Absence of gamma-sarcoglycan alters the response of p70S6 kinase to mechanical perturbation in murine skeletal muscle
- Moorwood C, Philippou A, Spinazzola J, Keyser B, Macarak EJ, Barton ER
- July 1, 2014
This research paper explores a crucial part of our muscles called the dystrophin glycoprotein complex (DGC), which helps keep our muscle cells strong and healthy. When parts of this system are damaged, it can lead to serious conditions like Duchenne Muscular Dystrophy or Limb Girdle Muscular Dystrophy that weaken the body's muscles over time. Scientists conducted experiments using different types of mouse cells and isolated muscle tissues from mice with these genetic mutations, as well as normal ones. They stretched the muscle samples to see how they respond under stress-a process similar to what happens when we exercise or move our bodies in certain ways. The researchers looked at specific proteins within the cells that change their behavior during this kind of physical activity and examined if calcium, a mineral essential for many cell functions including muscle contractions, played any role in these changes. They also studied how an important signaling molecule called mTOR is involved when our muscles are stretched or contracted.
This research paper investigates the structural and functional properties of the dystrophin glycoprotein complex (DGC) in various muscle cell types, including skeletal, cardiac, and smooth muscles. The DGC plays a crucial role by linking the extracellular matrix to the intracellular cytoskeleton for structural support within these cells [1-3]. Mutations leading to different forms of muscular dystrophy are associated with alterations in components of this complex, such as mutations in dystrophin causing Duchenne Muscular Dystrophy (DMD) and various sarcoglycan gene mutations resulting in Limb Girdle Muscular Dystrophy (LGMD). To understand the mechanisms underlying these diseases better, researchers employed a methodology involving cyclic passive stretch of myotubes, primary cultures from C57Bl/6 mice and isolated muscles with γ-sarcoglycan mutations. They used immunoblotting techniques to detect phosphorylation levels in lysates obtained after applying mechanical stress [4].
MLA
C, Moorwood, et al. “Absence of gamma-sarcoglycan alters the response of p70S6 kinase to mechanical perturbation in murine skeletal muscle.” PubMed Central, National Center for Biotechnology Information, https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4095884/. Accessed 30 Sept 2026.
Chicago
C, Moorwood, et al. “Absence of gamma-sarcoglycan alters the response of p70S6 kinase to mechanical perturbation in murine skeletal muscle.” PubMed Central. 30 September 2026. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4095884/.