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. Author manuscript; available in PMC: 2011 Aug 1.
Published in final edited form as: Biochim Biophys Acta. 2010 Mar 29;1803(8):960–967. doi: 10.1016/j.bbamcr.2010.03.019

Figure 3. CREB signaling is abnormal in 21day STZ-treated rat muscle.

Figure 3

(A) The phosphorylation (i.e., activation) status of CREB in gastrocnemius muscles of control and 21d STZ-treated rats was examined by Western blot analysis using antibodies that detect phospho-Ser133 and total CREB. Data are expressed as the mean ratio of phosphorylated protein to total protein ± SEM. Equal protein loading and transfer were confirmed by Ponceau S staining. n=6/group, *P<0.05. (B) To evaluate CREB function, the amounts of DHPRα1s, a gene target of CREB, were measured in gastrocnemius muscles by real time RT-PCR. Data are expressed as the mean ± SEM; n=8/group, *P<0.05.