Data on MyoD reduction by autophagy in C2C12 cells

Autophagy is a highly regulated physiologic mechanism in which cells maintain homeostasis by degrading excessive or unnecessary proteins and damaged or aged organelles through the lysosomal machinery (Yorimitsu and Klionsky, 2005) [1]. MyoD is basic helix-loop-helix (bHLH) transcription factors that regulate myoblast proliferation and myogenic differentiation. MyoD is expressed in adult skeletal muscle (Megeney et al., 1996) [2] and adult fibers (Brack et al., 2005) [3]. MyoD is mainly degraded by the ubiquitin-proteasome system (Floyd et al., 2001) [4] and partly by autophagy (Kim et al., 2012) [5]. Data showed that autophagy decreased MyoD protein in C2C12 cells by Western blotting analysis.


a b s t r a c t
Autophagy is a highly regulated physiologic mechanism in which cells maintain homeostasis by degrading excessive or unnecessary proteins and damaged or aged organelles through the lysosomal machinery (Yorimitsu and Klionsky, 2005) [1]. MyoD is basic helixloop-helix (bHLH) transcription factors that regulate myoblast proliferation and myogenic differentiation. MyoD is expressed in adult skeletal muscle (Megeney et al., 1996) [2] and adult fibers (Brack et al., 2005) [3]. MyoD is mainly degraded by the ubiquitinproteasome system (Floyd et al., 2001) [4] and partly by autophagy (Kim et al., 2012) [5]. Data

How data was acquired
Western blotting analysis, real-time PCR

Data format
Analyzed Experimental factors Autophagy in C2C12 cells was induced by treatment of high fetal bovine serum (FBS).

Experimental features
MyoD degradation by autophagy showed Western blotting under high concentrations of FBS. Data source location Chuncheon, Gangwon-do, Republic of Korea Data accessibility All data are available with this article

Value of the data
This data could give a base for the detection of MyoD protein in both muscle cells and C2C12 cells by Western blotting analysis.
The data will be useful for investigating that nutrition oversupply including high concentration of FBS may increase autophagy in both muscle cells and C2C12 cells.
The data allow us to promote that regulation of MyoD protein may suppress myoblast proliferation and myogenic differentiation.

Data
The autophagy was increased by treatment of dose-dependent FBS (1-20%) and a subsequent autophagy markers, LC3II and Beclin-1 proteins significantly increased (Fig. 1). Cell proliferation signal phospho-ERK significantly decreased according to dose-dependent FBS (Fig. 2). Proapoptotic molecule Bax protein expression was increased in more than 5% FBS treatments compared to the absence of FBS and antiapoptotic molecule Bcl-2 protein expression was reduced in more than 2% FBS treatments (Fig. 3). Under the same conditions, cytosolic MyoD protein was significantly decreased in 10 and 20% FBS condition (Fig. 4A), but MyoD mRNA did not change (Fig. 4B). C2C12 cells were treated with autophagy inhibitor bafilomycin A1, and then completely blocked degradation of MyoD (Fig. 5). Together, these results suggest that high FBS-induced autophagy results in degradation of MyoD protein in C2C12 myoblast cells.

Transparency document. Supporting information
Transparency data associated with this article can be found in the online version at http://dx.doi. org/10.1016/j.dib.2017.06.034.