Fig. 3. PP2A activity is significantly inhibited by in vivo OA and fostriecin treatment. / (A) Phosphatase activity in lysates of cells treated with 0.5 μM OA (OA) using either 32P-labeled phosphorylase a (upper panel) or 32P-labeled histone H1 (lower panel) as substrate. (B) Phosphatase activity in lysates of cells treated with 5 μM fostriecin (fostriecin) using 32P-labeled phosphorylase a as substrate. Cells exposed to vehicle alone (untreated) were used as controls. Assays were performed with further addition of vehicle alone (▪), 5 nM OA (▨), or 1 μM OA (■) to the lysates. Activities were expressed as a percentage of 32P release in untreated lysates. Data shown were mean ± SD of triplicate assays from at least 2 separate experiments.
Fig. 3.

PP2A activity is significantly inhibited by in vivo OA and fostriecin treatment.

(A) Phosphatase activity in lysates of cells treated with 0.5 μM OA (OA) using either 32P-labeled phosphorylase a (upper panel) or 32P-labeled histone H1 (lower panel) as substrate. (B) Phosphatase activity in lysates of cells treated with 5 μM fostriecin (fostriecin) using 32P-labeled phosphorylase a as substrate. Cells exposed to vehicle alone (untreated) were used as controls. Assays were performed with further addition of vehicle alone (▪), 5 nM OA (▨), or 1 μM OA (■) to the lysates. Activities were expressed as a percentage of 32P release in untreated lysates. Data shown were mean ± SD of triplicate assays from at least 2 separate experiments.

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