Page 40046, legend to Fig. 5A:
The first sentence should read "the PKA inhibitor H89 causes a
stimulation of G6PD" (not "an inhibition of G6PD"). The figure
and its correct legend are shown below.
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Fig. 5.
A, the PKA inhibitor H89 causes a
stimulation of G6PD activity in normal and high glucose. BAEC were
treated as in Fig. 1B, incubated with glucose for 24 h,
and then exposed to 50 µM H89 for 15 min. G6PD activity
was measured. Data were normalized by protein and expressed as
means ± S.E. of five separate experiments, each run in triplicate
(**, p < 0.005; ***, p < 0.001 compared with control). B, effect of PKA on G6PD activity.
BAEC were grown to 80% confluent and then lysed. Lysates were
incubated for 30 min at room temperature in the presence of the PKA
catalytic subunit in a buffer containing 25 mM Tris/HCl, pH
7.4, 1.3 mM dithiothreitol, and 5 mM Mg-ATP.
Units of PKA correspond to picomoles of phosphate/min.
Values shown are means ± S.E. of data from three separate
experiments (**, p < 0.005; ***, p < 0.001 compared with control). C, high glucose increases
phosphorylation of G6PD. BAEC that were 80% confluent were exposed to
32P. Then the glucose concentration was increased. After
3 h cells were harvested and lysed, and G6PD was
immunoprecipitated using antibody to G6PD. Following
immunoprecipitation, G6PD protein was resolved by SDS-polyacrylamide
gel electrophoresis and then exposed to x-ray film. N,
normal glucose; H, high glucose. Also the same experiment
was done using cells that were transiently transfected with G6PD tagged
with the epitope FLAG (data not shown). G6PD was then
immunoprecipitated using the antibody directed against the FLAG
epitope. The results were identical to those shown above in that
high glucose led to phosphorylation of FLAG-G6PD.
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