A homozygous DPM3 mutation in a patient with alpha-dystroglycan-related limb girdle muscular dystrophy.

Van den Bergh PYK., Sznajer Y., Van Parys V., van Tol W., Wevers RA., Lefeber DJ., Xu L., Lek M., MacArthur DG., Johnson K., Phillips L., Töpf A., Straub V.

Defects of O-linked glycosylation of alpha-dystroglycan cause a wide spectrum of muscular dystrophies ranging from severe congenital muscular dystrophy associated with abnormal brain and eye development to mild limb girdle muscular dystrophy. We report a female patient who developed isolated pelvic girdle muscle weakness and wasting, which became symptomatic at age 42. Exome sequencing uncovered a homozygous c.131T > G (p.Leu44Pro) substitution in DPM3, encoding dolichol-P-mannose (DPM) synthase subunit 3, leading to a 50% reduction of enzymatic activity. Decreased availability of DPM as an essential donor substrate for protein O-mannosyltransferase (POMT) 1 and 2 explains defective skeletal muscle alpha-dystroglycan O-glycosylation. Our findings show that DPM3 mutations may lead to an isolated and mild limb girdle muscular dystrophy phenotype without cardiomyopathy.

DOI

10.1016/j.nmd.2017.07.006

Type

Journal article

Publication Date

2017-11-01T00:00:00+00:00

Volume

27

Pages

1043 - 1046

Total pages

3

Keywords

Alpha-dystroglycan, DPM3, Dolichol-P-mannose synthase, Limb girdle muscular dystrophy, Dystroglycans, Female, Homozygote, Humans, Mannosyltransferases, Membrane Proteins, Middle Aged, Muscle, Skeletal, Muscular Dystrophies, Limb-Girdle, Mutation, Phenotype

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