Decorin activates Akt downstream of IGF-IR and promotes myoblast differentiation.

Decorin, a small leucine-rich proteoglycan, plays an important role in cellular activities through modification of growth factors. It also acts as a signaling molecule to non-muscle cells through epidermal growth factor receptor or insulin-like growth factor I receptor (IGF-IR). However, it is unclear if decorin acts as a signaling molecule to myogenic cells. In this study, we investigated the effect of decorin on the differentiation of myoblasts and the signaling via IGF-IR to myogenic cells. C2C12 myoblasts cultured in media containing decorin for 72 h showed more extensive formation of multinucleated myotubes than control cells cultured in the same media without decorin. The protein expressions of myogenin and myosin heavy chian were higher in decorn-treated cells than in control cells. These results suggest that decorin enhances the differentiation of myoblasts. Western blot analysis and immunocytochemistry showed that IGF-IR was expressed in myoblasts and myotubes. Furthermore, Akt, which is downstream of IGF-IR, was more phosphorylated in myoblasts cultured in media containing decorin than those in media without decorin. These results suggest that decorin activates Akt downstream of IGF-IR and enhances the differentiation of myogenic cells.