期刊
AMERICAN JOURNAL OF PHYSIOLOGY-ENDOCRINOLOGY AND METABOLISM
卷 280, 期 2, 页码 E221-E228出版社
AMER PHYSIOLOGICAL SOC
DOI: 10.1152/ajpendo.2001.280.2.E221
关键词
myoblast; myotube; growth differentiation factor 8; sarcopenia; growth differentiation factor
资金
- NIA NIH HHS [1RO1 AG-14369] Funding Source: Medline
- NIDDK NIH HHS [1RO1 DK-46296] Funding Source: Medline
- NIGMS NIH HHS [5SO6 GM-08140-23] Funding Source: Medline
Myostatin mutations in mice and cattle are associated with increased muscularity, suggesting that myostatin is a negative regulator of skeletal muscle mass. To test the hypothesis that myostatin inhibits muscle cell growth, we examined the effects of recombinant myostatin in mouse skeletal muscle C2C12 cells. After verification of the expression of cDNA constructs in a cell-free system and in transfected Chinese hamster ovary cells, the human recombinant protein was expressed as the full-length (375-amino acid) myostatin in Drosophila cells (Mst375D), or the 110-amino acid carboxy-terminal protein in Escherichia coli (Mst110EC). These proteins were identified by immunoblotting and were purified. Both Mst375D and Mst110EC dose dependently inhibited cell proliferation (cell count and Formazan assay), DNA synthesis ([H-3] thymidine incorporation), and protein synthesis ([1-C-14] leucine incorporation) in C2C12 cells. The inhibitory effects of both proteins were greater in myotubes than in myoblasts. Neither protein had any significant effects on protein degradation or apoptosis. In conclusion, recombinant myostatin proteins inhibit cell proliferation, DNA synthesis, and protein synthesis in C2C12 muscle cells, suggesting that myostatin may control muscle mass by inhibiting muscle growth or regeneration.
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