Figure 4
Figure 4. Goat anti-μ F(ab′)2–mediated membrane-proximal events. (A) Ca2+ flux in response to goat anti-μ F(ab′)2 was assayed for 5 minutes. Scatter plots of fold change in Ca2+ flux relative to control in 16 U-CLL versus 16 M-CLL cases. (B) Scatterplots depicting fold change in phospho-Akt, phospho-Erk, and phospho-p38MAPK levels in 20 B-CLL cases divided into U-CLL and M-CLL subgroups. U-CLL and M-CLL exhibited significant differences in the extent of phospho-Akt and phospho-Erk up-regulation after exposure to goat anti-μ. (C) Comparison of efficacy of HB57-dex and goat anti-μ F(ab′)2 in eliciting protein phosphorylation of Akt, Erk, and p38 MAPK, in B cells from 20 CLL cases. Goat anti-μ elicited a stronger response in terms of Akt phosphorylations than HB57-dex did (P < .05).

Goat anti-μ F(ab′)2–mediated membrane-proximal events. (A) Ca2+ flux in response to goat anti-μ F(ab′)2 was assayed for 5 minutes. Scatter plots of fold change in Ca2+ flux relative to control in 16 U-CLL versus 16 M-CLL cases. (B) Scatterplots depicting fold change in phospho-Akt, phospho-Erk, and phospho-p38MAPK levels in 20 B-CLL cases divided into U-CLL and M-CLL subgroups. U-CLL and M-CLL exhibited significant differences in the extent of phospho-Akt and phospho-Erk up-regulation after exposure to goat anti-μ. (C) Comparison of efficacy of HB57-dex and goat anti-μ F(ab′)2 in eliciting protein phosphorylation of Akt, Erk, and p38 MAPK, in B cells from 20 CLL cases. Goat anti-μ elicited a stronger response in terms of Akt phosphorylations than HB57-dex did (P < .05).

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