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LARGE glycans on dystroglycan function as a tunable matrix scaffold to prevent dystrophy

Author

Listed:
  • Matthew M. Goddeeris

    (Howard Hughes Medical Institute, Roy J. and Lucille A. Carver College of Medicine, The University of Iowa
    Roy J. and Lucille A. Carver College of Medicine, The University of Iowa)

  • Biming Wu

    (Howard Hughes Medical Institute, Roy J. and Lucille A. Carver College of Medicine, The University of Iowa
    Roy J. and Lucille A. Carver College of Medicine, The University of Iowa
    Present address: Department of Biomedical Engineering, University of Michigan, Ann Arbor, Michigan 48109, USA.)

  • David Venzke

    (Howard Hughes Medical Institute, Roy J. and Lucille A. Carver College of Medicine, The University of Iowa
    Roy J. and Lucille A. Carver College of Medicine, The University of Iowa)

  • Takako Yoshida-Moriguchi

    (Howard Hughes Medical Institute, Roy J. and Lucille A. Carver College of Medicine, The University of Iowa
    Roy J. and Lucille A. Carver College of Medicine, The University of Iowa)

  • Fumiaki Saito

    (Teikyo University School of Medicine, 2-11-1 Kaga, Itabashi-ku, Tokyo 173-8605, Japan)

  • Kiichiro Matsumura

    (Teikyo University School of Medicine, 2-11-1 Kaga, Itabashi-ku, Tokyo 173-8605, Japan)

  • Steven A. Moore

    (Roy J. and Lucille A. Carver College of Medicine, The University of Iowa)

  • Kevin P. Campbell

    (Howard Hughes Medical Institute, Roy J. and Lucille A. Carver College of Medicine, The University of Iowa
    Roy J. and Lucille A. Carver College of Medicine, The University of Iowa
    Roy J. and Lucille A. Carver College of Medicine, The University of Iowa
    Roy J. and Lucille A. Carver College of Medicine, The University of Iowa)

Abstract

This study finds a direct correlation between LARGE-glycan extension on dystroglycan and the protein’s capacity for extracellular matrix ligands; in regenerating mouse muscle, short LARGE-glycan polysaccharides cause various defects, including muscle dysfunction and a predisposition to dystrophy, and in muscular dystrophy patients, increased clinical severity of disease corresponds to shorter LARGE-glycans.

Suggested Citation

  • Matthew M. Goddeeris & Biming Wu & David Venzke & Takako Yoshida-Moriguchi & Fumiaki Saito & Kiichiro Matsumura & Steven A. Moore & Kevin P. Campbell, 2013. "LARGE glycans on dystroglycan function as a tunable matrix scaffold to prevent dystrophy," Nature, Nature, vol. 503(7474), pages 136-140, November.
    • Handle: RePEc:nat:nature:v:503:y:2013:i:7474:d:10.1038_nature12605
    DOI: 10.1038/nature12605
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    Cited by:

    1. M. Osman Sheikh & Chantelle J. Capicciotti & Lin Liu & Jeremy Praissman & Dahai Ding & Daniel G. Mead & Melinda A. Brindley & Tobias Willer & Kevin P. Campbell & Kelley W. Moremen & Lance Wells & Geer, 2022. "Cell surface glycan engineering reveals that matriglycan alone can recapitulate dystroglycan binding and function," Nature Communications, Nature, vol. 13(1), pages 1-13, December.

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