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Bone morphogenetic protein-12 and -13 inhibit terminal differentiation of myoblasts, but do not induce their
M Inada1, T Katagiri, S Akiyama
1Department of Biochemistry, School of Dentistry, Showa University, Tokyo, Japan.
Abstract:
Effects of bone morphogenetic protein (BMP)-12 and BMP-13, new members of the BMP family which belong to the transforming growth factor (TGF)-beta superfamily, on terminal differentiation of myoblasts were examined in C2C12 and L-6 myoblasts. When the myoblasts were cultured with BMP-12 or BMP-13, the expression of the myosin heavy chain and the formation of multinucleated myotubes mRNA in L-6 cells. The inhibitory effects of BMP-12 and BMP-13 on myogenic differentiation were similar to the effects of BMP-2, though their potencies were lower than BMP-2. Unlike BMP-2, neither BMP-12 nor BMP-13 induced alkaline phosphatase activity in C2C12 myoblasts. The differences in the biological activities of these new BMPs suggest that the intracellular signalling pathway used by BMP-12 and BMP-13 differs from that of BMP-2.
Insights
Bone morphogenetic proteins (BMPs) -12 and -13 inhibit myoblast differentiation, similar to BMP-2 but with lower potency. These new BMPs may utilize distinct intracellular pathways compared to BMP-2.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Bone morphogenetic proteins (BMPs) are crucial signaling molecules in the transforming growth factor (TGF)-beta superfamily.
- BMPs play significant roles in cell differentiation, proliferation, and development.
- Understanding the specific functions of novel BMPs is essential for elucidating cellular processes.
Purpose of the Study:
- To investigate the effects of novel bone morphogenetic proteins (BMPs)-12 and -13 on the terminal differentiation of myoblasts.
- To compare the myogenic differentiation activities of BMP-12 and BMP-13 with a known BMP, BMP-2.
- To explore potential differences in intracellular signaling pathways utilized by these BMPs.
Main Methods:
- C2C12 and L-6 myoblasts were cultured in the presence of BMP-12 or BMP-13.
- Myogenic differentiation was assessed by measuring myosin heavy chain expression and multinucleated myotube formation.
- Alkaline phosphatase activity was evaluated in C2C12 myoblasts.
Main Results:
- BMP-12 and BMP-13 inhibited the expression of myosin heavy chain mRNA and the formation of multinucleated myotubes in L-6 cells.
- The inhibitory effects of BMP-12 and BMP-13 on myogenic differentiation were comparable to BMP-2, albeit with lower potency.
- Neither BMP-12 nor BMP-13 induced alkaline phosphatase activity in C2C12 myoblasts, unlike BMP-2.
Conclusions:
- BMP-12 and BMP-13 exhibit inhibitory effects on myoblast terminal differentiation.
- The biological activities of BMP-12 and BMP-13 suggest they may engage distinct intracellular signaling pathways compared to BMP-2.
- Further research is warranted to fully elucidate the signaling mechanisms of BMP-12 and BMP-13 in myogenesis.