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Fig. 7. Characterization of signaling proteins or pathways activated by SDF1 in C2C12 cells. C2C12 cells were stimulated for 10 minutes with SDF1 at the indicated concentrations and subsequently analyzed for activation (phosphorylation) of Akt, p38, Erk and different PKC isoforms by western blotting using phosphospecific antibodies. Protein loading was controlled by staining blots with (pan) antibodies that recognize the non-phosphorylated forms of the respective signaling molecules. In case of PKC isoforms, β-actin staining in combination with staining for all phosphorylated PKC isoforms using P-PKC-pan served as a loading control. SDF1 induced a dose-dependent increase in levels of phosphorylated Erk1, Erk2 or PKC ${zeta}$ , PKC ${lambda}$ [(p)-Erk1, (p)-Erk2 or (p)-PKC ${zeta}$ , (p)-PKC ${lambda}$ , respectively], but showed no effects on phosphorylated levels of Akt, p38 or pPKC ${alpha}$ , PKC β [(p)-Akt, (p)-p38 or (p)-PKC ${alpha}$ , (p)-PKCβ, respectively].

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