Figure 3. Gαq-deficient B cells are hyperresponsive to BCR triggering. (A–D) Splenic B cells from Gnaq−/− and WT chimeras were stimulated with anti-IgM F(ab′)2 for 0–30 min. Protein lysates were prepared from negatively selected total B cells (A and D) or from enriched FOB and MZB cells (D) and then analyzed by Western blotting. Akt (p-Ser473), PLCγ2, and Erk were probed with phospho-specific Abs and protein-specific Abs. Li-COR quantitative densitometry was used to determine the fold changes in phospho-Akt (B) and phospho-PLCγ2 (C). The ratios of phospho-specific proteins versus total ERK or PLCγ2 were obtained and data were normalized to WT B cells at time 0 (set as 1). Data in all panels are representative of two independent experiments.
Figure 3.

Gαq-deficient B cells are hyperresponsive to BCR triggering. (A–D) Splenic B cells from Gnaq−/− and WT chimeras were stimulated with anti-IgM F(ab′)2 for 0–30 min. Protein lysates were prepared from negatively selected total B cells (A and D) or from enriched FOB and MZB cells (D) and then analyzed by Western blotting. Akt (p-Ser473), PLCγ2, and Erk were probed with phospho-specific Abs and protein-specific Abs. Li-COR quantitative densitometry was used to determine the fold changes in phospho-Akt (B) and phospho-PLCγ2 (C). The ratios of phospho-specific proteins versus total ERK or PLCγ2 were obtained and data were normalized to WT B cells at time 0 (set as 1). Data in all panels are representative of two independent experiments.

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