Muscular dystrophy and neuronal migration disorder caused by mutations in a glycosyltransferase, POMGnT1

Dev Cell. 2001 Nov;1(5):717-24. doi: 10.1016/s1534-5807(01)00070-3.

A Yoshida ¹, K Kobayashi, H Manya, K Taniguchi, H Kano, M Mizuno, T Inazu, H Mitsuhashi, S Takahashi, M Takeuchi, R Herrmann, V Straub, B Talim, T Voit, H Topaloglu, T Toda, T Endo

Affiliations

Affiliation

1 Central Laboratories for Key Technology, Kirin Brewery Co., Ltd., Kanazawa-ku, 236-0004, Yokohama, Japan.

PMID: 11709191 DOI: 10.1016/s1534-5807(01)00070-3

Abstract

Muscle-eye-brain disease (MEB) is an autosomal recessive disorder characterized by congenital muscular dystrophy, ocular abnormalities, and lissencephaly. Mammalian O-mannosyl glycosylation is a rare type of protein modification that is observed in a limited number of glycoproteins of brain, nerve, and skeletal muscle. Here we isolated a human cDNA for protein O-mannose beta-1,2-N-acetylglucosaminyltransferase (POMGnT1), which participates in O-mannosyl glycan synthesis. We also identified six independent mutations of the POMGnT1 gene in six patients with MEB. Expression of most frequent mutation revealed a great loss of the enzymatic activity. These findings suggest that interference in O-mannosyl glycosylation is a new pathomechanism for muscular dystrophy as well as neuronal migration disorder.

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