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Analysis of Skeletal Muscle Function in the C57BL6/SV129 Syncoilin Knockout Mouse

Overview
Journal Mamm Genome
Specialty Genetics
Date 2008 Jul 3
PMID 18594912
Citations 7
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Abstract

Syncoilin is a 64-kDa intermediate filament protein expressed in skeletal muscle and enriched at the perinucleus, sarcolemma, and myotendinous and neuromuscular junctions. Due to its pattern of cellular localization and binding partners, syncoilin is an ideal candidate to be both an important structural component of myocytes and a potential mediator of inherited myopathies. Here we present a report of a knockout mouse model for syncoilin and the results of an investigation into the effect of a syncoilin null state on striated muscle function in 6-8-week-old mice. An analysis of proteins known to associate with syncoilin showed that ablation of syncoilin had no effect on absolute expression or spatial localization of desmin or alpha dystrobrevin. Our syncoilin-null animal exhibited no differences in cardiotoxin-induced muscle regeneration, voluntary wheel running, or enforced treadmill exercise capacity, relative to wild-type controls. Finally, a mechanical investigation of isolated soleus and extensor digitorum longus indicated a potential differential reduction in muscle strength and resilience. We are the first to present data identifying an increased susceptibility to muscle damage in response to an extended forced exercise regime in syncoilin-deficient muscle. This study establishes a second viable syncoilin knockout model and highlights the importance of further investigations to determine the role of syncoilin in skeletal muscle.

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References
1.
Sun N, Critchley D, Paulin D, Li Z, Robson R . Human alpha-synemin interacts directly with vinculin and metavinculin. Biochem J. 2007; 409(3):657-67. DOI: 10.1042/BJ20071188. View

2.
Kreplak L, Herrmann H, Aebi U . Tensile properties of single desmin intermediate filaments. Biophys J. 2008; 94(7):2790-9. PMC: 2267133. DOI: 10.1529/biophysj.107.119826. View

3.
Bellin R, Huiatt T, Critchley D, Robson R . Synemin may function to directly link muscle cell intermediate filaments to both myofibrillar Z-lines and costameres. J Biol Chem. 2001; 276(34):32330-7. DOI: 10.1074/jbc.M104005200. View

4.
Olive M, Goldfarb L, Moreno D, Laforet E, Dagvadorj A, Sambuughin N . Desmin-related myopathy: clinical, electrophysiological, radiological, neuropathological and genetic studies. J Neurol Sci. 2004; 219(1-2):125-37. DOI: 10.1016/j.jns.2004.01.007. View

5.
Shi X, Garry D . Muscle stem cells in development, regeneration, and disease. Genes Dev. 2006; 20(13):1692-708. DOI: 10.1101/gad.1419406. View