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Subcellular fractionation of dystrophin to the triads of skeletal muscle

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Abstract

Duchenne muscular dystrophy (DMD) is a human X-linked biochemical defect resulting in the progressive wasting of skeletal muscle of affected individuals1. It is the most common and is considered to be the most devastating of the muscular dystrophies, affecting about 1 in 3,500 live-born males2. The gene that, when defective, results in this disorder was recently isolated3–6. Using the cloned complementary DNA sequences corresponding to the DMD gene, antibodies have been produced that react with a protein species of relative molecular mass (Mr) ∼400,000 (400K) which was absent in two DMD-affected individuals and in mdx mice7. This protein species is called dystrophin because of its identification by molecular-genetic analysis of affected individuals. Here we show that dystrophin is associated with the triadic junctions in skeletal muscle, and is therefore probably involved with Ca2+ homoeostasis. We also show that the ∼450K ryanodine receptor/sarcoplasmic reticulum Ca2+ channel8, which has the large size and subcellular distribution characteristics of dystrophin, is an immunologically distinct protein species.

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Authors and Affiliations

  1. Department of Pediatrics, Harvard Medical School and Division of Genetics, Children's Hospital,

    Eric P. Hoffman & Louis M. Kunkel

  2. Howard Hughes Medical Institute, Boston, Massachusetts, 02115, USA

    Louis M. Kunkel

  3. Department of Physiology and Biophysics, University of Iowa, Iowa City, Iowa, 52242, USA

    C. Michael Knudson & Kevin P. Campbell

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  1. Eric P. Hoffman
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  2. C. Michael Knudson
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  3. Kevin P. Campbell
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  4. Louis M. Kunkel
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Hoffman, E., Knudson, C., Campbell, K. et al. Subcellular fractionation of dystrophin to the triads of skeletal muscle. Nature 330, 754–758 (1987). https://doi.org/10.1038/330754a0

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