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

Matthew M. Goddeeris, Biming Wu, David Venzke, Takako Yoshida-Moriguchi, Fumiaki Saito, Kiichiro Matsumura, Steven A. Moore and Kevin P. Campbell ()
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Matthew M. Goddeeris: Howard Hughes Medical Institute, 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
David Venzke: Howard Hughes Medical Institute, 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
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

Nature, 2013, vol. 503, issue 7474, 136-140

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.

Date: 2013
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DOI: 10.1038/nature12605

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