Abstract
The primary defect in Duchenne muscular dystrophy (DMD) is unknown but muscle growth failure and wasting of skeletal muscle must be the result of an imbalance between protein synthesis and degradation, that is, the rate of muscle protein synthesis is insufficient to replace degraded proteins and expand the protein mass. In patients with DMD, excretion of 3-methylhistidine is dramatically increased relative to creatinine and this is commonly accepted as evidence of increased muscle myofibrillar degradation1–3. As rapid wasting of muscle has not been observed to occur in the disease, increased protein degradation ought to be accompanied by increased protein synthesis and this has been observed or implied from measurements in animal models of the disease4–6. However, so far no direct measurements of muscle protein synthesis or degradation have been made in patients. We report here the first direct measurements in vivo of rates of skeletal muscle protein synthesis in patients suffering from DMD. The results, obtained using stable isotope tracers, clearly show that a marked reduction in muscle protein synthesis is the primary cause of the growth failure and that muscle protein degradation cannot be elevated.
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Rennie, M., Edwards, R., Millward, D. et al. Effects of Duchenne muscular dystrophy on muscle protein synthesis. Nature 296, 165–167 (1982). https://doi.org/10.1038/296165a0
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DOI: https://doi.org/10.1038/296165a0
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