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MFG-E8 protein promotes C2C12 myogenic differentiation by enhancing PI3K/Akt signaling

journal contribution
posted on 2023-05-03, 10:25 authored by He Li, Ying Ma, Weili Xu, Haoran Chen, Li DayLi Day
Milk fat globule-EGF factor 8 (MFG-E8) protein can promote growth factor induced survival and proliferation of vascular endothelial cells, leading to angiogenesis. Little has been reported on the potential effects of MFG-E8 on cell differentiation and the molecular mechanism. In this study, MFG-E8, the major component of milk fat globule membrane (MFGM) protein (82.35%), was isolated and purified using cellulose DEAE-52. Its effects on myogenic differentiation of murine skeletal muscle C2C12 cells were investigated using qRT-PCR, Western blotting and immunofluorescence assay. MFG-E8 promoted the formation of multinucleated myotubes, and increased the fusion index. In addition, Akt-activity was significantly increased during MFG-E8 induced C2C12 cell differentiation, whereas wortmannin, a PI3K inhibitor, was able to block the differentiation of C2C12 cells promoted by MFG-E8. MFG-E8 enhanced the expression of the myogenic regulatory factor MyHC in C2C12 cells over time. Conversely, the expression of MyHC was also inhibited by wortmannin. We conclude that MFG-E8 promotes the differentiation of C2C12 cells by activating the PI3K/Akt signaling pathway. Taken together, these results show that MFG-E8 could exert a beneficial effect on C2C12 myoblast cell differentiation, and therefore, it may have potential as a differentiation-inducing agent for the therapy of sarcopenia.


Rights statement

©The Royal Society of Chemistry and the Centre National de la Recherche Scientifique 2017


  • English

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Royal Society of Chemistry

Journal title

New Journal of Chemistry




Li, H., Ma, Y., Xu, W., Chen, H., & Day, L. (2017). MFG-E8 protein promotes C2C12 myogenic differentiation by enhancing PI3K/Akt signaling. New Journal of Chemistry, 41, 12061–12070. doi:10.1039/C7NJ02216F

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