of MyoD activity, as they negatively regulate the activity of MyoD in myotubes, through protein-protein interaction.[Early postoperative neurological deterioration after operations on the brain stem].
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