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).