| First Author | Ochala J | Year | 2009 |
| Journal | Ups J Med Sci | Volume | 114 |
| Issue | 4 | Pages | 235-41 |
| PubMed ID | 19878039 | Mgi Jnum | J:302928 |
| Mgi Id | MGI:6510936 | Doi | 10.3109/03009730903276399 |
| Citation | Ochala J, et al. (2009) Maintenance of muscle mass, fiber size, and contractile function in mice lacking the Z-disc protein myotilin. Ups J Med Sci 114(4):235-41 |
| abstractText | BACKGROUND: Myofibrillar myopathies constitute a rare group of congenital neuromuscular disorders, frequently associated with mutations in Z-disc proteins such as myotilin. Myotilin location and interactions with other Z-disc proteins are clearly defined, but its role in the regulation of muscle structure and function remains unknown. The present study aims at investigating this specific role of myotilin. METHODS: Skeletal and cardiac muscles were collected from adult mice with a targeted deletion of myotilin (myo(-/-)) and wild-type animals (myo(+/+)). RESULTS AND CONCLUSION: Similar skeletal and cardiac muscle weights were observed in myo(-/-) and myo(+/+) mice. At the muscle cell level, the size and force production of single membrane permeabilized fibers were identical between myo(-/-) and myo(+/+) rodents. Thus, myotilin does not have a significant influence on muscle mass, muscle fiber size, or regulation of muscle contraction. Alternatively, compensatory over-expressions of other elements including proteins from the same subfamily, or Z-disc proteins such as telethonin, or intermediate filaments may compensate for the lack of myotilin. |
