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Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy
Published on: December 16, 2021
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Protein arginine methyltransferase expression and activity during myogenesis
Nicole Y Shen, Sean Y Ng, Stephen L Toepp
1Department of Kinesiology, McMaster University, Hamilton, Ontario, Canada ljubicic@mcmaster.ca.
Bioscience Reports
|December 7, 2017
Summary
Protein arginine methyltransferases (PRMTs) are crucial for skeletal muscle development. PRMT1 expression increases during myogenesis, and its inhibition impairs muscle differentiation and mitochondrial function.
Area of Science:
- Biochemistry
- Cell Biology
- Muscle Physiology
Background:
- Protein arginine methyltransferases (PRMTs) play a role in skeletal muscle plasticity.
- The specific roles of PRMTs during muscle development are not fully understood.
Purpose of the Study:
- To investigate the expression and function of PRMT1, -4, and -5 during myogenesis.
- To elucidate the role of PRMT1 in skeletal muscle differentiation.
Main Methods:
- Utilized C2C12 muscle cells as an in vitro model for myogenesis.
- Assessed PRMT expression, activity (MMA, SDMA, ADMA), and histone methylation.
- Inhibited PRMT1 using TC-E 5003 to evaluate its impact on differentiation and mitochondrial function.
Main Results:
- PRMT1 mRNA and protein levels significantly increased during myogenesis, while PRMT4 and -5 remained unchanged.
- Asymmetric dimethylarginine (ADMA) levels, indicating Type I PRMT activity, increased during differentiation.
- PRMT1 inhibition led to decreased muscle differentiation, mitochondrial biogenesis, and respiratory function.
Conclusions:
- PRMTs exhibit specific expression patterns and target methylation during skeletal muscle development.
- PRMT1 plays a critical role in driving muscle differentiation through a mitochondrially mediated mechanism.
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