POMT1 mutation results in defective glycosylation and loss of laminin-binding activity in α-DG
POMT1 mutation results in defective glycosylation and loss of laminin-binding activity in α-DG
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DOI：
10.1212/01.wnl.0000115386.28769.65
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发表时间：
2004-03-23
期刊：
影响因子：
9.9
通讯作者：
Nishino, I
中科院分区：
文献类型：
--
作者：
Kim, DS;Hayashi, YK;Nishino, I
步行者-瓦尔堡综合征（WWS）是一种先天性肌营养不良症，伴有神经元迁移障碍和眼结构异常。最近在20%的WWS患者中发现了O-甘露糖基转移酶1基因（POMT 1）突变。作者报告了一例WWS患者和一种新的POMT 1突变。他们的患者表达α-肌营养不良蛋白聚糖（α-DG）核心蛋白，但完全糖基化的α-DG抗体表位缺失，与层粘连蛋白结合活性的丧失相关。
Walker - Warburg syndrome (WWS) is a congenital muscular dystrophy associated with neuronal migration disorder and structural eye abnormalities. The mutations in the O-mannosyltransferase 1 gene (POMT1) were identified recently in 20% of patients with WWS. The authors report on a patient with WWS and a novel POMT1 mutation. Their patient expressed alpha-dystroglycan (alpha-DG) core protein, but fully glycosylated alpha-DG antibody epitopes were absent, associated with the loss of laminin-binding activity.