Matches in Nanopublications for { ?s ?p "Because our results indicated that the combination of MEF2C-VP16 and E2F1-pRb(SP) could support the activity of MCK-reporter constructs as efficiently as could pRb, we further evaluated the ability of these two proteins to synergistically activate the expression of endogenous muscle genes. In pRb-deficient fibroblasts, MyoD transfection by itself induced low amounts of MHC expression and little or no detectable MCK (Figure 5a-c). In contrast, cells transfected with both MyoD and pRb produced high levels of MHC and MCK (Figure 5d-f). Cotransfection of MyoD with either MEF2C-VP16 or E2F1-pRb(SP) alone led to a relatively small increase in the intensity of MHC staining and low amounts of endogenous MCK expression (Figure 5g-l). However, the combination of MyoD, MEF2C-VP16, and E2F1-pRb(SP) produced cells that expressed very high levels of both MHC and MCK (Figure 5m-o), again mimicking the phenotype of cells transfected with MyoD and pRb. In summary, these results indicate that the ability of pRb to promote muscle differentiation can be fully substituted by the combination of E2F1-pRb(SP) and MEF2C-VP16, suggesting that the requirement for pRb to promote expression of late muscle-differentiation markers reflects the ability of this molecule both to arrest cells in G0 and to potentiate MyoD-mediated activation of the MEF2 TAD." ?g. }
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- _4 value "Because our results indicated that the combination of MEF2C-VP16 and E2F1-pRb(SP) could support the activity of MCK-reporter constructs as efficiently as could pRb, we further evaluated the ability of these two proteins to synergistically activate the expression of endogenous muscle genes. In pRb-deficient fibroblasts, MyoD transfection by itself induced low amounts of MHC expression and little or no detectable MCK (Figure 5a-c). In contrast, cells transfected with both MyoD and pRb produced high levels of MHC and MCK (Figure 5d-f). Cotransfection of MyoD with either MEF2C-VP16 or E2F1-pRb(SP) alone led to a relatively small increase in the intensity of MHC staining and low amounts of endogenous MCK expression (Figure 5g-l). However, the combination of MyoD, MEF2C-VP16, and E2F1-pRb(SP) produced cells that expressed very high levels of both MHC and MCK (Figure 5m-o), again mimicking the phenotype of cells transfected with MyoD and pRb. In summary, these results indicate that the ability of pRb to promote muscle differentiation can be fully substituted by the combination of E2F1-pRb(SP) and MEF2C-VP16, suggesting that the requirement for pRb to promote expression of late muscle-differentiation markers reflects the ability of this molecule both to arrest cells in G0 and to potentiate MyoD-mediated activation of the MEF2 TAD." provenance.
- _4 value "Because our results indicated that the combination of MEF2C-VP16 and E2F1-pRb(SP) could support the activity of MCK-reporter constructs as efficiently as could pRb, we further evaluated the ability of these two proteins to synergistically activate the expression of endogenous muscle genes. In pRb-deficient fibroblasts, MyoD transfection by itself induced low amounts of MHC expression and little or no detectable MCK (Figure 5a-c). In contrast, cells transfected with both MyoD and pRb produced high levels of MHC and MCK (Figure 5d-f). Cotransfection of MyoD with either MEF2C-VP16 or E2F1-pRb(SP) alone led to a relatively small increase in the intensity of MHC staining and low amounts of endogenous MCK expression (Figure 5g-l). However, the combination of MyoD, MEF2C-VP16, and E2F1-pRb(SP) produced cells that expressed very high levels of both MHC and MCK (Figure 5m-o), again mimicking the phenotype of cells transfected with MyoD and pRb. In summary, these results indicate that the ability of pRb to promote muscle differentiation can be fully substituted by the combination of E2F1-pRb(SP) and MEF2C-VP16, suggesting that the requirement for pRb to promote expression of late muscle-differentiation markers reflects the ability of this molecule both to arrest cells in G0 and to potentiate MyoD-mediated activation of the MEF2 TAD." provenance.