The pathological examination of biopsied skeletal muscle confirms the diagnosis of BMD. Immunohistochemical analyses of normal muscle demonstrate that dystrophin is present along with muscle cell membranes. Muscle from BMD patients contains reduced amounts of dystrophin that is stained discontinuously and patchy along the muscle cell membranes. Western blot analysis using dystrophin antibody reveals a band corresponding to 427 kDa, close to the predicted size of dystrophin, in extracts of normal muscle tissue. Shorter or lower amount of dystrophin is detected in muscle extracts from patients with BMD.
Dystrophin contains 3685 amino acids organized in four domains: N-terminal actin binding, triple helical rod, cystein-rich, and C-terminal domains. The internally truncated dystrophin identified in BMD maintains both N-terminal and C-terminal domains, but lacks some of the 24 repeat sequences of triple helical rod domain. Therefore, dystrophin is stained when antibody recognizing either N-terminal or C-terminal domains is used, but in some cases no dystrophin is stained as in DMD when antibody recognizing rod domain is employed.
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The use of dumbbells gives you a much more comprehensive strengthening effect because the workout engages your stabilizer muscles, in addition to the muscle you may be pin-pointing. Without all of the belts and artificial stabilizers of a machine, you also engage your core muscles, which are your body's natural stabilizers.