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Association of dystrophin and an integral membrane glycoprotein

Nature volume 338, pages 259–262 (1989)Cite this article

Abstract

DUCHENNE muscular dystrophy (DMD) is caused by a defective gene found on the X-chromosome1. Dystrophin is encoded by the DMD gene and represents about 0.002% of total muscle protein2. Immunochemical studies have shown that dystrophin is localized to the sarcolemma in normal muscle but is absent in muscle from DMD patients3–7. Many features of the predicted primary struc-ture of dystrophin are shared with membrane cytoskeletal pro-teins8, but the precise function of dystrophin in muscle is unknown. Here we report the first isolation of dystrophin from digitonin-solubilized skeletal muscle membranes using wheat germ agglutinin (WGA)-Sepharose. We find that dystrophin is not a glycoprotein but binds to WGA-Sepharose because of its tight association with a WGA-binding glycoprotein. The association of dystrophin with this glycoprotein is disrupted by agents that dis-sociate cytoskeletal proteins from membranes. We conclude that dystrophin is linked to an integral membrane glycoprotein in the sarcolemma. Our results indicate that the function of dystrophin could be to link this glycoprotein to the underlying cytoskeleton and thus help either to preserve membrane stability or to keep the glycoprotein non-uniformly distributed in the sarcolemma.

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Authors and Affiliations

  1. Department of Physiology and Biophysics, The University of Iowa College of Medicine, Iowa City, Iowa, 52242, USA

    Kevin P. Campbell & Steven D. Kahl

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  1. Kevin P. Campbell
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  2. Steven D. Kahl
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Campbell, K., Kahl, S. Association of dystrophin and an integral membrane glycoprotein. Nature 338, 259–262 (1989). https://doi.org/10.1038/338259a0

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