CMD, LGMD: New Light Shed on Sugar-Coating Process

New understanding of how the alpha-dystroglycan protein is glycosylated (sugar-coated) may have relevance for treating some forms of congenital and limb-girdle muscular dystrophy

by Quest Staff on August 13, 2013 - 3:19pm

Glycosylation — "sugar-coating" — of the muscle protein alpha-dystroglycan is known to be a crucial part of muscle function.

Without sufficient glycosylation, alpha-dystroglycan doesn't stick well to other proteins, and an important linkage between muscle fibers and their surroundings is disrupted.

Several forms of congenital muscular dystrophy (CMD) — Fukuyama CMD, Santavuori muscle-eye-brain disease and Walker-Warburg syndrome — and several types of limb-girdle muscular dystrophy (LGMD) — LGMD2I, LGMD2K, LGMD2M, LGMD2N and LGMD2O — appear to be caused by insufficient glycosylation of alpha-dystroglycan.

Now, biophysicist Kevin Campbell at the University of Iowa, and colleagues, have shed additional light on the highly complex mechanism by which sugar molecules are added to alpha-dystroglycan. These insights may contribute to the development of treatments for CMD and LGMD related to glycosylation abnormalities.

The results were published online Aug. 8, 2013, in Science.

Campbell has a current MDA grant for research closely related to this study.

For more information, see Muscle Health Depends on Sugar Superstructure (Science Daily).

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