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Protein degradation in cultured skeletal muscle from duchenne muscular dystrophy patients
Author(s) -
Neville Hans E.,
Harrold Sharon
Publication year - 1985
Publication title -
muscle and nerve
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.025
H-Index - 145
eISSN - 1097-4598
pISSN - 0148-639X
DOI - 10.1002/mus.880080312
Subject(s) - duchenne muscular dystrophy , myogenesis , multinucleate , itga7 , protein degradation , muscular dystrophy , skeletal muscle , muscle biopsy , myocyte , population , biology , dystrophin , biopsy , medicine , endocrinology , biochemistry , microbiology and biotechnology , environmental health
The loss of contractile protein in Duchenne muscular dystrophy could result from low rates of synthesis, abnormally high rates of protein degradation, or a combination of both. We measured overall protein degradation rates in cultured human muscle cells obtained at biopsy from patients with Duchenne dystrophy or various muscle diseases and normal subjects. Measurements were performed on confluent cultures exhibiting no growth and containing a mixed cell population of myoblasts, fibroblasts, and multinucleated myotubes. Using a new doubleisotope labeling protocol, we found protein degradation rates in all three groups to be similar ( K D = 0.0171–0.0176 hr −1 ), suggesting no detectable abnormality of overall protein degradation in cells derived from Duchenne dystrophy patients.