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. 2012 Aug 17;82(3):428–437. doi: 10.1124/mol.112.077966

Fig. 5.

Fig. 5.

A, Western blot analyses indicating the phosphorylation status of Kv11.1-HA-R887H compared with that of the wild-type channel and effects of stimulation of PKCs with 200 pM PMA + 10 μM PKC 20-28. B, densitometry analysis of phosphorylated Kv11.1-HA-WT or Kv11.1-HA-S890A relative to total protein. C and D, representative tail currents and amplitude histograms of the basal current activity from Kv11.1-HA-WT (n = 8) or Kv11.1-HA-R887H (n = 8) channels in CHO cells. E, quantification of Kv11.1-HA-WT (open bars) or Kv11.1-HA-S890A (orange bars) surface expression in CHO cells in response to 200 pM PMA for 2 h or PMA + PKC 20-28 or in cells expressing shRNA PKCα and compared with untreated cells. Each value represents the mean ± S.E. of at least six determinants in eight independent experiments. *, significant difference from the control (untreated) (P < 0.05, t test). F, Western blot analysis of Kv11.1-HA-WT or Kv11.1-HA-R887H in cytoplasm and plasma membrane fractions of CHO cells 18 h after transfection. Actin was detected only in the cytoplasmic fraction and was used as a loading control. G, amount of Kv11.1-HA-WT or Kv11.1-HA-R887H in the plasma membrane- or cytoplasm-containing fraction (relative to total = cytosol + membrane). The graphs represent consolidated data for each mutant from a representative of three experiments performed in triplicate, and the error bars show the S.D.s of triplicates. All the experiments were done in parallel. IP, immunoprecipitation; IB, immunoblot.